Download e-book for kindle: Growth Factors, Differentiation Factors, and Cytokines by K. C. Oberg, A. Brown, G. Carpenter (auth.), PD Dr. Andreas
By K. C. Oberg, A. Brown, G. Carpenter (auth.), PD Dr. Andreas Habenicht (eds.)
Leading foreign specialists give a contribution to this option of stories protecting the merging fields of progress components, differentiation elements, and cytokines. those seem to play basic roles in a large choice of physiological and pathophysiological tactics that come with the legislation of development in common and malignant cells, embryogenesis, the immune reaction, wound therapeutic, irritation, and atherogenesis. the key facets of modern examine and improvement are mentioned, supplying an enormous replace during this pioneering field.
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Additional resources for Growth Factors, Differentiation Factors, and Cytokines
Mroczkowski, and R. Ball cules comprisding 1217 and 1207 amino acid residues, respectively (Gray et al. 1983; Scott et al. 1983; Bell et al. 1986). The mouse and human cDNA sequences representing the coding regions of prepro-EGF are fairly conserved, exhibiting approximtely 75% homology. These unexpectedly large precursor molecules contain a hydrophobic domain which may serve to anchor the precursor to the plasma membrane thus making it structurally analogous to a receptor. In the kidney where the EGF precursor does not undergo proteolytic processing, it is plausible, but not shown, that the precursor molecule functions as a receptor for a yet unidentified ligand (RaIl et al.
1986 Paulsson et at. 1987 Goustin et at. 1985 Aboud et at. 1987 Rapollee et at. 1988 Gerwin et at. 1987 Mercola et at. 1988 Noble et at. 1988; Raff et at. 1988; Richardson et at. 1988 Kartha et at. 1988 Reviewed by Raines et at. 1989a Reviewed by Heldin and Westermark, this volume expression of PDGF B-chain transcripts during the first trimester of pregnancy suggests an autocrine and/or paracrine role of PDGF in embryogenesis (Goustin et al. 1985). Such differential expression of PDGF dimers as well as of PDGF receptor(s) (see below) may reflect the potential to introduce considerable flexibility into the biology of PDGF and is likely to target the growth factor to those cell types that express a given pattern of PDGF receptors to which a given dimer preferentially binds.
1988). This raises the intriguing possibility that phospholipase C or a closely associated protein is one of the substrates of the EGF receptor tyrosine kinase and it is possible that this activity of EGF applies to PDGF as well. PDGF Has Multiple Effects on the Arachidonic Acid Cascade Another early activity of PDGF is the activation of a cascade of reactions whose net result is the formation of two biologically potent oxygenated products of arachidonic acid, prostacyclin and prostaglandin E2 (Habenicht et al.
Growth Factors, Differentiation Factors, and Cytokines by K. C. Oberg, A. Brown, G. Carpenter (auth.), PD Dr. Andreas Habenicht (eds.)