Relevant bibliographies by topics / Proteins; Lectin

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  2. Dissertations / Theses
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Academic literature on the topic 'Proteins; Lectin'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Proteins; Lectin"

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Coelho, Luana Cassandra Breitenbach Barroso, Priscila Marcelino dos Santos Silva, Vera Lúcia de Menezes Lima, Emmanuel Viana Pontual, Patrícia Maria Guedes Paiva, Thiago Henrique Napoleão, and Maria Tereza dos Santos Correia. "Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications." Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–22. http://dx.doi.org/10.1155/2017/1594074.

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Lectins are proteins extensively used in biomedical applications with property to recognize carbohydrates through carbohydrate-binding sites, which identify glycans attached to cell surfaces, glycoconjugates, or free sugars, detecting abnormal cells and biomarkers related to diseases. These lectin abilities promoted interesting results in experimental treatments of immunological diseases, wounds, and cancer. Lectins obtained from virus, microorganisms, algae, animals, and plants were reported as modulators and tool markers in vivo and in vitro; these molecules also play a role in the induction of mitosis and immune responses, contributing for resolution of infections and inflammations. Lectins revealed healing effect through induction of reepithelialization and cicatrization of wounds. Some lectins have been efficient agents against virus, fungi, bacteria, and helminths at low concentrations. Lectin-mediated bioadhesion has been an interesting characteristic for development of drug delivery systems. Lectin histochemistry and lectin-based biosensors are useful to detect transformed tissues and biomarkers related to disease occurrence; antitumor lectins reported are promising for cancer therapy. Here, we address lectins from distinct sources with some biological effect and biotechnological potential in the diagnosis and therapeutic of diseases, highlighting many advances in this growing field.
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Tirta Ismaya, Wangsa, Raymond Rubianto Tjandrawinata, and Heni Rachmawati. "Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials." Molecules 25, no. 10 (May 20, 2020): 2368. http://dx.doi.org/10.3390/molecules25102368.

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The mushroom Agaricus bisporus secretes biologically active compounds and proteins with benefits for human health. Most reported proteins from A. bisporus are tyrosinases and lectins. Lectins are of therapeutic or pharmaceutical interest. To date, only limited information is available on A. bisporus lectins and lectin-like proteins. No therapeutic products derived from A. bisporus lectin (ABL) are available on the market despite its extensive exploration. Recently, A. bisporus mannose-binding protein (Abmb) was discovered. Its discovery enriches the information and increases the interest in proteins with therapeutic potential from this mushroom. Furthermore, the A. bisporus genome reveals the possible occurrence of other lectins in this mushroom that may also have therapeutic potential. Most of these putative lectins belong to the same lectin groups as ABL and Abmb. Their relationship is discussed. Particular attention is addressed to ABL and Abmb, which have been explored for their potential in medicinal or pharmaceutical applications. ABL and Abmb have anti-proliferative activities toward cancer cells and a stimulatory effect on the immune system. Possible scenarios for their use in therapy and modification are also presented.
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Bonnardel, François, Julien Mariethoz, Serge Pérez, Anne Imberty, and Frédérique Lisacek. "LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification." Nucleic Acids Research 49, no. D1 (November 11, 2020): D1548—D1554. http://dx.doi.org/10.1093/nar/gkaa1019.

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Abstract Lectins are non-covalent glycan-binding proteins mediating cellular interactions but their annotation in newly sequenced organisms is lacking. The limited size of functional domains and the low level of sequence similarity challenge usual bioinformatics tools. The identification of lectin domains in proteomes requires the manual curation of sequence alignments based on structural folds. A new lectin classification is proposed. It is built on three levels: (i) 35 lectin domain folds, (ii) 109 classes of lectins sharing at least 20% sequence similarity and (iii) 350 families of lectins sharing at least 70% sequence similarity. This information is compiled in the UniLectin platform that includes the previously described UniLectin3D database of curated lectin 3D structures. Since its first release, UniLectin3D has been updated with 485 additional 3D structures. The database is now complemented by two additional modules: PropLec containing predicted β-propeller lectins and LectomeXplore including predicted lectins from sequences of the NBCI-nr and UniProt for every curated lectin class. UniLectin is accessible at https://www.unilectin.eu/
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Milcheva, R., S. Petkova, and P. Babál. "Detection of O-glycosylated proteins from different Trichinella species muscle larvae total extracts." Helminthologia 46, no. 3 (September 1, 2009): 139–44. http://dx.doi.org/10.2478/s11687-009-0027-6.

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AbstractThe aim of the work was to analyze oligosaccharide composition with the focus on O-linked glycoproteins presence in the total extract obtained from different Trichinella species muscle larvae by means of lectin affino-blot with lectins selected for their sugar specificity. The absence of reactivity with two lectins, Tritrichomonas mobilensis lectin and Maackia amurensis agglutinin, indicated that the species of the Trichinella genus do not synthesize sialic acid. Reactivity with Helix pomatia lectin, Vicia villosa lectin-B4, peanut agglutinin and Ulex europeus lectin-I identified the presence of O-linked glycans identical to carcinoma-associated Tn-antigen (GalNAc-α-Ser/Thr) and T-antigen (Gal-β1,3-GalNAc-α-Ser/Thr) and also structures analogous to ABH-blood group antigens. The results obtained may contribute to a better understanding of the glycobiology of this parasitic nematode in relation to occupation of its intracellular niches.
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Brinda, K. V., Avadhesha Surolia, and Sarawathi Vishveshwara. "Insights into the quaternary association of proteins through structure graphs: a case study of lectins." Biochemical Journal 391, no. 1 (September 26, 2005): 1–15. http://dx.doi.org/10.1042/bj20050434.

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The unique three-dimensional structure of both monomeric and oligomeric proteins is encoded in their sequence. The biological functions of proteins are dependent on their tertiary and quaternary structures, and hence it is important to understand the determinants of quaternary association in proteins. Although a large number of investigations have been carried out in this direction, the underlying principles of protein oligomerization are yet to be completely understood. Recently, new insights into this problem have been gained from the analysis of structure graphs of proteins belonging to the legume lectin family. The legume lectins are an interesting family of proteins with very similar tertiary structures but varied quaternary structures. Hence they have become a very good model with which to analyse the role of primary structures in determining the modes of quaternary association. The present review summarizes the results of a legume lectin study as well as those obtained from a similar analysis carried out here on the animal lectins, namely galectins, pentraxins, calnexin, calreticulin and rhesus rotavirus Vp4 sialic-acid-binding domain. The lectin structure graphs have been used to obtain clusters of non-covalently interacting amino acid residues at the intersubunit interfaces. The present study, performed along with traditional sequence alignment methods, has provided the signature sequence motifs for different kinds of quaternary association seen in lectins. Furthermore, the network representation of the lectin oligomers has enabled us to detect the residues which make extensive interactions (‘hubs’) across the oligomeric interfaces that can be targetted for interface-destabilizing mutations. The present review also provides an overview of the methodology involved in representing oligomeric protein structures as connected networks of amino acid residues. Further, it illustrates the potential of such a representation in elucidating the structural determinants of protein–protein association in general and will be of significance to protein chemists and structural biologists.
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Hirabayashi, Jun, and Ryoichi Arai. "Lectin engineering: the possible and the actual." Interface Focus 9, no. 2 (February 15, 2019): 20180068. http://dx.doi.org/10.1098/rsfs.2018.0068.

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Lectins are a widespread group of sugar-binding proteins occurring in all types of organisms including animals, plants, bacteria, fungi and even viruses. According to a recent report, there are more than 50 lectin scaffolds (∼Pfam), for which three-dimensional structures are known and sugar-binding functions have been confirmed in the literature, which far exceeds our view in the twentieth century (Fujimoto et al. 2014 Methods Mol. Biol. 1200 , 579–606 ( doi:10.1007/978-1-4939-1292-6_46 )). This fact suggests that new lectins will be discovered either by a conventional screening approach or just by chance. It is also expected that new lectin domains including those found in enzymes as carbohydrate-binding modules will be generated in the future through evolution, although this has never been attempted on an experimental level. Based on the current state of the art, various methods of lectin engineering are available, by which lectin specificity and/or stability of a known lectin scaffold can be improved. However, the above observation implies that any protein scaffold, including those that have never been described as lectins, may be modified to acquire a sugar-binding function. In this review, possible approaches to confer sugar-binding properties on synthetic proteins and peptides are described.
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Takeuchi, Yuko, Ryoji Shinya, Kouichi Kuroda, Natsuko Miura, Kazuyoshi Futai, and Mitsuyoshi Ueda. "Surface coat proteins of the pine wood nematode, Bursaphelenchus xylophilus: profiles of stage- and isolate-specific characters." Nematology 11, no. 3 (2009): 429–38. http://dx.doi.org/10.1163/156854109x447006.

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AbstractThe present study was made to determine the binding patterns of several lectins to the surface coat (SC) proteins of various isolates and developmental stages of the pine wood nematode (PWN), Bursaphelenchus xylophilus. Also, the detailed characteristics of the SC proteins were profiled by using molecular techniques. The lectin-binding study demonstrated the stage-specific characters of SC in binding to the lectin, wheat germ agglutinin (WGA). WGA binding was observed only to the outer surfaces of third-stage propagative juveniles and to the egg shells, and this occurred more frequently in virulent than in avirulent PWN isolates. A greater variety of lectins bound to eggs than to any other life stage. For characterisation, the SC proteins extracted were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and analysed by lectin blotting. The results showed that the carbohydrate and protein patterns of the SC of the PWN changed during nematode development.
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Clerch, L. B., P. L. Whitney, and D. Massaro. "Rat lung lectin synthesis, degradation and activation. Developmental regulation and modulation by dexamethasone." Biochemical Journal 245, no. 3 (August 1, 1987): 683–90. http://dx.doi.org/10.1042/bj2450683.

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Soluble lectins are widely distributed cell-agglutinating proteins. Their activity is developmentally regulated in several tissues, including the lung, but virtually nothing is known about the mechanisms of the developmental regulation or the turnover of these proteins. We studied mechanisms that might be responsible for the developmentally regulated changes in the activity of a lectin (beta-galactoside-binding protein) found in the lung, and determined if its activity or turnover could be modulated by treatment of rat pups with a glucocorticosteroid hormone (dexamethasone). Our studies on the activity and turnover of the lectin indicated that the peak of lectin activity (units/mg of protein) that occurred at age 12 days appeared to be brought about by two means: an increase in the activity of the lectin molecule itself (units/micrograms of lectin) that occurred at age 8 days, and 1.5-fold increase in the absolute rate of lectin synthesis at age 11 days. The decline in lectin activity was associated with a decrease in its rate of synthesis, return to the baseline extent of activation, and an increased rate of degradation. Treatment of rat pups with dexamethasone diminished the peak of lectin activity (units/mg of protein) by about 25%. This effect of dexamethasone was due, at least in part, to the complete prevention of activation of the lectin molecule (units/micrograms of lectin) and a premature increase in the rate of lectin degradation. Perhaps the normal fall in lectin activity after age 11 days is caused by mechanisms induced by the increase in serum corticosteroid that occurs at that age.
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Melgarejo, Luz Marina, Nohora Vega, and Gerardo Pérez. "Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds." Brazilian Journal of Plant Physiology 17, no. 3 (September 2005): 315–24. http://dx.doi.org/10.1590/s1677-04202005000300006.

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Two lectins were isolated from Canavalia ensiformis and Dioclea grandiflora seeds. Gel filtration produced a fraction corresponding to Con A or D. grandiflora lectin while erythroagglutination assays revealed a distinct fraction presenting a lectin that agglutinates human red blood cells (RBCs) but not rabbit RBCs. Hydrophobic interaction chromatography showed that the latter fraction yielded a protein that readily agglutinates human erythrocytes; the lectin was also purified by affinity chromatography on Lac-Sepharose showing similar properties to that of the Phenyl-Sepharose-purified lectin. Despite minor differences (carbohydrate content or A1%1cm), the two lectins showed similar molecular properties in that they consisted of two non-covalently linked monomers having a Mr of 29-30 kDa and their pI values indicated that both lectins were slightly acidic proteins. The C. ensiformis lectin (CEL-II) and D. grandiflora lectin (DGL-II) specifically recognised the H-type 2 blood group (alpha-L-Fuc (1-2)-beta-D-Gal (1-4)-beta-D-GlcNAc-O-R), while binding to H-type 1, H-type 3, H-type 4, Leª or Le y was weaker. Carbohydrate inhibition of erythroagglutination showed that simple sugars were weakly recognised by the lectins, if at all. The N-terminal region presented a unique sequence hitherto found only in some Diocleinae lectins (designated type II). The overall results confirmed the existence of a second distinct lectin type, phylogenetically close to Diocleinae species. The data indicate a functional similarity among lectins of this type which possesses distinctive characteristics differentiating them from "classical" Man/Glc lectins.
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Ogilvie, Mary L., JoAnn Wilson Byl, and T. Kent Gartner. "Platelet Aggregation Is Stimulated by Lactose-lnhibitable Snake Venom Lectins." Thrombosis and Haemostasis 62, no. 02 (1989): 704–7. http://dx.doi.org/10.1055/s-0038-1646887.

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SummaryFive lactose-specific lectins from snake venoms were tested for the ability to stimulate the aggregation of human platelets. Three of the lectins, bushmaster (Lachesis muta), cottonmouth (Aricistrodon piscivorous leukostoma) and rattlesnake (Crotalus atrox) lectins, consistently stimulated secretion and aggregation. Thrombolectin (Bothrops atrox) occasionally caused aggregation. Copperhead (Agkistrodon contortrix contortrix) lectin did not by itself cause platelet aggregation. Lactose, a specific inhibitor of hemagglutination mediated by these lectins was a potent inhibitor of lectin-induced aggregation. Antiserum specific for bushmaster lectin inhibited aggregation by bushmaster lectin. In contrast, the same antiserum and anti-cottonmouth lectin serum enhanced aggregation by low levels of the other lectins.A variety of substances were assayed in the aggregometer for the ability to inhibit aggregation in response to these lectins. Both secretion and aggregation were inhibited by PGI2 and PGEx. Furthermore, lectin-induced aggregation was completely blocked by trifluoperazine and partially blocked by indomethacin. Monoclonal antibodies specific for GP IIb/IIIa (AP2, A2A9, LJP5, LJCP8) but not monoclonals directed against other platelet membrane proteins (API and AP3) inhibited lectin-induced aggregation. The peptide Arg-Gly-Asp-Ser but not Arg-Ala-Asp-Ser was a potent inhibitor of aggregation.
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Dissertations / Theses on the topic "Proteins; Lectin"

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Perdikoulis, Michael V. "Studies on the modular organization of human properdin and C1q of the complement pathway." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312551.

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Batista, Adelina Braga. "Potential fungicidal and insecticidal proteins present in seeds Dioclea megacarpa Rolfe." Universidade Federal do CearÃ, 2009. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=3789.

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CoordenaÃÃo de AperfeiÃoamento de NÃvel Superior
Dioclea megacarpa Rolfe is the correct synonym for D. relexa var. grandiflora. This species belongs to Fabaceae, the legume family. Previous studies, realized in our research group, showed the presence of active proteins for several phytopathogenic fungi in the seeds of this species, among of them Aspergillus niger. Thus, the present work was proposed with the objective of determining the bioactivity of protein(s) from D.megacarpa seeds against fungi, leading to its/their purification and partial characterization and further investigation of its/their action mechanism. Another approach of this work it was analyze the insecticidal potential of glucose/mannose-specific lectin, isolated from D.megacarpa seeds (Moreira et al., 1983), against the cowpea bruchid Callosobruchus maculatus. For this, seed flour was placed in contact with 0.15 M NaCl (1:5, w/w), followed by stirring for 3 h, filtration through a nylon cloth, re-extraction for 1 h, centrifugation at 11,500 x g, for 30 min, at 4 oC. The supernatant obtained, named total extract, showed antifungal activity against A. niger and presented several bioactive proteins, including lectin (129.27 UH/mgP, using trypsinized rabbit erythrocytes), trypsin inhibitor (18.91 mg de tripsina inibida/gF), urease (47.50 U/gF), toxin (LD50 119.60 mgP/Kg mice body weight ), chitinase (1.66 nKat/mgP) e β-1,3-glucanase (0.55 nKat/mgP). On the other hand, peroxidasic and proteolytic activities were not detected. For purification of antifungal principle, several chromatographies were performed on Sephadex G-50, Chitin and Resource Q, this last connected to an FPLC system. The purified antifungal protein, named Dm-PAF, with apparent molecular mass of 67-68 kDa (SDS-PAGE), did not show any haemagglutinating or chitinolytic activity and presented its NH2-terminal sequence blocked. Dm-PAF, at a very low concentration (0.015 ÂgP/ÂL), it was able to inhibit the growth of Saccharomyces cerevisiae and Candida tropicalis yeasts. The investigation of the antifungal action mechanism excluded the possibility of interaction between Dm-PAF and H+-ATPase pumps. In addition, the glucose/mannose-specific lectin, obtained from Sephadex G-50 column, exhibited a potent insecticidal activity against C. maculatus, interfering in important parameters related to life cycle of this insect. These data show to be the D. megacarpa seeds a rich source of biologically interesting proteins, possibly involved in the defense mechanism of plants
Dioclea megacarpa Rolfe à usada como sinonÃmia de D. relexa var. grandiflora, uma espÃcie pertencente à famÃlia Fabaceae (Leguminosae). Estudos prÃvios, realizados por nosso grupo de pesquisa, demonstraram a presenÃa em suas sementes de proteÃnas ativas contra fungos fitopatogÃnicos, dentre esses Aspergillus niger. Assim, o presente trabalho foi proposto no intuito de avaliar a bioatividade de proteÃnas de sementes de D. megacarpa contra fungos, conduzindo à sua purificaÃÃo e caracterizaÃÃo parcial, bem como à investigaÃÃo de seu mecanismo de aÃÃo. Outro objetivo deste trabalho foi examinar o potencial inseticida da lectina com especificidade por glucose-manose, isolada de sementes de D. megacarpa (Moreira et al., 1983), contra o bruquÃdeo do feijÃo-caupi Callosobruchus maculatus. Para tanto, farinha de sementes foi posta em contato com NaCl 0,15 M (1:5, p/v), seguida de agitaÃÃo contÃnua por 3 h, filtraÃÃo em pano de trama fina, re-extraÃÃo por 1 h e centrifugaÃÃo a 11.500 x g, 30 min, 4 oC. O sobrenadante obtido, denominado de extrato total, se mostrou ativo contra A. niger e apresentou vÃrias proteÃnas bioativas, compreendendo lectina (129,27 UH/mgP, com eritrÃcitos tripsinizados de coelho), inibidor de tripsina (18,91 mg de tripsina inibida/gF), urease (47,50 U/gF), toxina (DL50 119,60 mgP/Kg de peso corpÃreo de camundongo), quitinase (1,66 nKat/mgP) e β-1,3-glucanase (0,55 nKat/mgP). Por outro lado, atividades peroxidÃsica e proteolÃtica nÃo foram detectadas. Para purificaÃÃo da proteÃna antifÃngica, foram realizadas cromatografias em matrizes de Sephadex G-50, Quitina e Resource-Q, essa Ãltima acoplada ao sistema de FPLC. A proteÃna antifÃngica purificada de sementes de D. megacarpa, denominada de Dm-PAF, com massa molecular aparente de 67-68 kDa (PAGE-SDS), nÃo mostrou atividades hemaglutinante e quitinÃsica e apresentou sua seqÃÃncia NH2-terminal bloqueada. Dm-PAF, em concentraÃÃo baixÃssima (0,015 ÂgP/ÂL), se mostrou capaz de inibir o crescimento das leveduras Saccharomyces cerevisiae e Candida tropicalis, cuja investigaÃÃo do mecanismo de aÃÃo nÃo revelou envolvimento dessa proteÃna com bombas de H+-ATPase. Em adiÃÃo, a lectina ligante a glucose-manose, obtida na cromatografia em Sephadex G-50, mostrou potente atividade inseticida contra C. maculatus, interferindo em parÃmetros importantes relacionados ao ciclo de vida do inseto. Os dados apresentados mostram as sementes de D. megacarpa como uma rica fonte de proteÃnas interessantes, possivelmente envolvidas no mecanismo de defesa das plantas
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Does, Maria Petronella. "Chimeric proteins of stinging nettle lectin, chitinase and [beta]-1,3-glucanase." [S.l. : Amsterdam : s.n.] ; Universiteit van Amsterdam [Host], 2000. http://dare.uva.nl/document/55397.

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Sousa, Michelle Amelia De. "Investigation into the lectin component of Type II ribosome inactivating proteins." Thesis, University of Warwick, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.264904.

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Baba, Kei'ichi. "LECTIN AND RELATED PROTEINS IN THE BARK OF Sophora japonica L." Kyoto University, 1990. http://hdl.handle.net/2433/78243.

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Reidy, Michael James. "Engineering of the RTB Lectin as a Carrier Platform for Proteins and Antigens." Diss., Virginia Tech, 2007. http://hdl.handle.net/10919/26155.

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The major obstacle many promising drugs struggle to overcome is the barrier imposed by the outer cell membrane. In addition to technologies such as liposomes and cell-penetrating peptides, more attention is being given to the class of proteins known as lectins to deliver therapeutic and antigenic proteins to the interiors of cells. Lectins bind to but do not modify sugars, and provide an efficient route to endocytosis. The galactose/N-acetyl-galactosamine specific lectin ricin B-chain (RTB) is especially attractive in possibly fulfilling a carrier role due to its well-characterized endocytotic trafficking and its efficacy over a wide range of cell types. By producing RTB recombinantly in plants it is possible to create a fully active, non-toxic carrier that does not rely on the processing of large amounts of toxic material (e.g. castor bean). Payload molecules such as small molecules and proteins can be attached to RTB via chemical conjugation at primary amine groups, without the loss of lectin or uptake activities. The biotin/streptavidin interaction and direct genetic fusion of polypeptides also provide efficient mechanisms for the attachment of payload proteins to RTB. An immunoglobulin domain-based scaffolding mechanism bridges modified RTB and payload proteins when co-expressed in Agrobacterium-infiltrated plant leaves. Carrier and payload proteins expressed in plants and E. coli, respectively, and purified independently are not able to assemble into an efficient carrier/payload arrangement. These findings show that plant cells are able to correctly produce the two components of the carrier/payload system and assemble them into an efficient and flexible capture and carry technology.
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Down, Rachel Elizabeth. "Use of endogenous plant defensive proteins to confer resistance to aphids in crop plants." Thesis, Durham University, 1998. http://etheses.dur.ac.uk/4786/.

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A liquid artificial diet system, which was suitable for bioassay of added compounds, was developed for the glasshouse potato aphid, Aulacorthum solani. The diet supported normal growth and reproduction of this insect. Once established, the artificial diet bioassay system was used to test potential insecticidal activities of a variety of proteins found naturally occurring in plants. Effects on survival, development and fecundity were measured. The lectin found in snowdrop, Galanthus nivalis agglutinin (GNA) was found to significantly reduce the fecundity of A. solani, in terms of parthenogenetic nymph production, when administered in artificial diets at the 0.1% w/v level. No significant reductions in survival were found, although GNA administered in vitro did appear to slow the development of A. solani. Transgenic potato plants expressing GNA were used in a growth room trial to show that the reduction in fecundity with the in vitro trials could be reproduced in planta. Aphids feeding on the GNA-expressing potatoes had a significantly lower cumulative nymph production than those feeding on non- transformed plants. The transgenic plants had no effect on the survival of A. solani. The GNA-expressing plants were tested in a larger scale glasshouse trial and resulted in a significantly slower buildup of aphids when compared to control potatoes, thus confirming the results of the artificial diet bioassays and in planta growth room trials. Immunohistochemical studies were performed to detect the presence of GNA in the gut lumen of A. solani fed on artificial diet containing 0.1% w/v GNA; the lectin was observed to be selectively concentrated in the region of the epithelial membrane in the stomach, suggesting that binding to surface carbohydrates or glycoproteins was taking place. Binding to the gut surface has been suggested to mediate lectin toxicity in higher animals, and other insects. A synergistic effect was observed with transgenic potatoes expressing a double construct encoding GNA and bean chitinase (BCH); A. solani cumulative nymph production on these plants was significantly reduced compared to aphids feeding on control and GNA-only expressing plants. However, interestingly, BCH-only expressing plants did not significantly affect the fecundity of A. solani, although a slight reduction in nymph production was observed. On the basis of reports in the literature that suggested that chitin-binding lectins were toxic to insects, an attempt to isolate the gene encoding the chitin-binding stinging nettle lectin was made. RNA was extracted from nettle rhizomes and used to prepare a cDNA library. Successful library construction was verified. PGR methods and a primary screen of the library were used in an attempt to locate the gene.
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Toot, Amanda Lee. "Localization and characterization of C-type lectin-like family of proteins in Leptospira interrogans." [Ames, Iowa : Iowa State University], 2007.

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Aroso, Miguel Ângelo Mouta Martins. "Characterisation of ZG16p, a unique mammalian lectin from pancreatic zymogen granules." Doctoral thesis, Universidade de Aveiro, 2015. http://hdl.handle.net/10773/14099.

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Doutoramento em Bioquímica
The mechanisms of secretory granule biogenesis and regulated secretion of digestive enzymes in pancreatic acinar cells are still not well understood. To shed light on these processes, which are of biological and clinical importance (e.g., pancreatitis), a better molecular understanding of the components of the granule membrane, their functions and interactions is required. The application of proteomics has largely contributed to the identification of novel zymogen granule (ZG) proteins but was not yet accompanied by a better characterization of their functions. In this study we aimed at a) isolation and identification of novel membrane-associated ZG proteins; b) characterization of the biochemical properties and function of the secretory lectin ZG16p, a membrane-associated protein; c) exploring the potential of ZG16p as a new tool to label the endolysosomal compartment. First, we have performed a suborganellar proteomics approach by combining protein analysis by 2D-PAGE and identification by mass spectrometry, which has led to the identification of novel peripheral ZGM proteins with proteoglycan-binding properties (e.g., chymase, PpiB). Then, we have unveiled new molecular properties and (multiple) functions of the secretory lectin ZG16p. ZG16p is a unique mammalian lectin with glycan and proteoglycan binding properties. Here, I revealed for the first time that ZG16p is highly protease resistant by developing an enterokinase-digestion assay. In addition I revealed that ZG16p binds to a high molecular weight complex at the ZGM (which is also protease resistant) and forms highly stable dimers. In light of these findings I suggest that ZG16p is a key component of a predicted submembranous granule matrix attached to the luminal side of the ZGM that fulfils important functions during sorting and packaging of zymogens. ZG16p, may act as a linker between the matrix and aggregated zymogens due to dimer formation. Furthermore, ZG16p protease resistance might be of higher importance after secretion since it is known that ZG16p binds to pathogenic fungi in the gut. I have further investigated the role of ZG16p binding motifs in its targeting to ZG in AR42J cells, a pancreatic model system. Point mutations of the glycan and the proteoglycan binding motifs did not inhibit the targeting of ZG16p to ZG in AR42J cells. I have also demonstrated that when ZG16p is present in the cytoplasm it interacts with and modulates the endo-lysosomal compartment. Since it is known that impaired autophagy due to lysosomal malfunction is involved in the course of pancreatitis, a potential role of ZG16p in pancreatitis is discussed.
Os mecanismos de biogénese dos grânulos secretores e a secreção regulada das enzimas digestivas, nas células acinares do pâncreas, ainda não são totalmente compreendidos. Para esclarecer estes processos, que são de importância biológica e clínica (ex., pancreatite), é necessário um melhor conhecimento molecular dos componentes da membrana dos grânulos, as suas funções e interações. A aplicação da proteómica contribuiu largamente para a identificação de novas proteínas dos grânulos de zimogénio (ZG) mas ainda não foi acompanhada por uma melhor caracterização das suas funções. Este estudo teve como objectivos a) o isolamento e identificação de novas proteínas associadas à membrana dos ZG; b) a caracterização das propriedades bioquímicas e da função da lectina ZG16p, uma proteína associada a membrana dos ZG; c) explorar o potencial da ZG16p como uma nova ferramenta para marcar o compartimento endolisossomal. Inicialmente, efetuamos uma abordagem proteómica ao estudo das frações dos ZG, a qual nos levou à identificação de novas proteínas periféricas da ZGM com capacidade de se ligarem a proteoglicanos (Chymase e PpiB). Depois, começamos a desvendar as propriedades moleculares e (múltiplas) funções da lectina ZG16p. A ZG16p é uma proteína única nos mamíferos com capacidade de se ligar a glicanos e a proteoglicanos. Pela primeira vez, foi revelado que a ZG16p é extremamente resistente a proteases através do desenvolvimento de um ensaio de digestão com enterokinase. Adicionalmente, demonstrei que a ZG16p se liga a um complexo de elevado peso molecular (também resistente a proteases) e forma homodímeros muito estáveis. À luz destas descobertas, nós sugerimos que a ZG16p poderá actuar como um elo de ligação aos proteoglicanos, ajudando na formação e estabilização de uma rede/estrutura (matriz submembranar) ligada ao lúmen da ZGM, que desempenhará uma função importante durante a segregação e empacotamento dos zimogénios. A ZG16p poderá atuar como um elo de ligação entre a matriz e os zimogénios agregados devido à sua capacidade para formar dímeros. Adicionalmente, a resistência da ZG16p a protéases poderá ser de maior importância após a secreção, uma vez que é sabido que a ZG16p se liga a fungos patogénicos nos intestinos. Investiguei ainda, o papel dos domínios de ligação da ZG16p na sua segregação para os ZG em células AR42J, um modelo pancreático. A mutação pontual dos motivos de ligação a glicanos e a proteoglicanos não alterou a segregação da ZG16p para os ZG. Também demonstrei que quando a ZG16p se encontra no citoplasma liga-se ao compartimento endolisossomal. Como é sabido, a desregulação da autofagia devido ao funcionamento defeituoso dos lisossomas está associado à pancreatite, por isso iremos discutir o papel potencial da ZG16p nesta doença.
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Fraser, Stuart Tallis. "Lectin - carbohydrate interactions in lympho-haemopoiesis: a study of L-selectin, ligands of L-selectin and CD24 inthe rat." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1998. http://hub.hku.hk/bib/B31236844.

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Books on the topic "Proteins; Lectin"

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Sousa, Michelle Amelia De. Investigation into the lectin component of type 11 ribosome inactivating proteins. [s.l.]: typescript, 1996.

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1923-, Lis H., ed. Lectins. London: Chapman and Hall, 1989.

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1923-, Lis H., ed. Lectins. 2nd ed. Dordrecht: Kluwer Academic Publishers, 2003.

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Lord, Mike, and Martin R. Hartley. Toxic plant proteins. Heidelberg: Springer, 2010.

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Ezekowitz, R. Alan B. Collectins and innate immunity. New York: Springer, 1996.

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Carbohydrate recognition: Biological problems, methods, and applications. Hoboken, N.J: Wiley, 2011.

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Kilpatrick, David C. Handbook of animal lectins: Properties and biomedical applications : a compendium of galectins, collectins, selectins, pentraxins, and other carbohydrate-binding proteins from throughout the animal kingdom. Chichester: John Wiley, 2000.

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M, Shannon Leland, Chrispeels Maarten J. 1938-, and University of California, Riverside. Dept. of Botany and Plant Sciences, eds. Molecular biology of seed storage proteins and lectins: Proceedings of the Ninth Annual Symposium in Plant Physiology, January 9-11, 1986, University of California, Riverside. Rockville, Md: American Society of Plant Physiologists, 1986.

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Tkac, Jan. Chapter Perspectives in Glycomics and Lectin Engineering. Springer Nature, 2014.

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1938-, Mirelman David, ed. Microbial lectins and agglutinins: Properties and biological activity. New York: Wiley, 1986.

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Book chapters on the topic "Proteins; Lectin"

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Minic, Z., L. Leproust, Y. de Kouchkovsky, and S. Brown. "Lectin-Type Proteins of Medicago sativa Roots." In Biological Nitrogen Fixation for the 21st Century, 255. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-5159-7_124.

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Shen, Zhao-Wen. "Membrane Glycoproteins and Plant and Animal Proteins with Lectin or Lectin-Like Properties." In The Molecular Immunology of Complex Carbohydrates, 187–203. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1663-3_8.

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Haab, Brian B. "Probing Glycoforms of Individual Proteins Using Antibody-Lectin Sandwich Arrays." In Proteomics for Biological Discovery, 311–28. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2019. http://dx.doi.org/10.1002/9781119081661.ch13.

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Yoshida, Yukiko. "Lectin-Type Ubiquitin Ligase Subunits: Fbs Proteins and Their Applications for Use." In Methods in Molecular Biology, 215–24. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0430-4_22.

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Ferguson, R. E., D. H. Jackson, R. Hutson, N. Wilkinson, P. Harnden, P. Selby, and R. E. Banks. "Detection of Glycosylation Changes in Serum and Tissue Proteins in Cancer by Lectin Blotting." In Advances in Experimental Medicine and Biology, 113–14. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-25515-x_19.

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Peumans, Willy J., and Els J. M. Van Damme. "Seed Lectins." In Seed Proteins, 657–83. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4431-5_28.

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Sandbulte, Matthew R., and Maryna C. Eichelberger. "Analyzing Swine Sera for Functional Antibody Titers Against Influenza A Neuraminidase Proteins Using an Enzyme-Linked Lectin Assay (ELLA)." In Methods in Molecular Biology, 337–45. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0758-8_28.

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Frigerio, Lorenzo, and Lynne M. Roberts. "The Synthesis of Ricinus communis Lectins." In Toxic Plant Proteins, 191–205. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-12176-0_10.

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Ferreras, José Miguel, Lucía Citores, Rosario Iglesias, Pilar Jiménez, and Tomás Girbés. "Sambucus Ribosome-Inactivating Proteins and Lectins." In Toxic Plant Proteins, 107–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-12176-0_6.

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Propheter, Daniel C., Ku-Lung Hsu, and Lara K. Mahal. "Recombinant Lectin Microarrays for Glycomic Analysis." In Protein Microarray for Disease Analysis, 67–77. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-043-0_6.

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Conference papers on the topic "Proteins; Lectin"

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Noval, Claudia, Marina Ferreira, Diego Gonçalves, Yasmin Braga, Rodrigo Figueiredo, Leonardo Nimrichter, and Allan Guimarães. "Purification and evaluation of antifungal properties of lectin-Fc proteins against Aspergillus fumigatus." In IV International Symposium on Immunobiologicals & VII Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2019. http://dx.doi.org/10.35259/isi.sact.2019_32694.

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Aihara, M., S. Morimoto, Y. Sawada, A. Kimura, Y. Chiba, and Y. Yoshida. "A ROLE OF PLATELET MEMBRANE COMPONENTS IN THE INTERACTION OF PLATELET-COLLAGEN-VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644480.

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To determine a role of platelet membrane components on the interaction of platelet-collagen-von Willebrand factor(vWF), several experimental approaches were used. The adhesion of human fixed washed platelets(FWP) to collagen was decreased after the treatment with Serratia marcescens protease(100 ug/ml), but the collagen cofactor activity(COo) of vWF that enhances the adhesion of FWP to collagen was still present after the digestion. Although the platelet adhesion in the absence of normal plasma was not changed by the addition of monoclonal antibody(M-ab) against platelet membrane glycoprotein(GP) IIb/lIIa(1 0E5, BS Coller), the adhesion was decreased by 30-50% after the treatment of the platelets with 10-100 ug/ml anti-GPIb(6D1, BS Coller). The adhesion of FWP to collagen was inhibited by lectins;the adhesion was 58-75% in the presence of 100-400 ug/ml L. culinaris lectin or weat germ agglutinin and the adhesion was nil in the presence of 100 ug/ml Ricinus communis agglutinin I or 200 ug/ml concanavalin A. By the crossed aff ino-immunoelectrophoresis, the binding of GP Ilb/lIIa in Triton-solubilized platelet supernatant to the collagen spacer gel was observed. When CHAPSO solubilized platelet was applied to the collagen column and the fractions containing adhesion inhibitor were eluated by 0.3M NaCl, Mr of 240K, 220K, 21 OK, 116K, 61K, 54K, 50K and 45K proteins were identified besides the proteins which correspond to thrombospondin, GPIb, GP lib or Ilia by SDS-PAGE(7.5% gel, silver stain). GOo in normal plasma was not changed by anti-GPIIb/lIIa but was decreased to 32-38%by anti-GPIb. M-ab against vWF, CLB-RAg 35(van Mourik), that inhibits the binding of vWF to platelet by ristocetin decreased COo in normal plasma by 70% and CLB-RAg 201 (van Mourik) that inhibits the binding of vWF to collagen did completely inhibit the COo in normal plasma. In conclusion, our data suggest that (1) GPIb is partly involved in the platelet adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo of vWF is partly mediated though GPIb; and (4) several platelet membrane protein(s) besides GPIb or GPIIb/lIIa may be also involved in both the adhesion of platelets to collagen and CCo of vWF.
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Gonzatto, Vitor, Maria Eduarda Bezerra Milhomem, Ana Carolina Lima Delfino, Kátia Bonfim Leite de Moura Sérvulo, and Lidiane Pereira de Albuquerque. "INVESTIGAÇÃO DA PRESENÇA DE LECTINAS EM PREPARAÇÕES DE FOLHAS DE Anacardium occidentale L. E Syzigium cumini (L.) SKEELS." In I Congresso Brasileiro de Biotecnologia On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/795.

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Introdução: Lectinas são glicoproteínas que reconhecem glicoconjugados de superfícies celulares, possibilitando diversas aplicações biotecnológicas. Objetivo: Investigar a presença de lectinas em folhas de A. occidentale e S. cumini Material e métodos: A farinha das folhas secas de S. cumini e A.occidentale foram homogeneizadas em NaCl 0,15 M. Após filtração e centrifugação, o sobrenadante correspondeu ao extrato. As proteínas presentes no extrato foram precipitadas com (NH4)2SO4 obtendo-se a fração proteica F0-60% (após centrifugação/dialise). As preparações foram avaliadas quanto à concentração proteica e a presença de lectinas foi avaliada pela atividade hemaglutinante (AH) utilizando eritrócitos humanos e de coelho. Realizou-se o ensaio de inibição da AH com carboidratos. Para o ensaio do efeito do pH sobre a AH, as F0-60% foram incubadas em tampões na faixa de pH 4-8; Para determinar a estabilidade térmica, as F0-60% foram incubadas entre 30 e 100 °C antes da realização da AH. Resultados: A concentração proteica para S.cumini foi de 5,0 mg/mL(extrato) e 7,0 mg/mL (F0-60%) e de A. occidentale 17 mg/mL (extrato) e 8,6 mg/mL(F0-60%). No ensaio de AH as preparações mostraram maior AH para eritrócitos de coelho. A lectina em F0-60% de S.cumini foi inibida por glicose, galactose, lactose e manose; e A.occidentale por frutose, maltose, manose, e metil-α-D-glicopiranosídeo. Para S.cumini, AHE de F0-60% foi diminuída em toda faixa de pH testada e após aquecimento a 30 ºC. Na F0-60% de A.occidentale, a AHE foi mantida em toda faixa até pH 7,0,diminuíndo em pH 8,0; o aquecimento não alterou a AH. Conclusão: podese deduzir a presença de lectina nas preparações de folhas de A. occidentale e S. cumini, como demonstrado pelos ensaios de AH e de inibição. A Caracterização estrutural e investigação de atividades biológicas estão em planejamento.
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Lian, E. C. Y., and F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.

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We have previously reported the purification of a 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura. using 125I-labeled p37, the properties of its binding to platelets were studied. The binding of p37 to washed human platelets from 4 normal subjects and two TTP patients after recovery was specific, concentration dependent and saturable. The Scatchard analysis revealed that the binding sites for p37 was about 100,000 per platelet with a dissociation constant of 48 × 10−9 M. The binding of p37 to erythrocytes was very little and non-specific. Stimulation of platelets by thrombin or ADP did not have any effect on the binding of p37 to platelets. The monoclonal antibodies to platelet GP lb (6D1) and GP Ilb-llla (10E5)(A gift of Dr. Barry coller) did not inhibit the binding of p37 to platelets. Fibrinogen (1 mg/ml) and FVIII/vWF (250 ug/ml) reduced the binding slightly. The polyclonal antibodies to p37 as well as concanavalin-A inhibited the binding of p37 to platelets through their direct interaction with p37. Other lectins such as phytohemagglutinin, potato lectin and helix pomatia lectin did not have any effect. At 40 mM, sialic acid, α-D-(+)-glucose, D-(+)-mannose and D-fructose caused 91%,44%,79%, and 63% inhibition of p37 binding respectively. D-(+)-galactose did not interfere with the binding. It is concluded that p37 binds to platelets on the sites other than GP lb and Gp IIb-IIIa and its binding to platelets is inhibited by certain sugars.
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Naji, Foziyeh Esmaiel, Mohammed Ehlayel, Nader Al-Dewik, and Ahmed Malki. "Clinical Utility and Cost Effectiveness of Complement 3 and Complement 4 in different Clinical Subspecialties in Hamad Medical Corporation." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0161.

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Background: Complement system is one of ancient innate immune systems in our body fighting against pathogens and foreign bodies. Either one of its three pathways, classical, alternative or lectin activates it. Because of its role and importance in combating against different pathological conditions, it works through defined proteins including regulators and inhibitors. However, over or under stimulation of complement system can lead to various diseases. A number of analytical assays are used to measure complement proteins and its activation states considering complement 3 (C3), complement 4 (C4) as the most common test used. Objectives: Our aims are to study the clinical utility and cost effectiveness of C3 and C4 among different clinical subspecialties in Hamad Medical Corporation (HMC), Doha-Qatar. Design and methods: A retrospective study was conducted using electronic medical records to generate patient’s list from clinical immunology laboratory at HMC. Data on 326 patients were collected from 1st January till 31st March, 2017 and used as pilot study after omitting duplications. The data was studied for its demographical, disease categories, C3 and C4 test results. C3 and C4 test cost were calculated inside HMC and compared to other healthcare providers in country and abroad. Results: A total of 326 patients, 148 males and 178 females (M/F ratio:0.8:1), of age (mean age ±SD) of 36 ± 17.6 years. 289(86%) were >15 years and 47(14%) were 15 or less. Kidney diseases (34%), autoimmune diseases (25%), and allergic diseases (18%) were the top 3 diseases, and constituted 77% of all diseases. 45/336 (13.4%) showed low C3, C4, or both. Mean levels of C3 (±SD) was 120.8 ±36.3 mg/dl, and C4 was27.85±11.9 mg/dl. High C3 and C4 levels were observed in 53 (15.7%) of patients. The cost of performing one test either C3 or C4 in HMC is 22 QR ($6), while other healthcare providers inside the country costed 150-300 QR ($41.2-$82.4). Conclusion: Autoimmune diseases, renal diseases and joist diseases were the most common diseases with low C3 and C4 levels. Although the cost of a single test of C3 or C4 is low, the total annual cost is huge. The treating physician is recommended to exercise judicious clinical wisdom when ordering C3 or C4 tests as diagnostic tools
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Koç, Mehmet, Emine Varhan, Zehra Kasımoğlu, and Hilal Şahin Nadeem. "The effect of different wall materials on the production of suppressed-pungent capsaicin microparticles." In 21st International Drying Symposium. Valencia: Universitat Politècnica València, 2018. http://dx.doi.org/10.4995/ids2018.2018.7721.

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The aim of this study was to investigate the effects of wall materials types on the production of double-layered and suppressed-pungent capsaicin microparticles via spray chilling method. For this purpose, palm oil and different proteins (gelatin, sodium caseinate and whey protein) were used as wall materials, while soy lecithin was selected as stabilizer. Sample encapsulated only with palm oil (single-layered) was used as control. Centrifuge stability and kinetic stability were analyzed on the prepared emulsions. Total and surface capsaicin, microencapsulation efficiency, melting point temperature and fusion enthalpy analysis were carried out on the capsaicin microparticles obtained by spray chilling.Keywords: Capsaicin; Spray chilling method; Pungency; Double-layered microparticles
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Kehrel, B., L. Ballesian, R. Kokott, W. Stenzinger, K. J. Clemetson, and J. Van De Loo. "REVERSIBLE DEFICIENCY OF INTACT THROMBOSPONDIN AND MEMBRANE GLYCOPROTEIN Ia IN PLATELETS OF A PATIENT WITH A BLEEDING DISORDER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644654.

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A 52 year old female patient with a severe bleeding tendency since the age of two was studied. Her history revealed recurrent petechial bleedings, two severe postoperative haemorrhagic episodes and intensivemenstrual bleedings which required blood transfusions. Coagulation studies ruled out any coagulation disorder including von Willebrand's disease. Platelet count and morphology(using light and electron microscopy) were normal. The patient had prolonged bleeding times (up to 15 min). Her platelets aggregated normally in response to ADP, arachidonic acid, thrombin, ionophore A 23187, epinephrine and ristocetin. In contrast, platelet aggregation in the presence of collagen and wheat germ agglutinin could only be achieved with very high doses of these agonists. Repeated analyses of the patient's platelet proteins by two-dimensional 0'Farrel gel electrophoresis followed by silver staining or blotting onto nitrocellulose and staining with a mixture of peroxidase-coupled lectins showed that glycoprotein la and intact thrombospondin were absent. An immunoblot for thrombospondin showed several proteins with lower molecular weight than thrombospondin. Preincubation of the patient's platelets with thrombospondin normalized collagen-induced aggregation.At a recent follow-up examination the patient had no petechial bleedings. Platelet protein analysis revealed thatintact thrombospondin and glycoprotein la were present. These results suggest that both glycoprotein la and thrombospondin have essential roles in collagen-induced platelet aggregation.
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Koller, E., and F. Koller. "LIPOPROTEIN BINDING TOHUMAN PLATELETS IS LOCATED AT GPIIb/IIIa COMPLEX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643702.

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Human Platelets possess specific binding sites for low density lipoproteins (LDL) and high density lipoproteins(HDL)(1). Binding of both classes of plasma lipoproteins, though competitive, has been shown by several groups to facilitate platelet activation.Isolated washed platelets occasionally aggregate upon addition of high concentrations of LDL even in the absence of known platelet activators. The proteins responsible for this binding have been visualized by ligand blotting (2). Both types of ligand specifically bind to two glycoproteins with molecular weights of 135 and 115 kD, respectively. The conditions of binding to these two proteins, however, markedly differ from those known for other lipoprotein receptors.Following extensive purification, these two species are still present at concentrations relative to each other that depend markedly on the conditions of purification. The purified, solubilized receptor was tested under various conditions, including in the absence and presence of calcium, after disulfide-reduction, and following chymotrypsin digestion. In parallel experiments, the same preparations were tested with respect to binding of fibrinogen, different lectins, and thealloantibody anti-PlAI . The results strongly support the assumption, that the two protein bands associated with lipoprotein binding are constituents of the GP-IIb/IIIa complex.These first results may have greatimplications for our understanding ofthe mechanism by which lipoproteins facilitate platelet stimulation.
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Bienz, D., T. Wager, and K. J. Clemetson. "ISOLATION AND CHARACTERIZATION OF HUMAN PLATELET MEMBRANE GLYCOPROTEINS Ia AND IIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643910.

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Glycoproteins (GP) Ia and IIa are relatively minor components of the platelet surface with similar molecular properties. Nieuwenhuis et al. (Nature 319, 470-72, 1985) described a patient whose platelets show no response to collagen. The correlating lack of GPIa in the platelets of this patient suggests this glycoprotein being the receptor for collagen. Santoro (Cell, 46, 913-20, 1986) described a 160 kDa glycoprotein that binds to collagen in the presence of MG2 + and is possibly identical with GPIa. The role of GPIIa is still unknown but a similar molecule has also been found on endothelial cells. It has been suggested that GPIa and GPIIa are complexed with a further membrane component GPIc. The two glycoproteins show only slight difference in molecular weight, isoelectric point and in their affinity for various lectins. As a result they coisolate using most separation techniques.GPIa is usually associated with the cytoskeleton while GPIIa is mostly found in the soluble phase. GPIa is dissociated from the cytoskeleton by addition of 2% SDS (final conc.) and sonication. Performing Triton X-114 phase partition, GPIIa is found in the detergent phase. After the detergents of the GPIa and GPIIa enriched protein solutions are exchanged with the non-ionic octanoyl-N-methyl glucamide, the glycoproteins are further purified by affinity chromatography on wheat germ agglutinin-Sepharose followed by Lens culinaris lectin-Sepharose both of which bind GPIa and GPIIa. A major contaminant during the purification is GPIb. Final purification of GPIa and GPIIa was obtained by preparative SDS-PAGE using electroelution into a membrane trap. Latest results show an enrichment of GPIa and a lack of GPIb in pseudopodes, isolated by the method of Rotman et al. (Proc. Natl. Acad. Sci. USA, 4357-61, 1982).
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Azevedo, Isa Maria Ferreira, Renally Barbosa Da Silva, Aryane De Azevedo Pinheiro, Rômulo Farias Carneiro, and Luiz Gonzaga Do Nascimento Neto. "AVALIAÇÃO DA ATIVIDADE ANTITUMORAL DA LECTINA ISOLADA DA ESPONJA MARINHA CHONDRILLA CARIBENSIS." In II Congresso Brasileiro de Ciências Biológicas On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1270.

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Introdução: O câncer é o nome dado a um conjunto de mais de 100 doenças que tem em comum o crescimento desordenado de células, as quais podem, inclusive, invadir outros tecidos, ocasionando alto índice de mortalidade, assim sendo estabelecido como um importante problema de saúde pública. Células tumorais apresentam alterações significativas na expressão de glicoproteínas em suas superfícies e sua detecção precoce é uma etapa definitiva para a cura durante o tratamento. Na busca por novas moléculas com potencial biotecnológico, vários estudos de prospecção têm sido realizados em habitats marinhos. Lectinas oriundas dos habitats marinhos demonstram relevante potencial biotecnológico, na qual várias atividades biológicas estão descritas na literatura. Tendo em vista a frequente expressão de padrões aberrantes de glicosilação nas células tumorais, as lectinas por serem proteínas com capacidade de ligação seletiva a carboidratos surgem como promissores agentes antineoplásicos. Objetivo: Este trabalho objetivou avaliar a atividade antitumoral da lectina isolada da esponja marinha Chondrilla caribensis (CCL) sobre células de carcinoma de próstata (LNCaP), bem como analisar o perfil de citotoxicidade da CCL sobre a linhagem de queratinócitos normais (HaCaT). Material e Métodos: O efeito citotóxico da CCL foi avaliado através do ensaio de viabilidade celular usando o método colorimétrico do sal tetrazolium MTS para as células das linhagens LNCaP e HaCaT. As linhagens celulares foram expostas a concentrações de 500 a 7,8 µg.ml-1 de CCL por 48 h. Resultados: Os resultados mostraram uma redução de 76,71% na viabilidade de LNCaP nas concentrações de 500, 250 e 125 µg.ml-1 (IC50 = 44,31 µg.ml-1). Para a linhagem celular HaCaT, o tratamento com CCL nas concentrações de 500, 250 e 125 µg.ml-1 resultou na redução da viabilidade em 28,64 %; 12,24 % e 0,76 %, respectivamente, onde 71,36 % ± 0,588 das células HaCaT permaneceram viáveis após 48 h de tratamento. Conclusão: Em conclusão, os resultados sugerem que a CCL possui maior seletividade para a linhagem LNCaP, e em contrapartida apresentou toxicidade reduzida sobre queratinócitos humanos saudáveis. Estudos adicionais devem ser realizados para investigar o mecanismo de ação da CCL sobre as células utilizadas no estudo.
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