Relevant bibliographies by topics / Proteinaceo

Academic literature on the topic 'Proteinaceo'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Proteinaceo"

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Oppert, B., K. Hartzer, and M. Zuercher. "Digestive proteinases in Lasioderma serricorne (Coleoptera: Anobiidae)." Bulletin of Entomological Research 92, no. 4 (August 2002): 331–36. http://dx.doi.org/10.1079/ber2002179.

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AbstractThe cigarette beetle, Lasioderma serricorne (Fabricius), is a common pest of stored foods. A study of digestive proteinases in L. serricorne was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. Optimal casein hydrolysis by luminal proteinases of L. serricorne was in pH 8.5–9.0 buffers, although the pH of luminal contents was slightly acidic. Results from substrate and inhibitor analyses indicated that the primary digestive proteinases were serine proteinases. The most effective inhibitors of caseinolytic hydrolysis were from soybean (both Bowman Birk and Kunitz), with some inhibition by chymostatin, N-TOSYL-L-phenylalanine chloromethyl ketone, and leupeptin. Casein zymogram analysis identified at least eight proteolytic activities. Activity blot analyses indicated one major proteinase activity that hydrolysed the trypsin substrate N-α-benzoyl-L-arginine ρ-nitroanilide, and three major proteinase activities that hydrolysed the chymotrypsin substrate N-succinyl ala-ala-pro-phe ρ-nitroanilide. The absence of cysteine, aspartic, and metallo proteinases in L. serricorne digestion was evidenced by the lack of activation by thiol reagents, alkaline pH optima, and the results from class-specific proteinase inhibitors. The data suggest that protein digestion in L. serricorne is primarily dependent on trypsin- and chymotrypsin-like proteinases.
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Jankangram, Wichuda, and Sunthorn Chooluck. "In silico Analysis and Characterization of a Putative Aspartic Proteinase Inhibitor, IA3 from Lachancea kluyveri." Trends in Sciences 20, no. 3 (January 19, 2023): 6377. http://dx.doi.org/10.48048/tis.2023.6377.

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Aspartic proteinases play important role in various physiological and biological processes. Understanding catalytic mechanisms of these enzymes could lead to crucial medical and biological applications. Two types of aspartic proteinase inhibitors have been identified i.e. small molecule inhibitor and naturally occurring peptides. Most of aspartic proteinases are highly susceptible to inhibition by a series of small, non-proteinaceous natural products; pepstatin. However, only limited number of naturally-occurring polypeptide inhibitors of aspartic proteinases has so far been discovered. One among these inhibitors is Saccharomyces cerevisiae IA3. The S. cerevisiae Proteinase A (ScPrA) is solely and potently inhibited by this small polypeptide at sub-nanomolar level. It was proven that, not only IA3 has no detectable effect against a wide range of aspartic proteinases, but it was also shown to be cleaved as a substrate of these non-target enzymes. Bioinformatics analysis of the IA3 structure has been undertaken in this study. Database searching for sequence homology from available fungal genome data bank using the Basic Local Alignment Search Tool (BLAST) revealed that 4 structurally related, IA3-like proteins have successfully been identified. The amino acid sequence of IA3-like proteins from Lachancea kluyveri share highest degree of similarity toward wild-type IA3. The Lk-IA3-like gene was synthesized using a PCR-based gene synthesis method. Protein expression in E. coli, protein purification and characterization of Lk-IA3-like by enzyme kinetic assays were performed. The results indicated that Lk-IA3-like protein inhibits ScPrA at the Ki value of 190 ± 0.11 nM and possesses no inhibitory effect toward AfPrA (Aspergillus fumigatus proteinase A) or HuCatD (Human cathepsin D). HIGHLIGHTS Aspartic proteinases enzyme family is crucially involved in various physiological and biological processes including in the pathogenesis of numerous diseases which make them a possible target for drug design Inhibitors of aspartic proteinases are not only applied for human disease treatment but also extended to plant and other economically important animals Aspartic proteinase from cerevisiae (Proteinase A) is solely and potently inhibited by a small peptideinhibitor, IA3 Bioinformatics analysis of the naturally occurring aspartic proteinases inhibitor, IA3 structure has been undertaken in this research and putative IA3-like proteins have successfully been identified IA3-like proteins from Lachancea kluyveri were produced in coli and enzyme inhibition assays revealed that Lk-IA3-like protein inhibits ScPrA at the Ki value of 190 ± 0.11 nM GRAPHICAL ABSTRACT
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Rosenthal, P. J., K. Kim, J. H. McKerrow, and J. H. Leech. "Identification of three stage-specific proteinases of Plasmodium falciparum." Journal of Experimental Medicine 166, no. 3 (September 1, 1987): 816–21. http://dx.doi.org/10.1084/jem.166.3.816.

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We have identified and characterized three stage-specific proteinases of Plasmodium falciparum that are active at neutral pH. We analyzed ring-, trophozoite-, schizont-, and merozoite-stage parasites by gelatin substrate PAGE and characterized the identified proteinases with class-specific proteinase inhibitors. No proteinase activity was detected with rings. Trophozoites had a 28 kD proteinase that was inhibited by inhibitors of cysteine proteinases. Mature schizonts had a 35-40 kD proteinase that also was inhibited by cysteine proteinase inhibitors. Merozoite fractions had a 75 kD proteinase that was inhibited by serine proteinase inhibitors. The stage-specific activity of these proteinases and the correlation between the effects of proteinase inhibitors on the isolated enzymes with the effects of the inhibitors on whole parasites suggest potential critical functions for these proteinases in the life cycle of malaria parasites.
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Sever, Natasa, Metka Filipic, Joze Brzin, and Tamara T. Lah. "Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro." Biological Chemistry 383, no. 5 (May 15, 2002): 839–42. http://dx.doi.org/10.1515/bc.2002.088.

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Abstract Various types of proteinases are implicated in the malignant progression of human and animal tumors. Proteinase inhibitors may therefore be useful as therapeutic agents in antiinvasive and antimetastatic treatment. The aims of this study were (1) to estimate the relative importance of proteinases in B16 cell invasion in vitro using synthetic, classspecific proteinase inhibitors and (2) to assess the inhibitory effect of some naturally occurring cysteine proteinase inhibitors. Serine proteinase inhibitor reduced invasiveness by up to 24%, whereas inhibition of aspartic proteinases reduced invasion by 11%. Synthetic inhibitors of cysteine proteinases markedly impaired invasion: cathepsin B inhibitors, particularly Ca 074Me, inhibited invasion from 20 40%, whereas cathepsin L inhibitor Clik 148 reduced invasion by 11%. The potato cysteine proteinase inhibitor PCPI 8.7 inhibited invasion by 21%, whereas another potato inhibitor, PCPI 6.6, and the mushroom cysteine proteinase inhibitor clitocypin had no effects. As the inhibitors that inhibited cathepsin B were in general more efficient at impairing the invasiveness, we conclude that of the two cysteine proteinases, cathepsin B plays a more important role than cathepsin L in murine melanoma cell invasion.
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Garciacarreno, F. L., L. E. Dimes, and N. F. Haard. "Substrate-Gel Electrophoresis for Composition and Molecular Weight of Proteinases or Proteinaceous Proteinase Inhibitors." Analytical Biochemistry 214, no. 1 (October 1993): 65–69. http://dx.doi.org/10.1006/abio.1993.1457.

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Hiemstra, P. S. "Novel roles of protease inhibitors in infection and inflammation." Biochemical Society Transactions 30, no. 2 (April 1, 2002): 116–20. http://dx.doi.org/10.1042/bst0300116.

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The local balance between proteinase inhibitors and proteinases determines local proteolytic activity. Various studies have demonstrated the importance of serine proteinase inhibitors in regulating the activity of serine proteinases that are released by leucocytes during inflammation. Recently it has been shown that these inhibitors may also display functions that are distinct from those associated with the inhibition of leucocyte-derived proteinases. In this review the results of selected studies focusing on three inhibitors of neutrophil elastase, i.e. α1-proteinase inhibitor, secretory leucocyte proteinase inhibitor and elafin, are presented, with the aim of illustrating their possible involvement in the regulation of inflammation, host defence against infection, tissue repair and extracellular matrix synthesis.
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Ikeda, T. "Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187." Journal of Helminthology 77, no. 1 (March 2003): 21–26. http://dx.doi.org/10.1079/joh2002144.

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AbstractThe involvement of intrinsic proteinases in the excystment of Paragonimus ohirai metacercariae was studied in in vitro excystment induced by sodium (Na) cholate, a bile salt and A23187, a Ca2+ ionophore. The effects of various proteinase inhibitors on the in vitro excystment were examined and similar inhibitory profiles were obtained. Benzyloxycarbonyl-L-leucyl-L-leucinal (Z-Leu-Leu-H), a cysteine proteinase inhibitor and 4-(2-aminoethyl)-benzenesulfonyl fluoride (Pefabloc SC), a serine proteinase inhibitor completely inhibited excystment, while L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido (4-guanidino)-butane (E-64), a cysteine proteinase inhibitor and leupeptin, a cysteine/serine proteinase inhibitor permitted partial excystment at a lower rate, but inhibited it from proceeding from the partial excystment stage. In secretions released from metacercariae during excystment, proteinase activities detected towards various fluorogenic peptidyl substrates were almost completely inhibited by Z-Leu-Leu-H and E-64, but not by Pefabloc SC. Sodium cholate induced a higher secretion of cysteine proteinases and a higher rate of excystment than A23187. Profiles of cysteine proteinase activities towards five peptidyl substrates detected were markedly different among the two secretions and the lysate of newly excysted juveniles. Newly excysted juveniles released cysteine proteinases with similar activity profiles and levels to metacercariae induced by Na cholate-incubation, whereas the release of cysteine proteinases was reduced compared with metacercariae induced by A23187-incubation. These results provide valuable information about the involvement of intrinsic proteinases in metacercarial excystment.
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Bózner, P., and P. Demeš. "Proteinases inTrichomonas vaginalisandTritrichomonas mobilensisare not exclusively of cysteine type." Parasitology 102, no. 1 (February 1991): 113–15. http://dx.doi.org/10.1017/s0031182000060418.

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SUMMARYHigh molecular weight proteinases ofTrichomonas vaginalis(with apparentMrvalues 142 and > 220 kDa) andTritrichomonas mobilensis(Mr67, 86, 104 and 120 kDa), optimally active at pH 8, were analysed in gelatin-containing polyacrylamide gels. All of these proteinases were resistant to serine-, aspartic- as well as cysteine proteinase inhibitors. Both proteolytic bands inT. vaginalisand two proteinases inT. mobilensis(67 and 104 kDa) were inhibited by EDTA and EGTA suggesting that they belong to the metallo-proteinase class. The 67 kDa proteinase ofT. mobilensiswas inhibited also byo-phenanthroline. The other two bands ofT. mobilensis(86, 120 kDa) were not classified to any proteinase group since they appeared to be resistant to the chelating agents tested in this study.
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Jakobs, K. H., and K. Aktories. "Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets." Biochemical Journal 249, no. 3 (February 1, 1988): 639–43. http://dx.doi.org/10.1042/bj2490639.

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The influence of various proteinases on GTP hydrolysis was studied in membranes of human platelets. Of the proteinases examined, trypsin, acrosin and a recently described trypsin-like proteinase from bovine sperm, but not chymotrypsin, increased GTP hydrolysis. Similar to what was described previously for hormone-like agents, the stimulation of GTP hydrolysis by the proteinases was only observed at low GTP concentrations, with apparent Km values of 0.2-0.3 microM-GTP. Stimulation of the high-affinity GTPase by the proteinases occurred without apparent lag phase and was constant over a long period of incubation. The proteinase inhibitors leupeptin and soya-bean trypsin inhibitor blocked the stimulation of GTP hydrolysis, but did not reverse the effect of the proteinases. Treatment of platelet membranes with N-ethylmaleimide, which eliminates Gi-protein (inhibitory guanine-nucleotide-binding protein)-related GTPase stimulation by adrenaline, decreased stimulation of GTP hydrolysis by the proteinases only partially. Activation of GTP hydrolysis by the proteinases was partially additive with that caused by adrenaline, whereas thrombin stimulation was not increased further. The data indicate that, similarly to the proteinase thrombin, trypsin and trypsin-like proteinases can activate GTP-hydrolysing protein(s) that exhibit high affinity for GTP in platelet membranes. It is suggested that the proteinases interact in platelet membranes with a receptor site similar to that used by thrombin and that the observed GTPase stimulation is a reflection of a proteinase-receptor interaction with a guanine-nucleotide-binding regulatory protein.
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Dubin, A., J. Potempa, and J. Travis. "Structural and functional characterization of elastases from horse neutrophils." Biochemical Journal 300, no. 2 (June 1, 1994): 401–6. http://dx.doi.org/10.1042/bj3000401.

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In order better to understand the pathophysiology of the equine form of emphysema, two elastinolytic enzymes from horse neutrophils, referred to as proteinases 2A and 2B, have been extensively characterized and compared with the human neutrophil proteinases, proteinase-3 and elastase. Specificity studies using both the oxidized insulin B-chain and synthetic peptides revealed that cleavage of peptide bonds with P1 alanine or valine residues was preferred. Further characterization of the two horse elastases by N-terminal sequence and reactive-site analyses indicated that proteinases 2A and 2B have considerable sequence similarity to each other, to proteinase-3 from human neutrophils (proteinase 2A), to human neutrophil elastase (proteinase 2B) and to a lesser extent to pig pancreatic elastase. Horse and human elastases differed somewhat in their interaction with some natural protein proteinase inhibitors. For example, in contrast with its action on human neutrophil elastase, aprotinin did not inhibit either of the horse proteinases. However, the Val15, alpha-aminobutyric acid-15 (Abu15), alpha-aminovaleric acid-15 (Nva15) and Ala15 reactive-site variants of aprotinin were good inhibitors of proteinase 2B (Ki < 10(-9) M) but only weak inhibitors of proteinase 2A (Ki > 10(-7) M). In summary, despite these differences, the horse neutrophil elastases were found to resemble closely their human counterparts, thus implicating them in the pathological degradation of connective tissue in chronic lung diseases in the equine species.
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Dissertations / Theses on the topic "Proteinaceo"

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ZEYNALI, AMIRBAHADOR. "Two-photon assisted direct laser writing of proteinaceous microarchitectures containing plasmonic nanoparticles; characterization and optimization." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/304319.

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Le nanoparticelle metalliche, grazie alle loro affascinanti proprietà ottiche ed elettrochimiche, attirano l'attenzione di diverse discipline scientifiche e di ricerca ingegneristica. Tra queste proprietà, l'effetto fototermico indotto dalle risonanze plasmoniche, è una caratteristica notevole ed esclusiva delle nanoparticelle di metalli nobili che, ad oggi, vengono già sfruttate per vari scopi, sia per ricerca che, soprattutto, per applicazioni biomediche. Il fenomeno della risonanza plasmonica superficiale, caratterizzato da bande ben definite, fornisce a queste nanoparticelle una notevole la flessibilità nella risposta ottica che si può vantaggiosamente trasferire a matrici polimeriche in cui queste vengano disperse. In particolare, la possibilità di indurre un aumento di temperatura altamente localizzato che può essere attivato tramite un dispositivo di stimolazione esterno come una sorgente di luce, renderebbe tali matrici strumenti preziosi nel campo dei trattamenti cellulari e, in generale, dell'ingegneria dei tessuti In questa tesi, la tecnica di scrittura (photo-cross-link) laser diretta (DLW), attivata da assorbimento a due fotoni, è stata impiegata per fabbricare micro-architetture con il diverso modulo elastico (da 80kPa a 800kPa) a partire da un inchiostro proteico composto da albumina di siero bovino (BSA), un foto-iniziatore (Rose Bengale o blu di metilene) e nanoparticelle d'oro a simmetria non sferica (GNP). Mostriamo qui che la presenza di queste ultime, se opportunamente schermate dall’interazione con il foto-iniziatore, fornisce alle microstrutture foto-polimerizzate la capacità di generare un aumento della temperatura locale mediante stimolazione nella regione spettrale del vicino infrarosso. L'efficienza fototermica misurata sotto l’effetto di radiazione laser focalizzata a 800 nm (in continua) su microstrutture caricate con una bassa concentrazione di atomi d'oro (1% w/w) ha raggiunto 12.2 pm 0.4 C/W, che costituisce un record di effetto fototermico indotto su una microstruttura a base proteica proteinica stampata tramite DLW. La funzionalità foto-termica derivante dalle GNP incorporate nelle microstrutture proteiche fabbricate riveste una notevole potenzialità nello studio delle risposte di sistemi viventi, come cellule e colture di batteri, al rilascio di calore altamente localizzato e controllato sia per quanto riguarda il tempo di irraggiamento che la dose rilasciata.
Metallic nanoparticles, due to their fascinating optical and electrochemical properties, attract the attention of different science and engineering research disciplines. Among these properties, the plasmonic photothermal effect is a notable and exclusive feature of noble-metal nanoparticles that, by today, are exploited through lots of research activities for various purposes, especially for biomedical applications. This optically-tunable phenomenon uniquely increases the flexibility of the optical response of host matrices, by allowing to induce highly localized temperature increases that can be triggered via simple external stimulation device like a light source. Such matrices can be valuable tools in the field of cell treatments and, in general, tissue engineering. In the present study, the two-photon-assisted direct laser writing (DLW) technique was employed to fabricate microarchitectures with the different elastic modulus (80kPa to 800kPa) from a proteinaceous ink composed of bovine serum albumin (BSA), rose Bengal (RB), or methylene blue (MB), and non-spherical symmetric gold nanoparticles (GNPs), with the ability to generate local temperature increase by stimulation in the near-infrared spectral region. The recorded photothermal efficiency measured using focused continuous wave (CW) laser irradiation at 800nm on microstructures loaded with GNPs at low gold atom concentration (1%w/w) reached 12.2 pm 0.4 C/W, that is a record photothermal effect induced from a printed proteinaceous feature. This photo-thermal functionality arising from the GNPs embedded within the fabricated proteinaceous microstructures can then be applied for studying responses of living systems like cells and bacteria cultures under an externally triggered highly localized heat release.
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Turk, Boris. "Papain-like cysteine proteinases : regulation by proteinase inhibitors and pH /." Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 1996. http://epsilon.slu.se/avh/1996/91-576-5227-9.gif.

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Zhang, Xiaorong. "The roles of proteinases and proteinase inhibitors in plant-nematode interactions." Diss., Virginia Tech, 1994. http://hdl.handle.net/10919/37260.

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Bridges, Sylvia Shadinger. "Design, synthesis, and evaluation of cysteine protease inhibitors." Diss., Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/29738.

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Proteases are enzymes that cleave protein amide bonds. Proteases are involved in a myriad of biological processes and are considered good targets for drug design. The proteases described herein are cysteine proteases, which utilize a cysteine residue thiol to attack the amide carbonyl, leading to amide bond cleavage. Irreversible inhibitors of cysteine proteases react with the active site cysteine, forming a covalent bond and rendering the enzyme inactive. The first project involved the design and synthesis of aza-peptide epoxide inhibitors for calpain, a clan CA, ubiquitous, calcium-activated human enzyme involved in neurodegeneration. These inhibitors proved to be poor inactivators of calpain, demonstrating that the aza-peptide epoxide is a warhead specific to clan CD cysteine proteases (caspases, gingipains). Subsequently, a known epoxide inhibitor of calpain was optimized to create a more potent inhibitor. Several of these inhibitors were more potent than the parent, and all were demonstrated to inhibit calpain in a breast cancer cell line which was treated with paclitaxel to spike calpain activity. The second project involved the design and solid phase synthesis of aza-peptide Michael acceptor caspases inhibitors. The two goals of this project were to develop a solid phase method for synthesis of inhibitors that are tedious to synthesize in solution phase, and to use a variety of amino acid residues to determine the optimal interactions in the P3? position for various caspases. The synthesis was successful, and the optimal P3? residues were determined. The third project involved the kinetic evaluation of aza-peptide epoxide and Michael acceptor inhibitor designed for the gingipains. Gingipains K and R are virulence factors in the pathology of Porphyromonas gingivalis involved in gingivitis and periodontal disease. These inhibitors proved to be extremely potent inactivators of gingipains, with some of the highest rates of inhibition measured in the Powers laboratory. Gingipain K preferred larger, aromatic moieties in the P1? position, while gingipain R preferred the Michael acceptor inhibitors, with the P1? substituent having less of an impact on potency.
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Souza, Thais Paula de. "Efeito dos inibidores de proteinase de soja no padrão de expressão de proteinases de Spodoptera frugiperda." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-05112013-150120/.

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Dentre as substâncias químicas secretadas pelas plantas, contra os insetos herbívoros, os inibidores de peptidases são de grande interesse. A atenção dada a esses inibidores deve-se ao fato, de eles serem uma boa alternativa no controle de insetos praga, uma vez que não causam danos ao meio ambiente. Contudo, muitas espécies de insetos são capazes de escapar dos efeitos negativos dos inibidores de peptidases das plantas, via diferentes mecanismos adaptativos. Devido a esse fato, é importante compreender os mecanismos desenvolvidos pelos insetos para burlar os efeitos dos inibidores de peptidases das plantas. Diante desse panorama, este trabalho teve como objetivo estudar o mecanismo adaptativo das serina endopeptidases de Spodoptera frugiperda aos inibidores de endopeptidases de soja. Foram realizadas análises do transcriptoma dos intestinos das lagartas mantidas em exposição crônica ao inibidor. Para averiguar os efeitos causados devido à exposição crônica ao inibidor, foram realizadas comparações da expressão relativa, dos genes de tripsinas e quimotripsinas, de intestinos de lagartas de sexto instar. Contudo, para entender o efeito da exposição aguda ao inibidor, lagartas de S. frugiperda foram criadas em dieta artificial controle até o primeiro dia do sexto instar, após esse período elas foram transferidas para dieta artificial acrescida com 0,5 % dos inibidores de endopeptidases de soja, durante 48 horas. Para verificar a ocorrência de um possível controle epigenético na expressão dos genes, as lagartas foram conduzidas até a fase adulta e os adultos, de cada tratamento, foram acasalados entre si, constituindo uma segunda geração. Dados de expressão relativa foram obtidos, de indivíduos da primeira e segunda geração, e foram então comparados. Foram identificados 14 possíveis genes de quimotripsinas e nove possíveis genes de tripsinas. Os genes de tripsina foram divididos em dois grupos distintos em relação a sua sensibilidade aos inibidores de endopepetidases de soja e expressão relativa. Houve uma resposta diferenciada na ativação dos genes de serina endopeptidases de S. frugiperda, a qual dividiu os genes em dois grupos, os responsivos e os não responsivos ao inibidor. A exposição aguda ao inibidor ativou um pequeno grupo de genes, enquanto que a exposição crônica promoveu uma maior amplitude de expressão gênica, sugerindo mecanismos temporalmente regulados. Por último, evidências indicam, pela primeira vez, a possível ocorrência de um mecanismo epigenético, na resposta das enzimas digestivas aos inibidores de serina endopeptidases de soja.
Among the chemicals secreted by plants against insect herbivores, peptidase inhibitors (PIs) are of great interest. The attention given to PIs is due to the fact that they are a good alternative to control insect pests since they do not cause damage to human health and the environment. However, many species of insects are able to escape the negative effects of PIs plants via different adaptive mechanisms. Because of this, it is important to understand the mechanisms developed by insects to circumvent the effects of PIs plants. Against this background, this research aimed to study the adaptive mechanism of serine endopeptidases Spodoptera frugiperda to soybean endopeptidase inhibitors. For this purpose, larvae of S. frugiperda were reared on artificial diet and control artificial diet plus 0.5% of endopeptidase inhibitors of soybean. We conducted a transcriptome midgut of worms maintained in chronic ingestion of the inhibitor. The relative expression of the genes, trypsin and chymotrypsin, was also compared the midgut of sixth instar larvae kept in these diets. In another experiment, the larvae were conducted to moth, then the treatments were mated forming a second generation. Relative expression data were obtained for individuals of the first and second generation, and then compared. Identified 14 genes with potential of chymotrypsin and 9 trypsin like genes. The trypsin gene were divided into two groups for both their sensitivity to PI soybean endopeptidase, and for their relative expression pattern. There was a differentiated response on the genes activation of S. frugiperda serina endopeptidases. The genes were clustered in 2 groups, the responsive ones and the non responsive to the inhibitor. The acute exposition to the inhibitor activated a small group of genes and the chronic exposition affected several genes, indicating the existence of temporal regulated mechanism. Besides, there is a possible occurance of an epigenetic mechanism, which is related to the digestive serina endopeptidases inhibitors of soybean.
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Nadalini, Larissa Cristina Deppmann. "Caracterização do mecanismo adaptativo de Spodoptera frugiperda aos inibidores de proteinase de plantas." Universidade de São Paulo, 2007. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-07022008-151221/.

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A existência de uma família gênica diversa de serino proteinases em Lepidóptera sugere que essas proteinases desempenham um papel importante na adaptação desses insetos à presença de inibidores de proteinases vegetais. Essas enzimas têm se revelado estarem envolvidas no processo digestivo de larvas de insetos. Larvas de Spodoptera frugiperda foram alimentadas com uma dieta suplementada com inibidor de proteinase de soja (IPS) e a expressão gênica de proteinases intestinais foi avaliada através de PCR em tempo real. Análises de transcrição anteriores mostraram a existência de dois grupos de serino proteinases: um grupo de genes constitutivamente expressos em larvas controle que é induzido pela dieta contendo IPS e um segundo grupo que está ausente no controle, mas que é também induzido por uma dieta rica em IPS. No presente trabalho foi observado um terceiro grupo de proteinases que não são nem induzidas nem reprimidas pela presença do IPS na dieta. Essa observação sugere que a adaptação de S. frugiperda ao IPS envolve a síntese de novas proteinases, a indução de enzimas preexistentes e ainda um terceiro grupo insensível à presença dos inibidores. Proteinases dos intestinos de larvas crescidas em dieta com IPS mostraram insensibilidade ao inibidor. As proteinases também foram insensíveis quando a atividade foi verificada com um inibidor de proteinases de amplo espectrum. Os resultados aqui apresentados propõem que a adaptação de S. frugiperda ao IPS segue uma estratégia generalizada, baseada na indução geral de um grande grupo de endoproteinases.
The existence of a diverse serine proteinase gene family in lepidopteran insects has suggested its significant role in the insect adaptation to plant proteinase inhibitors. These enzymes have been shown to be involved in the proteolytic digestion process of insect larvae. Spodoptera frugiperda larvae were fed on a diet supplemented with soybean proteinase inhibitor (SPI) and the gene expression of intestinal proteinases was evaluated by real time PCR. Previous transcription analyses found two groups of intestinal serine proteinases: one group of genes constitutively expressed in the control larvae that is induced by the SPI-containing diet during the experiment, and a second group that is absent in the control but also induced by the SPI rich diet. Herein was observed a third group of proteinases that are neither induced nor repressed by the presence of SPI in the diet. This observation suggests that adaptation of S. frugiperda to SPI involves de novo synthesis, up regulation of existing enzymes and that there is a third group insensitive to the presence of the inhibitors. Proteinases from intestines of larvae reared on a diet with SPI showed insensitivity to the inhibitor. The proteinases were also insensitive when the activity was checked with a broad-spectrum potato proteinase inhibitor. The results here presented propose that adaptation of S. frugiperda to SPI follows a \"shotgun\" approach, based on a general up regulation of a large set of endoproteinases.
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Estrada, Sergio. "Cystatin A, a mammalian cysteine proteinase inhibitor : mechanism of inhibition of target proteinases by recombinant cystatin A variants /." Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 1998. http://epsilon.slu.se/avh/1998/91-576-5448-4.gif.

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Souza, Diego Pereira de. "ProteÃnas inibidoras de fitopatÃgenos em fluidos laticÃferos: atividade e mecanismo de aÃÃo." Universidade Federal do CearÃ, 2010. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=7887.

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CoordenaÃÃo de AperfeiÃoamento de Pessoal de NÃvel Superior
Um relevante nÃmero de espÃcies vegetais à descrito como plantas produtoras de um fluido leitoso comumente denominado de lÃtex. Nestas espÃcies, o lÃtex à sintetizado e armazenado sob pressÃo em um sistema de canais formados por cÃlulas altamente especializadas denominadas de laticÃferas, em cujos citoplasmas estÃo presentes todas as estruturas eucariontes em meio à Ãgua, borracha e inÃmeras molÃculas, muitas das quais especÃficas deste conteÃdo. Muitos estudos tÃm sugerido que molÃculas produzidas nestes fluidos participam da defesa vegetal. Neste trabalho, o lÃtex de 5 espÃcies foi coletado e processado em laboratÃrio para obtenÃÃo de suas fraÃÃes protÃicas e estas foram avaliadas quanto a atividade sobre fungos fitopatogÃnicos atravÃs de ensaios de inibiÃÃo da germinaÃÃo de esporos e crescimento de hifas. ProteÃnas do lÃtex de C. procera (PLCp), Cryptostegia grandiflora (PLCg) e Carica candamarcensis (P1 G10) apresentaram atividade antifÃngica enquanto que Plumeria rubra (PLPr) e Euphorbia tirucalli (PLEt) nÃo apresentaram atividade sobre qualquer dos fungos avaliados (Colletotrichum gloeosporioides, Fusarium oxysporum, Fusarium solani, Rhizoctonia solani, Neurospora sp. e Aspergillus niger). A atividade inibitÃria das fraÃÃes protÃicas se correlacionou diretamente com a presenÃa de atividade proteolÃtica do tipo cisteÃnica presente nas amostras de PLCp, PLCg e P1G10. A atividade antifÃngica foi aumentada na presenÃa de DTT, um ativador destas proteases e foi diminuÃda ou eliminada quanto Ãs amostras foram prÃ-tratadas com iodoacetamida (IAA), um inibidor especÃfico de proteases cisteÃnicas. AlÃm disso, a atividade antifÃngica foi observada quando papaÃna, uma protease cisteÃnica purificada do lÃtex de Carica papaya foi avaliada, mas tripsina e quimotripsina, duas proteases serÃnicas nÃo apresentaram atividade. AtravÃs de cromatografia em coluna de Mono-S Sepharose acoplada ao sistema de FPLC, uma protease cisteÃnica foi isolada de PLCg. A proteÃna purificada (Cg24-I) apresentou massa molecular de 24,118 KDa. A Cg24-I apresentou atividade proteolÃtica mÃxima em pH 8,0 e foi inibida por IAA e E-64, utilizando azocaseÃna e BANA como substratos, respectivamente. Cg24-I inibiu a germinaÃÃo de F. solani e foi capaz de alterar a permeabilidade das membranas dos esporos na concentraÃÃo de 90 ng/ml. Esse conjunto de resultados sugere que proteinases cisteÃnicas de fluidos laticÃferos participam da defesa das plantas contra fungos fitopatogÃnicos e que o provÃvel mecanismo de aÃÃo destas proteÃnas seja a alteraÃÃo da permeabilidade da membrana plasmÃtica destes microrganismos. A descriÃÃo de atividade antifÃngica de proteases cisteÃnicas oriundas de fluidos laticÃferos nÃo à ainda descrita em detalhes na literatura, sendo este um trabalho com carÃter original.
Canal systems containing secretions, such as latex, are widely disseminated in the plant kingdom. These fluids are chemically complex and exhibit intense metabolism. Despite their origin, latex is the cytoplasm of specialized cells growing intrusively into organized tissues and organs, forming an interconnected network allowing latex exudation immediately after tissue damage. Insecticidal effects of latex proteins have been described, however minor studies were devoted to investigate antifungal activities in latex. In this study proteins extracted from latex of Calotropis procera (Ait.) R.Br (PLCp), Plumeria rubra L.(PLPr), Carica candamarcensis Hook F.(P1 G10), Cryptostegia grandiflora (PLCg), and Euphorbia tirucalli L. (PLEt) were tested for antifungal activity against six phytopathogens (Fusarium solani, F. oxysporium, Aspergilus niger, Rhizoctonia solani, Neurospora sp. and Colletrotricum gloerosporioides). PLCp, PLCg and P1G10 exhibited antifungal activity and PLPr and PLEt were not efetive. Inhibitory activity of the protein fractions correlated with the cysteine-type proteolytic activity found in these fractions. The endogenous proteolytic activity and inhibitory activity on fungal growth were both increased when samples were first activated with DTT, a cysteine proteinase activator. Conversely, pre-treatment of samples with iodoacetamide, an inhibitor of these proteases rendered all samples deficient of both, proteolytic and antifungal activities. Antifungal of activity of cysteine proteinases of latex origin was also confirmed when papain, obtained from latex of Caryca papaya was tested while purified trypsin and chemotrysin, two serine-type proteases were not antifungal. A cysteine proteinase was thus, purified form PLCg by ion exchange chromatography on a Mono-S Sepharose matrix monitored by a FPLC system. The protein, named Cg24-I exhibited molecular mass of 26.118 KDa determined by MALDI spectrometry; maximum of proteolysis at pH 8.0 and inhibited by iodoacetamide and E-64 when assayed with azocazein or BANA as substrates. Cg24-I inhibited germination of F. solani and altered membrane permeability of spores at a minimum concentration of 90 ng/ml. Results present here suggest that cysteine proteinases of laticifer fluids are proteins with antifungal activity capable of damaging spore structure and inhibiting hyphae growth. Reports of antifungal activity of latex proteases are still scarce in literature and this work appears as an important contribution to this field. Furthermore, this work gives important evidence for the multiple defensive role of latex in plants.
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Macgregor, James Mylne. "Alimentary tract proteinases of the Southern corn rootworm (Diabrotica undecimpunctata howardi) and the potential of potato Kunitz proteinase inhibitors for larval control." Thesis, Durham University, 2001. http://etheses.dur.ac.uk/3808/.

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Proteolytic digestion by larval Diabrotica undecimpunctata howardi (Barber) (D.undecimpunctata) has been investigated with the aim of producing transgenic plants possessing enhanced resistance to this economically important crop pest. Biochemical characterisation in vitro by pH dependent hydrolysis and inhibition assays incorporating E-64, pepstatin A and soybean Kunitz trypsin inhibitor showed the majority of hydrolytic activity occurs at pH 5.5 and is performed by cysteine and aspartic endopeptidases. Cysteine and aspartic proteinase encoding clones were isolated from a larval alimentary tract cDNA library. Four cathepsin L-like cysteine proteinases and two cathepsin D-like aspartic proteinase cDNA clones were identified by codmg homology to known proteinase sequences. Analysis of primary and secondary sequence features revealed D. undecimpunctata aspartic proteinase 1 exhibits features associated with cathepsins E and is proposed to be a D. undecimpunctata cathepsm E-like aspartic proteinase.Cathepsin D-like aspartic proteinase inhibitors of the potato Kunitz protemase inhibitor (PKPI) family have been isolated by PCR and expressed employing the pET expression system (Novagen). In vitro assays demonstrated the inhibitory activity of PKPI-A and PKPl-B inhibitors against larval D. undecimpunctata alimentary tract proteolytic enzymes. To the authors knowledge this work represents the first reporting of the expression and purification of biologically active PKPI proteins. In vitro assays incorporating oryzacystatin I and PKPI proteins resulted in increased inhibition of proteolytic activity compared to single inhibitor and uninhibited control reactions. Inhibition assays provide evidence for the potential of a dual protemase inhibitor strategy to arrest protein hydrolysis by larval D. undecimpunctata, preventing essential amino acid absorption. Further research is necessary to characterise the properties of the digestive enzymes isolated in this work and the inhibitory spectrum of PKPI proteins. Transgenic crops expressing a combination of oryzacystatin and PKPI proteins would be predicted to show enhanced resistance to insect herbivores by virtue of digestive proteolysis inhibition.
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Mistry, Rohit. "Development of a sheep model to investigate the role of neutrophil proteinases and their endogenous inhibitors in acute lung injury : a novel proteinase inhibitor." Thesis, Imperial College London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.308934.

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Books on the topic "Proteinaceo"

1

Fusek, Martin. Aspartic proteinases: Physiology and pathology. Boca Raton, Fla: CRC Press, 1995.

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Turk, Boris. Papain-like cysteine proteinases: Regulation by proteinase inhibitors and pH. Uppsala: SverigesLantbruksuniversitet, 1996.

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Estrada, Sergio. Cystatin A, a mammalian cysteine proteinase inhibitor: Mechanism of inhibition of target proteinases by recombinant cystatin A variants. Uppsala: Sveriges Lantbruksuniversitet, 1998.

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Kirschke, Heidrun. Proteinases 1: lysosomal cysteine proteinases. London: Academic Press, 1995.

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Caspases, paracaspases, and metacaspases: Methods and protocols. New York: Humana, 2014.

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G, James Michael N., and International Conference on Aspartic Proteinases (7th : 1996 : Banff, Alta.), eds. Aspartic proteinases: Retroviral and cellular enzymes. New York: Plenum Press, 1998.

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Takahashi, Kenji, ed. Aspartic Proteinases. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6.

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James, Michael N. G., ed. Aspartic Proteinases. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5373-1.

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J, Barrett Alan, and Salvesen G, eds. Proteinase inhibitors. Amsterdam: Elsevier, 1986.

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Philippe, Taupin, ed. The cystatin superfamily of proteinase inhibitors. New York: Nova Science Publishers, 2007.

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Book chapters on the topic "Proteinaceo"

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diZerega, Gere S., and Kathleen E. Rodgers. "Proteinases and Proteinase Inhibitors." In The Peritoneum, 231–73. New York, NY: Springer New York, 1992. http://dx.doi.org/10.1007/978-1-4613-9235-4_8.

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Bode, Wolfram, and Robert Huber. "Natural protein proteinase inhibitors and their interaction with proteinases." In EJB Reviews, 43–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78046-2_5.

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Owen, Caroline A., and Edward J. Campbell. "Proteinases." In ARDS Acute Respiratory Distress in Adults, 139–65. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-3430-7_10.

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Jochum, M., W. Machleidt, H. Neuhof, and H. Fritz. "Proteinases." In Pathophysiology of Shock, Sepsis, and Organ Failure, 46–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-76736-4_5.

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Stockley, R. A., and D. Burnett. "Proteinases and Proteinase Inhibitors in the Pathogenesis of Pulmonary Emphysema in Humans." In Biochemistry of Pulmonary Emphysema, 47–69. London: Springer London, 1992. http://dx.doi.org/10.1007/978-1-4471-3771-9_5.

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Dunn, Ben M., Paula E. Scarborough, W. Todd Lowther, and Chetana Rao-Naik. "Comparison of the Active Site Specificity of the Aspartic Proteinases Based on a Systematic Series of Peptide Substrates." In Aspartic Proteinases, 1–9. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_1.

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Rao, Chetana, and Ben M. Dunn. "Evidence for Electrostatic Interactions in the S2 Subsite of Porcine Pepsin." In Aspartic Proteinases, 91–94. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_10.

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Dhanaraj, Raj R. V., Jim E. Pitts, Phil Nugent, Poonsook Orprayoon, Jon B. Cooper, Tom L. Blundell, Janna Uusitalo, and Merja Penttilä. "Protein Engineering of Surface Loops: Preliminary X-Ray Analysis of the Chy155–165rhi Mutant." In Aspartic Proteinases, 95–99. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_11.

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Szecsi, Pal Bela, and Hans Lilja. "Seminal Progastricsin." In Aspartic Proteinases, 101–5. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_12.

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Ichinose, Masao, Shinko Tsukada, Kazumasa Miki, Nobuyuki Kakei, Masashi Matsushima, Naohisa Yahagi, Satoshi Ishihama, et al. "Effects of Hydrocortisone on the Pepsinogen-Producing Cells in Rat Stomach Mucosa." In Aspartic Proteinases, 107–13. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_13.

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Conference papers on the topic "Proteinaceo"

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Jackson, Craig M. "A DEFINITION OF HEPARIN ANTICOAGULANT POTENCY APPLICABLE TO ALL HEPARINS AND HEPARIN-LIKE SUBSTANCES AND ITS PRACTICAL APPLICATION IN ASSAYING HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642928.

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Heparins increase the rate of inactivation of proteinases by antithrombin without being consumed in the inactivation reaction. The anticoagulant activity of any heparin or heparin preparation is thus determined by the increase in the inactivaton rate which it produces. This rate increase is dependent on the concentration of the heparin in the sample and on some now well known structural properties of the individual heparin molecules that produce high affinity for antithrombin . All proteinases are not inactivated by antithrombin equally rapidly in the absence of heparin, nor are heparins and heparin derivatives of different molecular weight equally effective in the inactivation of the same proteinase. Under appropriate conditions, the observed rate constant (kObs) for the heparin catalyzed proteinase inactivation reaction is simply related to the intrinsic potencies and concentrations of the individual high affinity heparin molecules in the sample. The intrinsic potency of a high affinity heparin molecule is the efficiency with which it catalyzes the inactivation of the particular proteinase, e.g. Factor Xa or thrombin, i.e., it is a second order rate constant, (designated k*) . After k* has been determined from kobs for a known heparin or heparin preparation and a particular proteinase, the concentration of heparin in an unknown sample can be calculated from the equation[H] = [HAT] = kobs/k* In general terms, the appropriate conditions, i.e.,the antithrombin and proteinase concentrations, the pH, and ionic strength, required for this equation to be used are those conditions for which all of the high affinity heparin is bound to the antithrombin and pseudo first order kinetic behavior occurs. At very low heparin concentrations, a correction for the inactivation of the proteinase by antithrombin alone is necessary, but is easily made.Supported by Organon Teknika Corporation and an Established Investigator Award from the American National Red Cross
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Larsson, L. J., E. P. Frisch, and I. Bjoörk. "PROPERTIES OF THE COMPLEX BETWEEN ou-MACROGLOBULIN AND THE PROTEINASE BRINASE FROM ASPERGILLUS ORYZAE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643039.

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Brinase, a proteinase from Aspergillus oryzae, has previously been shown to have a significant thrombolytic effect in patients suffering from peripheral arterial disease. Brinase is rapidly bound to α1-proteinase inhibitor and α2-macroglobulin (α2M) in plasma. Since binding of a proteinase to α2 M only results in ste-rical blockingof the active siteand not complete inactivation of the enzyme, it has been suggested that brinase in complex with α2M may retain ability to digest fibrin.To test this hypothesis, we have characterized the binding of brinase to α2M and the properties of the complex formed. Analyses by several techniques showed that one molecule of α2M can maximally bind twomolecules of brinase. The bait region and the thioester bonds of α2M were cleaved in this reaction in a similar manner as in the reactionwith trypsin. Moreover, a conformational change highly similar to that-caused by trypsin was induced in oα2M by brinase, as shown by changes of fluorescence emission, far-u.v. circular dichroism and u.v. absorption difference spectra. Thus, brinase appears to bind to α2M in the same manner as other proteinases. The activities of free brinase and two forms of brinase-α2M complex, produced by reaction of thetwo components in an equimolar ratio or by saturation of inhibitor with enzyme, were compared by two different assays with high-molecular-weight substrates, i.e. hide powder azure or fibrin. The complex formed with equimolar amounts of brinase and α2M showed ∼15% of the activity of free brinase in both assays, whereas the complex formed at saturation of inhibitor with enzyme showed ∼35% of the free brinase activity. Although the brinase-α2M complex, like other α2M proteinase complexes, is eliminated rapidly from plasma, the anility of the complex to cleave high-molecular-weight substrates may be an explanation of the thrombolytic effect of brinase seen in patients.
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Gibson, Stacy G., Koichiro Mihara, Andries Zijlstra, Matthew E. Hyndman, and Morley D. Hollenberg. "Abstract 2014: Genitourinary cancer-derived cells produce microenvironment proteinases that regulate proteinase activated receptors (PARs) to drive oncogenic signaling." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2014.

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Basañez, Gorka, Ana J. García Sáez, Oihana Terrones Uria, Juan Garcia Valero, Miguel Garcia Porras, Itsasne Bustillo Zabalbeitia, Hector Flores Romero, Ane Landajuela Larma, and Olatz Landeta Diaz. "BAK proteinaren mekanismo proapoptotikoa aztertzen." In I. Ikergazte. Nazioarteko ikerketa euskaraz. Bilbao: UEU arg, 2015. http://dx.doi.org/10.26876/ikergazte.i.47.

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DeSha, Michael S. "Biological Aerosol Sensor Breadboard." In The European Conference on Lasers and Electro-Optics. Washington, D.C.: Optica Publishing Group, 1998. http://dx.doi.org/10.1364/cleo_europe.1998.cfj7.

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In recent history, manmade and natural events have shown us the ever-present need for systems to monitor the troposphere for contaminates. These contaminants may take either a chemical or biological form, which determines the methods we use to monitor them. Monitoring the troposphere for biological contaminants is of particular interest to my organization. Whether manmade or natural, contaminants of a biological origin share a similar constitution: typically the aromatic amino acids tryptophan, phenylalanine, and tyrosine in varying amounts. All of these proteinaceous compounds have the capability to autofluoresce when exposed to ultraviolet radiation. This establishes the basis of the laser induced fluorescence (LIF) technique we use to detect biological contaminants. This technique can be employed in either point or remote detection schemes and is a valuable tool for discriminating proteinaceous from non-proteinaceous aerosols. For this particular presentation I am going to describe a breadboard point sensor I designed and fabricated to detect proteinaceous aerosols.
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Jung, Jung-Yeul, Ki-Taek Byun, Jae-Ho Hong, and Ho-Young Kwak. "Proteinaceous Bubbles and Nano Particle Flows in Microchannel." In ASME 2004 2nd International Conference on Microchannels and Minichannels. ASMEDC, 2004. http://dx.doi.org/10.1115/icmm2004-2437.

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Proteinaceous bubbles of 185 nm in average diameter were synthesized by a sonochemical treatment of bovine serum albumin in aqueous solution and the nanoparticles (TiO2) solution was made by ultrasonic irradiation. To study the macroscopic flow behavior associated with the changes in the state of microparticles, a flow test of these solutions in microchannels was done. Also the size distributions of the proteinaceous bubbles in solution before and after the flow test were measured by a light scattering method. Test results show that the air-filled proteinaceous bubbles in solution adjust their size to reduce the shear stress encountered in the flow through the microchannel. On the other hand, the flow rate of the solution with nanoparticles suspensions becomes smaller than that of deionized water above the flow rate of 6 cm3/min in the microchannel with a dimension of 100×150 μm2.
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Crisford, H. A., E. Sapey, and R. A. Stockley. "Validation of an In Vitro Model of the Proteinase/Anti-Proteinase Imbalance Observed in Alpha-1 Antitrypsin Deficiency." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a4080.

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Dooley, Kevin, and Scott Banta. "Engineering of functional proteinaceous hydrogels for biotechnology applications." In 2014 40th Annual Northeast Bioengineering Conference (NEBEC). IEEE, 2014. http://dx.doi.org/10.1109/nebec.2014.6972777.

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Sarioglu, Nurhan, Fuat Erel, Adnan Adil Hişmiogullari, and Celalettin Cevik. "Association between ADAMTs proteinases and Obstructive Sleep Apnea." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.oa1759.

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Erdozain Fernandez, Amaia Maite, Koldo Callado Hernando, Vincent Vialou, Sylvie Dumas, and Amaia Nuñez del Moral. "Zelulaz kanpoko matrizeko hevin proteinaren ikerketa giza garunean." In III. Ikergazte. Nazioarteko ikerketa euskaraz. Bilbao: UEU arg, 2019. http://dx.doi.org/10.26876/ikergazte.iii.04.01.

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Reports on the topic "Proteinaceo"

1

Radisky, Evette. Identification of Serine Proteinases Involved in Breast Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, September 2007. http://dx.doi.org/10.21236/ada475734.

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Tweten, Rodney K. Development of a Novel, Proteinase-Activated Toxin Targeting Tumor Neovascularization. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada391517.

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Tweten, Rodney K. Development of a Novel, Proteinase-Activated Toxin Targeting Tumor Neovascularization. Fort Belvoir, VA: Defense Technical Information Center, October 1998. http://dx.doi.org/10.21236/adb249654.

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Sieber, Fritz. Proteinated Subnano Particles of Elemental Selenium for the Treatment of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2005. http://dx.doi.org/10.21236/ada443081.

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Dolja, Valerian V., Amit Gal-On, and Victor Gaba. Suppression of Potyvirus Infection by a Closterovirus Protein. United States Department of Agriculture, March 2002. http://dx.doi.org/10.32747/2002.7580682.bard.

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The plant virus family Polyviridae is the largest and most destructive of all plant viruses. Despite the continuous effort to develop resistant plant varieties, there is a desperate need for novel approaches conferring wide-range potyvirus resistance. Based on experiments with the tobacco etch potyvirus (TEV)-derived gene expression vector, we suggested approach for screening of the candidate resistance genes. This approach relies on insertion of the genes into a virus vector and evaluation of the phenotypes of the resulting recombinant viruses. The genes which suppress infection by the recombinant virus are selected as candidates for engineering transgenic resistance. Our analysis of the TEV variants expressing proteins of the beet yellows closterovirus (BYV) revealed that one of those, the leader proteinase (L-Pro), strongly and specifically interfered with the hybrid TEV infection. Since closterovirus L-Pro is evolutionary related to potyviral helper component-proteinase (HC-Pro), we suggested that the L-Pro interfered with HC-Pro function via a trans-dominant inhibitory effect. Based on these findings, we proposed to test two major hypotheses. First, we suggested that L-Pro-mediated suppression of potyvirus infection is a general phenomenon effective against a range of potyviruses. The second hypothesis stated that the suppression effect can be reproduced in transgenic plants expressing L-Pro, and can be utilized for generation of resistance to potyviruses. In accord with these hypotheses, we developed two original objectives of our proposal: A) to determine the range of the closterovirus-derived suppression of potyviral infection, and B) to try and utilize the L-Pro-mediated suppression for the development of transgenic resistance to potyviruses. In the first phase of the project, we have developed all major tools and technologies required for successful completion of the proposed research. These included TEV and ZYMV vectors engineered to express several closteroviral L-Pro variants, and generation of the large collection of transgenic plants. To our satisfaction, characterization of the infection phenotypes exhibited by chimeric TEV and ZYMV variants confirmed our first hypothesis. For instance, similar to TEV-L- Pro(BYV) chimera, ZYMV-L-Pro(LIYV) chimera was debilitated in its systemic spread. In contrast, ZYMV-GUS chimera (positive control) was competent in establishing vigorous systemic infection. These and other results with chimeric viruses indicated that several closteroviral proteinases inhibit long-distance movement of the potyviruses upon co-expression in infected plants. In order to complete the second objective, we have generated ~90 tobacco lines transformed with closteroviral L-Pro variants, as well as ~100 lines transformed with BYV Hsp70-homolog (Hsp70h; a negative control). The presence and expression of the trans gene in each line was initially confirmed using RT-PCR and RNA preparations isolated from plants. However, since detection of the trans gene-specific RNA can not guarantee production of the corresponding protein, we have also generated L-Pro- and Hsp70h-specific antisera using corresponding synthetic peptides. These antisera allowed us to confirm that the transgenic plant lines produced detectable, although highly variable levels of the closterovirus antigens. In a final phase of the project, we tested susceptibility of the transgenic lines to TEV infection. To this end, we determined that the minimal dilution of the TEV inoculum that is still capable of infecting 100% of nontransgenic plants was 1:20, and used 10 plants per line (in total, ~2,000 plants). Unfortunately, none of the lines exhibited statistically significant reduction in susceptibility. Although discouraging, this outcome prompted us to expand our experimental plan and conduct additional experiments. Our aim was to test if closteroviral proteinases are capable of functioning in trans. We have developed agroinfection protocol for BYV, and tested if co- expression of the L-Pro is capable of rescuing corresponding null-mutant. The clear-cut, negative results of these experiments demonstrated that L-Pro acts only in cis, thus explaining the lack of resistance in our transgenic plants. We have also characterized a collection of the L-Pro alanine- scanning mutants and found direct genetic evidence of the requirement for L-Pro in virus systemic spread. To conclude, our research supported by BARD confirmed one but not another of our original hypotheses. Moreover, it provided an important insight into functional specialization of the viral proteinases and generated set of tools and data with which we will be able to address the molecular mechanisms by which these proteins provide a variety of critical functions during virus life cycle.
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Antonaci, Francesca C. Control of Transformation and Invasiveness of Breast Cancer Cells by Estrogen Regulation of Proteinase Inhibitor 9. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada471083.

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Dougherty, W. Understanding and targeting a novel plant viral proteinase/substrate interaction. Final report, July 1, 1989--June 30, 1995. Office of Scientific and Technical Information (OSTI), October 1995. http://dx.doi.org/10.2172/108096.

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Grubman, Marvin J., Yehuda Stram, Peter W. Mason, and Hagai Yadin. Development of an Empty Viral Capsid Vaccine against Foot and Mouth Disease. United States Department of Agriculture, August 1995. http://dx.doi.org/10.32747/1995.7570568.bard.

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Foot-and-mouth disease (FMD), a highly infectious viral disease of cloven-hoofed animals, is economically the most important disease of domestic animals. Although inactivated FMD vaccines have been succesfully used as part of comprehensive eradication programs in Western Europe, there are a number of concerns about their safety. In this proposal, we have attempted to develop a new generation of FMD vaccines that addresses these concerns. Specifically we have cloned the region of the viral genome coding for the structural proteins and the proteinase responsible for processing of the structural protein precursor into both a DNA vector and a replication-deficient human adenovirus. We have demonstrated the induction of an FMDV-specific immune response and a neutralizing antibody response with the DNA vectors in mice, but preliminary potency and efficacy studies in swine are variable. However, the adenovirus vector induces a significant and long-lived neutralizing antibody response in mice and most importantly a neutralizing and protective response in swine. These results suggest that the empty capsid approach is a potential alternative to the current vaccination strategy.
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Grafi, Gideon, and Brian Larkins. Endoreduplication in Maize Endosperm: An Approach for Increasing Crop Productivity. United States Department of Agriculture, September 2000. http://dx.doi.org/10.32747/2000.7575285.bard.

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The focus of this research project is to investigate the role of endoreduplication in maize endosperm development and the extent to which this process contributes to high levels of starch and storage protein synthesis. Although endoreduplication has been widely observed in many cells and tissues, especially those with high levels of metabolic activity, the molecular mechanisms through which the cell cycle is altered to produce consecutive cycles of S-phase without an intervening M-phase are unknown. Our previous research has shown that changes in the expression of several cell cycle regulatory genes coincide with the onset of endoreduplication. During this process, there is a sharp reduction in the activity of the mitotic cyclin-dependent kinase (CDK) and activation of the S-phase CDK. It appears the M-phase CDK is stable, but its activity is blocked by a proteinaceous inhibitor. Coincidentally, the S-phase checkpoint protein, retinoblastoma (ZmRb), becomes phosphorylated, presumably releasing an E2F-type transcriptional regulator which promotes the expression of genes responsible for DNA synthesis. To investigate the role of these cell cycle proteins in endoreduplication, we have created transgenic maize plants that express various genes in an endosperm-specific manner using a storage protein (g-zein) promoter. During the first year of the grant, we constructed point mutations of the maize M-phase kinase, p34cdc2. One alteration replaced aspartic acid at position 146 with asparagine (p3630-CdcD146N), while another changed threonine 161 to alanine (p3630-CdcT161A). These mutations abolish the activity of the CDK. We hypothesized that expression of the mutant forms of p34cdc2 in endoreduplicating endosperm, compared to a control p34cdc2, would lead to extra cycles of DNA synthesis. We also fused the gene encoding the regulatory subunit of the M- phase kinase, cyclin B, under the g-zein promoter. Normally, cyclin B is expected to be destroyed prior to the onset of endoreduplication. By producing high levels of this protein in developing endosperm, we hypothesized that the M-phase would be extended, potentially reducing the number of cycles of endoreduplication. Finally, we genetically engineered the wheat dwarf virus RepA protein for endosperm-specific expression. RepA binds to the maize retinoblastoma protein and presumably releases E2F-like transcription factors that activate DNA synthesis. We anticipated that inactivation of ZmRb by RepA would lead to additional cycles of DNA synthesis.
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Sela, Shlomo, and Michael McClelland. Investigation of a new mechanism of desiccation-stress tolerance in Salmonella. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7598155.bard.

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Low-moisture foods (LMF) are increasingly involved in foodborne illness. While bacteria cannot grow in LMF due to the low water content, pathogens such as Salmonella can still survive in dry foods and pose health risks to consumer. We recently found that Salmonella secretes a proteinaceous compound during desiccation, which we identified as OsmY, an osmotic stress response protein of 177 amino acids. To elucidate the role of OsmY in conferring tolerance against desiccation and other stresses in Salmonella entericaserovarTyphimurium (STm), our specific objectives were: (1) Characterize the involvement of OsmY in desiccation tolerance; (2) Perform structure-function analysis of OsmY; (3) Study OsmY expression under various growth- and environmental conditions of relevance to agriculture; (4) Examine the involvement of OsmY in response to other stresses of relevance to agriculture; and (5) Elucidate regulatory pathways involved in controlling osmY expression. We demonstrated that an osmY-mutant strain is impaired in both desiccation tolerance (DT) and in long-term persistence during cold storage (LTP). Genetic complementation and addition of a recombinantOsmY (rOsmY) restored the mutant survival back to that of the wild type (wt). To analyze the function of specific domains we have generated a recombinantOsmY (rOsmY) protein. A dose-response DT study showed that rOsmY has the highest protection at a concentration of 0.5 nM. This effect was protein- specific as a comparable amount of bovine serum albumin, an unrelated protein, had a three-time lower protection level. Further characterization of OsmY revealed that the protein has a surfactant activity and is involved in swarming motility. OsmY was shown to facilitate biofilm formation during dehydration but not during bacterial growth under optimal growth conditions. This finding suggests that expression and secretion of OsmY under stress conditions was potentially associated with facilitating biofilm production. OsmY contains two conserved BON domains. To better understand the role of the BON sites in OsmY-mediated dehydration tolerance, we have generated two additional rOsmY constructs, lacking either BON1 or BON2 sites. BON1-minus (but not BON2) protein has decreased dehydration tolerance compared to intact rOsmY, suggesting that BON1 is required for maximal OsmY-mediated activity. Addition of BON1-peptide at concentration below 0.4 µM did not affect STm survival. Interestingly, a toxic effect of BON1 peptide was observed in concentration as low as 0.4 µM. Higher concentrations resulted in complete abrogation of the rOsmY effect, supporting the notion that BON-mediated interaction is essential for rOsmY activity. We performed extensive analysis of RNA expression of STm undergoing desiccation after exponential and stationary growth, identifying all categories of genes that are differentially expressed during this process. We also performed massively in-parallel screening of all genes in which mutation caused changes in fitness during drying, identifying over 400 such genes, which are now undergoing confirmation. As expected OsmY is one of these genes. In conclusion, this is the first study to identify that OsmY protein secreted during dehydration contributes to desiccation tolerance in Salmonella by facilitating dehydration- mediated biofilm formation. Expression of OsmY also enhances swarming motility, apparently through its surfactant activity. The BON1 domain is required for full OsmY activity, demonstrating a potential intervention to reduce pathogen survival in food processing. Expression and fitness screens have begun to elucidate the processes of desiccation, with the potential to uncover additional specific targets for efforts to mitigate pathogen survival in desiccation.
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