J Schlessinger, A B Schreiber, A Levi, I Lax, T Libermann, Y Yarden
{"title":"Regulation of cell proliferation by epidermal growth factor.","authors":"J Schlessinger, A B Schreiber, A Levi, I Lax, T Libermann, Y Yarden","doi":"10.3109/10409238309102791","DOIUrl":"https://doi.org/10.3109/10409238309102791","url":null,"abstract":"<p><p>Epidermal Growth Factor (EGF) is a 6045 dalton polypeptide which stimulates the proliferation of various cell types in vitro and in vivo. EGF binds to diffusely distributed membrane receptors which rapidly cluster primarily on coated pits areas on the plasma membrane. Subsequently, the EGF-receptor complexes are endocytosed and degraded by lysosomal enzymes. The lateral diffusion coefficient (D) of EGF-receptor complexes on cultured cells increases gradually from D = 2.8 X 10(-10) cm2/sec at 5 degrees C to 8.5 X 10(-10) cm2/sec at 37 degrees C. In the same range of temperature the rotational correlation times change from 25 to 50 microseconds to approximately 350 microseconds. Hence, at 4 degrees C, the occupied EGF receptors translate and rotate rapidly in the plane of the membrane. At 37 degrees C, EGF receptors form microclusters composed of 10 to 50 molecules. Moreover, it is concluded that both at 4 degrees C and 37 degrees C lateral diffusion of the occupied receptors is not the rate determining step for either receptor clustering or internalization. EGF receptor is a 150,000 to 170,000 dalton glycoprotein. The receptor is in close proximity to an EGF-sensitive, cAMP-independent, tyrosine-specific protein kinase which also phosphorylates the receptor molecules itself. The EGF sensitive kinase is similar to the kinase activity which is associated with certain RNA tumor viruses. The fact that the non-mitogenic cyanogen-bromide cleaved EGF is as potent as native EGF in stimulating phosphorylation suggests that EGF-induced, protein phosphorylation is a necessary but insufficient signal for the induction of DNA synthesis by EGF. EGF receptor serves also as the binding site for Transforming Growth Factors (TGF) which compete with EGF and induce anchorage-independent growth of normal cells in soft agar. Tumor promoters such as phorbol ester effect the binding of EGF to its membrane receptors and its ability to stimulate DNA synthesis. EGF itself has also some tumor promoting activity. Hence, the membrane receptor for EGF seems to participate in the regulation of normal and neoplastic growth. Monoclonal antibodies against EGF receptor (IgM) induce various early and delayed effects of EGF, while their monovalent Fab' fragments are devoid of biological activity. These observations support the notions that EGF receptor rather than EGF itself is the active moiety and that the role of the hormone is to perturb the receptor in the appropriate way, probably by inducing the microaggregation of EGF receptors.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 2","pages":"93-111"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102791","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17363852","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Proton transfer in the catalytic mechanism of carbonic anhydrase.","authors":"D N Silverman, S H Vincent","doi":"10.3109/10409238309102794","DOIUrl":"https://doi.org/10.3109/10409238309102794","url":null,"abstract":"","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 3","pages":"207-55"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102794","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17374248","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Molecular biology of growth hormone.","authors":"A C Paladini, C Peña, E Poskus","doi":"10.3109/10409238309102800","DOIUrl":"https://doi.org/10.3109/10409238309102800","url":null,"abstract":"","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"15 1","pages":"25-56"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102800","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17380358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The design of biologically active polypeptides.","authors":"B Robson","doi":"10.3109/10409238309102796","DOIUrl":"https://doi.org/10.3109/10409238309102796","url":null,"abstract":"<p><p>On the one hand considerable advances are being made in the computer-aided calculation of polypeptide structure and behaviour, while on the other even very simple reasoning has lead to some apparent successes in the design and synthesis of biologically active peptides. While this looks extremely promising, there is a case for arguing that progress made in both these areas is to some degree illusory. Such criticisms as can be made, however, turn out to be highly constructive, suggesting a profitable and still workable approach to the problem of rational polypeptide design.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 4","pages":"273-96"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102796","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17418596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Glycoprotein synthesis and embryonic development.","authors":"W J Lennarz","doi":"10.3109/10409238309102795","DOIUrl":"https://doi.org/10.3109/10409238309102795","url":null,"abstract":"<p><p>One of the most striking morphogenetic events during embryonic development is gastrulation, a process that leads to formation of the primitive gut. Using sea urchin embryos, we have studied the synthesis and function of glycoproteins during gastrulation. These studies have revealed that at least three processes are induced prior to gastrulation: de novo synthesis of dolichol; phosphorylation of dolichol by dolichol kinase, which may catalyze the final step in the de novo pathway; and initiation of the synthesis of N-linked glycoproteins. Whether or not activation of the glycosylation process results merely because of the production of dolichyl monophosphate or because, in addition, proteins containing glycosylatable-Asn-X-Ser/Thr-sequences are first translated just prior to gastrulation, is currently being investigated.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 4","pages":"257-72"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102795","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17418595","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Conformational properties of the neurotoxins and cytotoxins isolated from Elapid snake venoms.","authors":"M J Dufton, R C Hider","doi":"10.3109/10409238309102792","DOIUrl":"https://doi.org/10.3109/10409238309102792","url":null,"abstract":"<p><p>The review will critically assess the information available on the conformation of homologous neurotoxins and cytotoxins isolated from Elapid snakes. Particular attention will be given to the dynamics of the molecules in solution because there is the possibility that defined intramolecular rearrangements are involved at the sites of action. Such properties will be then reconciled with the known X-ray crystallographic and sequence data in order to derive likely structure-activity relationships.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"14 2","pages":"113-71"},"PeriodicalIF":0.0,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238309102792","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17401513","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Affinity labeling via deamination reactions.","authors":"M L Sinnott","doi":"10.1080/10409238209104423","DOIUrl":"https://doi.org/10.1080/10409238209104423","url":null,"abstract":"<p><p>An electrophilic center at saturated carbon generated by the departure of molecular nitrogen shows minimum discrimination between various nucleophiles. The generation of such a center in the active site of a protein is therefore an attractive way of labeling that active site. The chemistry of deamination reactions will be discussed with respect to the practicality of triggering the deamination in the active sites of proteins. Successful applications of this principle using the N-nitrosamide functionality, the alkyl aryl triazene functionality, and the diazo functionality will be described. Reasons why active-site reagents incorporating this type of covert electrophilicity are more specific than those incorporating an overtly electrophilic center (such as -CO-CH2-Halogen) will be advanced. The actual and potential application of deamination precursors to the specific inhibition of physiological activities in living cells will be discussed.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"12 4","pages":"327-72"},"PeriodicalIF":0.0,"publicationDate":"1982-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238209104423","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17344876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The biosynthetic pathway of the asparagine-linked oligosaccharides of glycoproteins.","authors":"R J Staneloni, L F Leloir","doi":"10.1080/10409238209104422","DOIUrl":"https://doi.org/10.1080/10409238209104422","url":null,"abstract":"<p><p>This review deals with the structure and addition of the different types of oligosaccharides to asparagine residues in proteins. This process occurs in several steps, first an oligosaccharide which contains N-acetylglucosamine mannose and glucose is built up joined to dolichyl diphosphate. The oligosaccharide is then transferred to a polypeptide chain, loses its glucose, and is modified by removal of some monosaccharides and addition of others giving rise to a variety of saccharides.</p>","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"12 4","pages":"289-326"},"PeriodicalIF":0.0,"publicationDate":"1982-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238209104422","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17857857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The main types of organization of genetic material in eukaryotes.","authors":"Y V Ilyin, G P Georgiev","doi":"10.3109/10409238209108708","DOIUrl":"https://doi.org/10.3109/10409238209108708","url":null,"abstract":"","PeriodicalId":75744,"journal":{"name":"CRC critical reviews in biochemistry","volume":"12 3","pages":"237-87"},"PeriodicalIF":0.0,"publicationDate":"1982-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10409238209108708","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17344875","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}