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Relevant bibliographies by topics / Epidermal growth factor; Peptide substrates

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Academic literature on the topic 'Epidermal growth factor; Peptide substrates'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Epidermal growth factor; Peptide substrates"

1

Guyer, C. A., R. L. Woltjer, K. J. Coker, and J. V. Staros. "Peptide Substrate Recognition by the Epidermal Growth Factor Receptor." Archives of Biochemistry and Biophysics 312, no. 2 (August 1994): 573–78. http://dx.doi.org/10.1006/abbi.1994.1347.

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Engel, Kate, Tomoaki Sasaki, Qi Wang, and John Kuriyan. "A highly efficient peptide substrate for EGFR activates the kinase by inducing aggregation." Biochemical Journal 453, no. 3 (July 12, 2013): 337–44. http://dx.doi.org/10.1042/bj20130537.

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Formation of an asymmetric dimer by the EGFR (epidermal growth factor receptor) kinase domains results in allosteric activation. Since this dimer does not readily form in solution, the EGFR kinase domain phosphorylates most peptide substrates with a relatively low catalytic efficiency. Peptide C is a synthetic peptide substrate of EGFR developed by others that is phosphorylated with a significantly higher catalytic efficiency, and we sought to understand the basis for this. Peptide C was found to increase EGFR kinase activity by promoting formation of the EGFR kinase domain asymmetric dimer. Activation of the kinase domain by Peptide C also enhances phosphorylation of other substrates. Aggregation of the EGFR kinase domain by Peptide C probably underlies activation, and Peptide C precipitates several other proteins. Peptide C was found to form fibrils independent of the presence of EGFR, and these fibrils may facilitate aggregation and activation of the kinase domain. These results establish that a peptide substrate of EGFR may increase catalytic activity by promoting kinase domain dimerization by an aggregation-mediated mechanism.

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TONG, KIRK, CHERYL A. GUYER, and JAMES V. STAROS. "Steric constraints in the recognition of peptide substrates for the epidermal growth factor receptor kinase." International Journal of Peptide and Protein Research 47, no. 3 (January 12, 2009): 219–26. http://dx.doi.org/10.1111/j.1399-3011.1996.tb01348.x.

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Campos-González, R., and J. R. Glenney. "Temperature-dependent tyrosine phosphorylation of microtubule-associated protein kinase in epidermal growth factor-stimulated human fibroblasts." Cell Regulation 2, no. 8 (August 1991): 663–73. http://dx.doi.org/10.1091/mbc.2.8.663.

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Treatment of normal human fibroblasts with epidermal growth factor (EGF) results in the rapid (0.5 min) and simultaneous tyrosine phosphorylation of the EGF receptor (EGFr) and several other proteins. An exception to this tyrosine phosphorylation wave was a protein (42 kDa) that became phosphorylated on tyrosine only after a short lag time (5 min). We identified this p42 kDa substrate as the microtubule-associated protein (MAP) kinase using a monoclonal antibody to a peptide corresponding to the C-terminus of the predicted protein (Science 249, 64-67, 1990). EGF treatment of human fibroblasts at 37 degrees C for 5 min resulted in the tyrosine phosphorylation of 60-70% of MAP kinase as determined by the percent that was immunoprecipitated with antiphosphotyrosine antibodies. Like other tyrosine kinase growth factor receptors, the EGFr is activated and phosphorylated at 4 degrees C but is not internalized. Whereas most other substrates were readily tyrosine phosphorylated at 4 degrees C, MAP kinase was not. When cells were first stimulated with EGF at 4 degrees C and then warmed to 37 degrees C without EGF, tyrosine phosphorylation of MAP kinase was again observed. Treatment of cells with the protein kinase C activator phorbol myristate acetate (PMA) also resulted in the tyrosine phosphorylation of MAP kinase, and again only at 37 degrees C. Tryptic phosphopeptide maps demonstrated that EGF and PMA both induced the phosphorylation of the same peptide on tyrosine and threonine. This temperature and PMA sensitivity distinguishes MAP kinase from most other tyrosine kinase substrates in activated human fibroblasts.

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Soler, C., and M. Soley. "Rapid and delayed effects of epidermal growth factor on gluconeogenesis." Biochemical Journal 294, no. 3 (September 15, 1993): 865–72. http://dx.doi.org/10.1042/bj2940865.

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Most reports on the effects of epidermal growth factor (EGF) on gluconeogenesis have indicated that such effects depend on the substrate used and are only observable after a lag time of 30-40 min. Recently, an immediate and transient effect of EGF on glucose synthesis was described in a perfused liver system. Here we extend the study of the effect of EGF on gluconeogenesis to isolated hepatocytes from fasted rats. The delayed effect of EGF on gluconeogenesis was studied by adding the substrate 40 min after the peptide. Under these conditions EGF increased glucose synthesis from pyruvate, decreased it when the substrate was lactate or glycerol and did not modify gluconeogensis from fructose or dihydroxyacetone. EGF did not affect the metabolic flux through glycolysis, determined as the production of lactate+pyruvate from 30 mM glucose. Furthermore, EGF did not modify the metabolic flux through pyruvate kinase, determined as the production of lactate+pyruvate from 1 mM dihydroxyacetone. The differing effects of EGF on gluconeogenesis depending on the substrate used can be explained by the effects of EGF on the cytosolic redox state (measured as the lactate/pyruvate ratio). About 20 min after the addition of EGF, the mitochondrial redox state (measured as the 3-hydroxybutyrate/acetoacetate ratio) decreased. This effect of EGF was blocked by ammonium, which also abolished the effect of the peptide on gluconeogenesis. Thus the effect of EGF at the mitochondrial level appears to be necessary for its effects on gluconeogenesis. Taken together, our results indicate that the delayed effects of EGF on gluconeogenesis are secondary to the effects of the peptide at both the mitochondrial and cytosolic levels. In addition to these delayed effects, we observed that EGF rapidly and transiently stimulated glucose synthesis from lactate, decreased the cytosolic redox state and increased oxygen consumption. All of these rapid effects required the presence of extracellular calcium and disappeared in the presence of rotenone, suggesting that this rapid effect of EGF on gluconeogenesis is secondary to the stimulation of mitochondrial respiration.

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Kracht, M., M. Shiroo, C. J. Marshall, J. J. Hsuan, and J. Saklatvala. "Interleukin-1 activates a novel protein kinase that phosphorylates the epidermal-growth-factor receptor peptide T669." Biochemical Journal 302, no. 3 (September 15, 1994): 897–905. http://dx.doi.org/10.1042/bj3020897.

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We have isolated from KB cells stimulated with interleukin-1 (IL-1) a protein kinase that phosphorylates a peptide (T669) based on the sequence around T669 of the epidermal growth factor (EGF) receptor. The enzyme, which had an apparent molecular mass of 45 kDa on gel-filtration chromatography, was purified 170,000-fold from cytosolic extracts by sequential chromatography on Mono Q, Mono S, phenyl-Sepharose, Superose 12, ATP-Sepharose and Mono Q. The enzyme activity co-chromatographed at the last step with a 45 kDa protein band that stained for phosphotyrosine. This peak fraction also contained some actin and a 60 kDa protein that stained weakly for phosphotyrosine. The T669 peptide is a substrate for mitogen-activated protein (MAP) kinase. Amounts of IL-1-induced T669 kinase and activated recombinant p42 MAP kinase having equal activity on T669 peptide were compared on commonly used MAP kinase substrates. T669 kinase was two or three orders of magnitude less active on myelin basic protein or microtubule-associated protein-2 than was MAP kinase. The IL-1-induced T669 kinase did not react with antiserum to p42/p44 MAP kinase. It was inactivated by treatment with protein phosphatase 2A or protein phosphotyrosine phosphatase 1B, so it may be regulated by dual phosphorylation in similar fashion to MAP kinase. The dephosphorylated enzyme was not re-activated by MAP kinase kinase. This novel enzyme could lie on a kinase cascade induced by IL-1. It may be responsible for phosphorylating T669 of the EGF receptor.

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Baron, V., N. Gautier, N. Rochet, R. Ballotti, B. Rossi, S. Saint-Pierre, E. Van Obberghen, and J. Dolais-Kitabgi. "Antibodies to insulin receptor tyrosine kinase stimulate its activity towards exogenous substrates without inducing receptor autophosphorylation." Biochemical Journal 260, no. 3 (June 15, 1989): 749–56. http://dx.doi.org/10.1042/bj2600749.

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Anti-peptide antibodies directed against a highly-conserved sequence of the insulin receptor tyrosine kinase domain have been used to study the relationship between this specific region and kinase activation. Antibodies have been prepared by the injection into a rabbit of a synthetic peptide (P2) corresponding to residues 1110-1125 of the proreceptor. The peptide exhibits 88-95% sequence similarity with the corresponding sequence in the v-ros protein and in receptors for epidermal growth factor and for insulin-like growth factor 1. Two antibodies with different specificities could be separated from total antiserum obtained after immunization with P2. One antibody [anti-(P-Tyr)] cross-reacted with phosphotyrosine and immunoprecipitated solely autophosphorylated receptors. This antibody was shown to increase or decrease the receptor tyrosine kinase activity depending on its concentration. In all circumstances receptor autophosphorylation and substrate phosphorylation were modulated in a parallel fashion. The second antibody (anti-P2) failed to immunoprecipitate the insulin receptor, but was found to interact with both the peptide and the receptor by e.l.i.s.a. assay. Using a tyrosine co-polymer we found that anti-P2 activated the insulin receptor kinase leading to substrate phosphorylation at a level similar to that observed with insulin. This effect was additive to the hormonal effect. In contrast, receptor autophosphorylation was not modified by the anti-peptide. The differential effect of this anti-peptide further supports the idea that receptor autophosphorylation and kinase activity towards exogenous substrates might be independently regulated. Finally, our data suggest that conformational changes in the receptor tyrosine kinase domain may be sufficient for activation of its enzymic activity.

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Pallen, C. J., D. S. Y. Lai, H. P. Chia, I. Boulet, and P. H. Tong. "Purification and characterization of a higher-molecular-mass form of protein phosphotyrosine phosphatase (PTP 1B) from placental membranes." Biochemical Journal 276, no. 2 (June 1, 1991): 315–23. http://dx.doi.org/10.1042/bj2760315.

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Purification of a major placental membrane protein phosphotyrosine phosphatase (PTP-I) through the use of a nonhydrolysable phosphotyrosine analogue affinity ligand has enabled identification of the enzyme as a single polypeptide of at least 46 kDa. This phosphatase specifically dephosphorylates phosphotyrosine-containing substrates, including the src peptide, the epidermal-growth-factor receptor tyrosine kinase and the non-receptor tyrosine kinase p56lck. The p56lck can be dephosphorylated by PTP-I at two tyrosine residues (Tyr-394 and Tyr-505), which are differentially phosphorylated in vitro and in vivo and have been suggested to modulate kinase activity. The activity of PTP-I towards these substrates indicates a possible function of regulation of cellular tyrosine phosphorylation pathways at the level of growth-factor receptor and/or oncogene/proto-oncogene tyrosine kinases. Kinetic analyses show that PTP-I exhibits a Km value of about 2 microM with either src peptide or reduced, carboxyamidomethylated and maleylated (RCM)-lysozyme as substrate, and is inhibited in a mixed competitive manner by the polyanions heparin and poly(Glu4,Tyr1). Sequencing of PTP-I peptides reveals almost complete identity with sequences within the N-terminal half of the 37 kDa non-receptor tyrosine phosphatase 1B. However, the size and amino acid composition of PTP-I are similar to that of a higher-molecular-mass form of PTP 1B predicted from cDNA cloning. These results suggest that the 37 kDa PTP 1B is a proteolysed form of PTP-I, and provide evidence that a larger form of PTP 1B exists in vivo, at least in association with placental membranes.

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Thompson, H. L., M. Shiroo, and J. Saklatvala. "The chemotactic factor N-formylmethionyl-leucyl-phenylalanine activates microtubule-associated protein 2 (MAP) kinase and a MAP kinase kinase in polymorphonuclear leucocytes." Biochemical Journal 290, no. 2 (March 1, 1993): 483–88. http://dx.doi.org/10.1042/bj2900483.

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Incubation of human polymorphonuclear leucocytes (PMN) with either the chemotactic factor N-formylmethionyl-leucylphenylalanine (FMLP) or phorbol 12-myristate 13-acetate (PMA) activates a kinase with phosphorylating activity towards a known microtubule-associated protein-2 (MAP) kinase substrate, the epidermal growth factor receptor peptide (T669). Activation of this enzyme by FMLP was maximal at 1 min, decreasing by 10 min. Activation by PMA was slightly slower than that by FMLP, but more prolonged (maximal at 5 min, with no significant decrease by 20 min). The enzyme induced by either stimulant bound strongly to phenyl-Sepharose, had a molecular mass of 40 kDa on gel filtration and phosphorylated three MAP kinase substrates, i.e. MAP, myelin basic protein and the T669 peptide. By use of antibodies to MAP kinases and phosphotyrosine, the enzyme was identified as the 42 kDa MAP kinase (also known as extracellular-signal-regulated kinase 2, ERK2). Stimulation of PMN with FMLP or PMA was also found to induce a kinase kinase which phosphorylated human recombinant MAP kinase on threonine and tyrosine, with concomitant activation. These results suggest that MAP kinase and the kinase kinase are involved in the activation of PMN by chemotactic factors such as FMLP.

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Hubler, L., P. S. Leventhal, and P. J. Bertics. "Alteration of the kinetic properties of the epidermal growth factor receptor tyrosine kinase by basic proteins." Biochemical Journal 281, no. 1 (January 1, 1992): 107–14. http://dx.doi.org/10.1042/bj2810107.

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Previous studies have shown that lysine- and arginine-rich proteins can enhance the activity of tyrosine and serine/threonine protein kinases. However, the kinetics and mechanism of this activation are not fully understood. Therefore we investigated the ability of poly(amino acids) and the arginine-rich protein, protamine, to alter the kinetic properties of epidermal growth factor (EGF) receptor protein-tyrosine kinase activity using immunoaffinity-purified receptor isolated from human epidermoid carcinoma (A431) cells. Poly(L-lysine), poly(L-arginine) and protamine stimulated EGF receptor kinase activity by 3-5-fold at non-saturating doses of ATP and peptide substrate, while poly(L-glutamate) had no effect. Initial kinetic studies demonstrated an increase in the maximum velocity and a decrease in the apparent Km for the peptide substrate angiotensin II in the presence of the basic effectors. Further analysis of the kinetic mechanism by product inhibition revealed that protamine altered the pattern of ADP inhibition towards the peptide substrate but not towards ATP. The change was indicative of the receptor's ability to form an enzyme-angiotensin II-ADP ternary complex in the presence of protamine but not in its absence. In addition, the basic effectors had a substantially decreased influence on the kinase activity of a C-terminally truncated form of the EGF receptor. Thus the changes in kinase activity may be partially mediated by the C-terminal region of the receptor, which contains the sites of receptor self-phosphorylation. These results suggest that the basic domains of proteins can interact with the EGF receptor to induce changes in its kinetic properties, especially with regard to reactant recognition and binding.

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Dissertations / Theses on the topic "Epidermal growth factor; Peptide substrates"

1

Page, Timothy C. M. "Mechanism based inhibitors of tyrosine kinases." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260163.

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Choudhury, Qamrul Ghani. "Control of arachidonic acid release by epidermal growth factor and lipocortin-1 in A549 cells." Thesis, Queen Mary, University of London, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.327127.

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Felton, Andrew. "Synthesis of peptide fragments of human epidermal growth factor by a new active ester method." Thesis, Oxford Brookes University, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.306385.

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Fredriksson, Anna. "Tracer development and PET studies : labeled proinsulin C-peptide and an EGFR-TK inhibitor /." Stockholm, 2002. http://diss.kib.ki.se/2002/91-7349-191-8.

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Bradford, Kathleen Ann. "The role of epidermal growth factor and parathyroid hormone related peptide (1-34) in three choriocarcinoma cell lines as a model for implantation of human trophoblast." Thesis, University of Southampton, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.395901.

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Greco, Gabriele [Verfasser]. "Regulation of the epithelial barrier in the rumen epithelium of sheep by incubation with single short-chain fatty acid at different pH, with glucagon-like peptide 1, glucagon-like peptide 2, and epidermal growth factor / Gabriele Greco." Berlin : Freie Universität Berlin, 2021. http://d-nb.info/123127610X/34.

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Pfeffer, Inga. "Interplay between 2-oxoglutarate oxygenases and cancer : studies on the aspartyl/asparaginyl-beta-hydroxylase." Thesis, University of Oxford, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.711703.

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Farias, Caroline Brunetto de. "BDNF/TrkB em câncer colorretal : interações funcionais com GRPR e EGFR." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2012. http://hdl.handle.net/10183/72306.

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BDNF/TrkB são descritos em diversas neoplasias onde iniciam sinais mitogênicos, facilitam o crescimento tumoral, previnem apoptose e regulam angiogênese e metástase. Outros fatores de crescimento também são importantes para tumorigênese, como GRP/GRPR e EGF/EGFR. O objetivo geral deste trabalho foi investigar o papel de BDNF/TrkB em câncer colorretal avaliando possíveis interações com GRPR e EGFR. Verificamos que BDNF e seu receptor, TrkB, estão presentes em amostras de pacientes com câncer colorretal esporádico, e os níveis de BDNF encontram-se mais elevados no tecido neoplásico que no tecido adjacente ao tumor. O tratamento com RC- 3095, um antagonista de GRPR, na linhagem celular de câncer colorretal humana, HT-29, causa diminuição nos níveis de NGF secretados pelas células e aumento de BDNF em relação ao controle não tratado. RC-3095 inibe a proliferação e viabilidade celular das linhagens HT-29 (EGFR positiva) e SW-620 (EGFR negativa), embora apenas em HT-29 ocorra um aumento significativo na expressão de mRNA de BDNF. Por isso, um anticorpo monoclonal anti-EGFR, cetuximabe, foi combinado a RC-3095, nas células HT-29, sendo capaz de prevenir tal aumento, sugerindo que este efeito seja mediado por EGFR. Os tratamentos com um inibidor de Trks, K252a (1000 nM) ou com cetuximabe (10 nM) também inibem a proliferação celular. Entretanto, a combinação de BDNF a cetuximabe previne este efeito, enquanto que a combinação de doses não efetivas de K252a (10 nM) à cetuximabe (1 nM) inibe a proliferação celular de HT- 29. Além disso, cetuximabe também causa aumento na expressão de mRNA de TrkB e BDNF, após 600 minutos de tratamento. Nossos resultados sugerem que a inibição da proliferação celular in vitro ou do crescimento tumoral in vivo devem acontecer através do bloqueio combinado entre GRPR e TrkB em células de câncer colorretal EGFR positivas, e que BDNF também esteja envolvido em mecanismos de resistência a fármacos. Por isso, o bloqueio de BDNF / TrkB pode emergir como potencial alvo antitumoral.
BDNF / TrkB are described in various cancers where they participate in tumor growth, apoptosis, angiogenesis and metastasis. Furthermore, other growth factors are also important to tumorigenesis as GRP/GRPR and EGF/EGFR. Therefore, the aim of this study was to investigate the role of BDNF/TrkB in colorectal cancer evaluating the interactions with GRPR and EGFR. We found that BDNF and its receptor, TrkB, are present in samples from patients diagnosed with sporadic colorectal cancer, and BDNF levels were higher in tumor tissue compared to adjacent tumor tissue. Treatment with RC-3095, GRPR antagonist, in human colorectal cancer cell line, HT-29 caused a decrease in NGF levels secreted by cells, and generated increase of BDNF when compared to untreated control. RC-3095 inhibited the proliferation and cell viability in HT-29 (EGFR positive) and SW-620 (EGFR negative), but only HT-29 cells showed a significant increase in BDNF mRNA expression. Therefore, a monoclonal anti-EGFR antibody, cetuximab was combined with RC-3095 in HT-29 cells, and was able to prevent such an increase, suggesting that this effect is mediated by EGFR. The treatment with a Trk inhibitor, K252a (1000 nM) or cetuximab (10 nM), inhibited cell proliferation. However, the combination of BDNF with cetuximab prevented this effect, whereas the combination of ineffective doses of K252a (10 nM) with cetuximab (1 nM) still inhibited cell proliferation of HT-29. Furthermore, cetuximab also caused an increase in BDNF and TrkB mRNA expression, 600 minutes after treatment. In summary, our results suggest that inhibition of cell proliferation in vitro or tumor growth in vivo must occur between the combination of GRPR and TrkB in EGFR positive colorectal cancer cells, and that BDNF is also involved in drug resistance mechanisms. Therefore, blockage of BDNF / TrkB may emerge as potential antitumor target.

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Puccio, François. "Influence de l'hydrocortisone, de l'egf, de la bombesine et du grf sur la proliferation cellulaire et la maturation du tractus gastrointestinal et du pancreas chez le jeune rat non sevre." Paris 6, 1988. http://www.theses.fr/1988PA066497.

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HSIAO, CHING-YI, and 蕭清懿. "Utilization of MelC1 signal peptide of Streptomyces spp. for secretory production of human epidermal growth factor." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/92604046462676141595.

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碩士
國防醫學院
微生物及免疫學研究所
96
Human epidermal growth factor (hEGF) has important biological functions and widely been used in clinical and cosmetic fields. Thus, production of hEGF in safe quality and in high quantity is desired. In this studies, MelC1 signal peptide of Streptomyces was fused with the gene of hEGF for secretory production in E. coli or in Streptomyces lividans 66. Under control of T7 promoter, pHL701/mel-hEGF was successfully expressed in cytosol of E. coli and the desired hEGF was secreted into medium as detected by western blotting and MALDI-TOF. It was found that mel-hEGF or hEGF encoded in pJNC101 or pJNC102 under control of snpA promoter was expressed in cytosol of S. lividan in low level and no evidence of extracellular secretion has been obtained based on western blotting. Failure of detecting secretory product could derive from low level of expression in cytosol. Recently discovered TAT pathway in E. coli could be the route for the secretory production of hEGF since Mel signal peptide of streptomyces belong to TAT family and Caf1 whoch belongs to SEC family was not able to bring about the secretory production of hEGF under similar circumstance. Also, it could be that strong T7 promoter drove a lot of expression of hEGF for MelC1 mediated secretion into medium.

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Book chapters on the topic "Epidermal growth factor; Peptide substrates"

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Mukku, Venkant R., John L. Kirkland, Tsu-Hui Lin, Russell B. Lingham, and George M. Stancel. "The Epidermal Growth Factor (EGF) Receptor." In Peptide Hormone Receptors, edited by M. Y. Kalimi and J. R. Hubbard, 335–84. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110850246-007.

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Carpenter, G., and M. I. Wahl. "The Epidermal Growth Factor Family." In Peptide Growth Factors and Their Receptors I, 69–171. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-49295-2_4.

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Carpenter, G., and M. I. Wahl. "The Epidermal Growth Factor Family." In Peptide Growth Factors and Their Receptors I, 69–171. New York, NY: Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4612-3210-0_4.

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Kageyama, Ryoichiro, and Glenn T. Merlino. "In vitro transcription of epidermal growth factor receptor gene." In Peptide Growth Factors Part C, 242–50. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)98025-2.

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Scott, James, Mark J. Selby, and Graeme I. Bell. "[17] Isolation of complementary DNA encoding mouse nerve growth factor and epidermal growth factor." In Peptide Growth Factors - Part B, 194–207. Elsevier, 1987. http://dx.doi.org/10.1016/0076-6879(87)47110-3.

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Lin, Peter H., Richard Selinfreund, and Walker Wharton. "Isolation of cell membrane for epidermal growth factor receptor studies." In Peptide Growth Factors Part C, 251–59. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)98026-3.

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Pepinsky, R. Blake. "Phosphorylation of lipocortin-1 by the epidermal growth factor receptor." In Peptide Growth Factors Part C, 260–72. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)98027-4.

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Nishikawa, Katsuzo, Yoshino Yoshitake, and Shigeru Ikuta. "[2] Derivation of monoclonal antibody to human epidermal growth factor." In Peptide Growth Factors - Part A, 11–22. Elsevier, 1987. http://dx.doi.org/10.1016/s0076-6879(87)46005-9.

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Mroczkowski, Barbara. "Expression of epidermal growth factor precursor cDNA in animal cells." In Peptide Growth Factors Part C, 175–85. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)98018-2.

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Gill, Gordon N., and Wolfgang Weber. "[7] Purification of functionally active epidermal growth factor receptor protein using a competitive antagonist monoclonal antibody and competitive elution with epidermal growth factor." In Peptide Growth Factors - Part A, 82–88. Elsevier, 1987. http://dx.doi.org/10.1016/s0076-6879(87)46010-2.

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Conference papers on the topic "Epidermal growth factor; Peptide substrates"

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Schleuning, W. D. "THE BIOCHEMISTRY AND CELL BIOLOGY OF SINGLE CHAIN UROKINASE TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642956.

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Urokinase was discovered in the late nineteenth century, as an enzymatic principle in urine, that initiates the dissolution of blood clots. The basis of this phenomenon was recognized more than fifty years ago as the activation of plasminogen, the precursor of a tryptic protease, then known as profibrinolysin. Despite this long history, detailed data on the biochemistry of plasminogen activation have only become available recently. Urokinase (now designated urokinase-type plasminogen activator : u-PA) is synthesized and secreted as a single chain polypeptide (Mr-: 53,000) by many cell types. Single chain u-PA (scu-PA) is with equal justification called prourokinase (pro-u-PA), notwithstanding its low catalytic activity for synthetic peptide substrates and plasminogen, as most proenzymes of proteases display a certain degree of activity. The structure of pro-u-PA has been elucidated by protein and cDNA sequencing. It consists of three domains, exhibiting characteristic homology to other proteins: a serine protease domain, homologous to trypsin, chymotrypsin and elastase; a kringle domain, likewise found in prothrombin, plasminogen, tissue-type plasminogen activator (t-PA) and Factor XII; and an epidermal growth factor (EGF)-like domain, found in many other proteins, including certain clotting factors. Pro-u-PA is activated by the cleavage of its LYS158-Ile159 h1 bY either plasmin or kallikrein. This cleavage leads to a high increase of Kcat values with respect to both plasminogen and synthetic peptide substrates, but apparently to a reduction of its affinity to plasminogen. Thrartoin inactivates pro-u-PA irreversibly by the cleavage of the Arg156-Phe157 bond. U-PA but not pro-u-PA rapidly forms ccnplexes with plasminogen activator inhibitors (PAI)-l and PAI-2: second order rate constants Kass are respectively > 107 and 0.9xl06 (M-11sec-1). Unknown enzymes process pro-u-PA and u-PA to low molecular weight (LMW) pro-u-PA and LMW u-PA (Mr: 33,000) by cutting off a fragment consisting of the kr ingle and the EGF—like region. Pro—u—PA mediated plasminogen activation is fibrin dependent in vivo, and to a certain degree in vitro. Hie biochemical basis of this fibrin specificity is at present uncertain, although there are reports indicating that it may require polyvalent cations. Through its EGF-like region HMW pro-u-PA and HMW u-PA are capable of binding to specific membrane protein receptors which are found on many cells. Thus, u-PA activity may be restricted to the cell surface. According to a recent report, binding of u—PA to the receptor may also mediate signal transduction in auto- or paracrine growth control. In cells permissive for the respective pathways, pro-u-PA gene transcription is stimulated by mechanisms of signal transduction, that include the cAMP, the tyrosine specific kinase and the protein kinase C dependent pathways. Glucocorticoid hormones downregulate pro-u-PA gene transcription in cells where the gene is canstitutively expressed. Although different cells vary greatly in their response to agents that stimulate urokinase biosynthesis, growth factors and other mitogens are in many cases effective inducers. Significantly elevated levels of u-PA are also found in many malignant tissues. These findings and many others suggest that plasminogen activation by u-PA provides localized extracellular matrix degradation which is required for invasive growth, cell migration and other forms of tissue remodelling. Fibrin represents in this view only a variant of an extracellular matrix, which is provided through the clotting system in the case of an emergency.

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2

Teshima, G., R. Harris, R. Keck, A. Meunier, J. Burnier, and B. Keyt. "CHARACTERIZATION OF LIMITED PROTEOLYTIC DIGESTS OF TISSUE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644375.

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Tissue plasminogen activator (tPA) is a single chain glycoprotein of 527 amino acids consisting of structural domains homologous to other plasma proteins ("finger","epidermal growth factor", "kringles" and "protease"). Unlike zymogens of other serine proteases, tPA in the single chain form (1-527), has amidolytic and fibrinolytic activity. However, the amidolytic activity is enhanced when tPA is cleaved by plasmin at the Arg275-Ile276 bond to yield the disulfide bonded two chain form. We used trypsin to study the structure and function of tPA by limited digestion. Aliquots of tPA (1 mg/ml) were digested at pH 7 with varying amounts of trypsin (1:10,000, 1:1000, 1:100 and 1:10; enzyme to substrate ratio). The dilute solutions of trypsin (1:10,000) were effective at completely converting one chain tPA to the two chain form, but little additional proteolysis was observed on SDS-PAGE. The proteolytic fragments of tPA were isolated by reduction and carboxymethylation (RCM), SDS gel electrophoresis and reversed phase HPLC. The RCM polypeptides were identified by amino acid composition and sequence. Specific antisera were prepared against peptide antigens of tPA including (1-27), (1-275), (276-527) and (502525). Immunoblotting experiments with the tryptic digests of tPA indicated that the region (1-275) is more susceptible to proteolytic attack than the protease (275-527). Specific cleavage sites were identified at positions 7, 10, 27 and 40. Partially digested tPA preparations were tested for enzymatic activity as determined by hydrolysis of the peptide substrate S-2288 or by clot lysis. Limited proteolysis at the amino terminus was correlated with significant loss of fibrinolytic . activity but minimal effect on the amidolytic activity. Increased tryptic digestion resulted in complete loss of amidolytic activity and significant reduction in antigenic activity as determined by polyclonal anti-tPA ELISA. These results areconsistent with the amino terminal "finger" domain being in part responsible for the fibrin-binding specificity of tPA. Limited tryptic digest of tPA, cleaves first at Arg-275, then subsequently cleaves the "finger" with associated loss of fibrinolytic activity.

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3

Frazier, D., Shu Wha Lin, J. Ware, Kenneth Smith, Howard Reisner, M. DeSerres, A. Wallmark, R. Ljung, I. M. Nilsson, and D. W. Stafford. "MAPPING OF 6 MONOCLONAL ANTIBODIES TO HUMAN FACTOR IX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643565.

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In order to map the regions of human factor IX recognized by monoclonal antibodies we have inserted random fragments of the coding region of the cDNA for human factor IX into the lambda phage expression vector, lambda gtll. The resultant recombinant phage were screened with monoclonal antibodies, the immunoreactive phage were isolated, and the DNA of the inserted fragment was sequenced to determine which amino acids were immunoreactive. This data, coupled with data obtained from the use of specific fragments of human factor IX expressed in E. coli from a T7 phage promoter, has allowed us to map the location of several epitopes on the surface of the factor IX molecule. In those cases where the antibodies are specific for human factor IX, additional narrowing of the epitope is possible by comparing the amino acid sequence of human factor IX to the bovine molecule. Six monoclonal antibodies from 3 different laboratories have been mapped. The immunodominant epitopes appear to be the amino terminus of the activation peptide, the amino terminus of the heavy chain and the epidermal growth factor domains.

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Giannelli, B. F. "MOLECULAR GENETICS OF HAEMOPHILIA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643981.

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Abstract:

Haemophilia B, an X-linked recessive disease with an incidence of 1/30,000 newborn males, is due to defects in the gene for coagulation factor IX, which is on the long am of the X chromosome at band Xq27.1. This gene consists of approximately 34 Kb and contains 8 exons which specify a mRtfc of 2803 residues coding for a protein of 415 aa preceded by a prepro signal peptide of 46 aa. Coripanson of the functional domains of the factor IX protein with the exon structure of the gene supports the exon/protein domain hypothesis of gene evolution. The factor IX gene seems to be formed by a number of functionally and evolutionally independent modules. The signal peptide and the gla (γcarboxy-glutamic) region encoded in the first three exons are homologous to those of factor X, protein C and prothrombin. Thevfourth and fifth exons which code for the connecting peptide are homologous to one another and to the epidermal growth factor, a module that has been used in the construction of a great variety of proteins including different members of the coagulation and fibrinolytic pathways. The sixth exon encodes the activation peptide region, while the catalytic region of factor IX is coded by the seventh and eighth exon. This is at variance with other serine protease genes that have different exons for the segments containing the cardinal ami no-acids of the active centre (histidine, aspartic acid and serine).Natural selection acts against detrimental mutations of the factor IX gene and at each generation a proportion of haemophilia B genes is eliminated, as a significant number of patients does not reproduce. There appears to be no selective advantage to the heterozygote and therefore haemophilia B is maintained in the population by new mutations. Consequently, a significant proportion of patients should be born to non-carrier mothers, and unrelated patients should carry different gene defects, as recently verified by detailed analysis of individual haemophilia B genes.The defects of factor IX described so far comprise both point mutations and gene deletions. The latter affect either part or the whole of the gene and are often associated with the development of antibodies against therapeutically adninistered factor IX (the inhibitor complication). Since gene deletions may result in the complete absenceof factor IX synthesis or in the production of an extremely abnormal product, it has been suggested that mutationspreventing the synthesis of a factor IX gene product capable of inducing immune tolerance to normal factor IX is important in predisposing to the inhibitor complication.Among the point mutations described so far, those affecting the signal peptide are of particular interest. Substitutions of the arginine at positions -4 and -1 cause failure of propeptide cleavage. Thus they indicate that the propeptide consists of 18 aa an(lthat lts excision is necessary for factor IX function. It appears also that the propeptide contains a signal for γcarboxylation which has been conserved during the evolution of different γcarboxylated proteins.In spite of coagulant treatment, haemophilia B is a serious disease and one for which genetic counselling is required. Paramount for this is the detection of carriers and the diagnosis ofaffected male fetuses. DNA probes derived from the cloned factor IX gene have been used for this purpose. Carrier and first or second trimester prenatal diagnoses have been done using factors IX gene markers to follow the transmission of haemophilia B genes. Six sequence variations causing restriction fragment length polymorphisms (RFLP) in the factor IX gene have been detected and used as markers for such indirect diagnoses The efficiency of the above markers is reduced by linkage disequilibrium but, nevertheless, they offer definite carrier and nremtal diagnoses in 75-80% of the relatives of familial cases of haemophilia B.The indirect detection of gene defects is of modest help in the counselling of individuals from the families of isolated patients, but new methods for the direct detection of gene mutations promise better results in such families and also the attainment of % diagnostic success in relatives of familial cases.Finally the successful expression of recombinant factor IX genes in tissue culture and transgenic mammals raises hopes of therapeutic advances.

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