Epidermal growth factor precursor

If a single gene is cloned in sufficient quantity, it can be sequenced (see Deoxyribonucleic acid) and the amino acid sequence of the gene product can be predicted from the nucleotide sequence of the DNA. For example, the amino acid sequences of the insulin receptor, nicotinic and muscarinic cholinergic acetylcholine receptors, epidermal growth factor precursor and many (thousands) other proteins have been predicted in this way. 

Murakami, Y., S. Mizuno, and Y. Uehara. Accelerated degradation of 160 kDa epidermal growth factor (EGF) receptor precursor by the tyrosine kinase... 

All of the growth factors characterized so far are proteins (table 24.7). Many of them are cleaved from larger precursors. The 53-amino-acid epidermal growth factor (EGF) is cleaved from a precursor of 1,168 amino acids. This precursor is a membrane-spanning protein, with the EGF moiety and nine related sequences in the extracellular domain. EGF is homologous to several other growth factors,... 

The epidermal growth factor (EGF) subfamily of cytokines produced as large transmembranar precursor molecules containing at least one EGF domain in the extracellular region. This domain consists of at least two antiparallel P-strands connected to the intervening loops by three disulfide bonds. 

Gritti, A., Cova, L., Parati, E. A., Galli, R., and Vescovi, A. L., Basic fibroblast growth factor supports the proliferation of epidermal growth factor-generated neuronal precursor cells of the adult mouse CNS, Neurosci. Lett., 185, 151, 1995. 

Schematic representation of human LDL receptor showing five domains. The receptor mediates internalization of LDL and IDL by specific interaction of their B-lOO and E apoprotein moieties with two cysteine-rich negatively charged areas of domain 1. Domain 2 is homologous to epidermal growth factor (EGF) precursor, suggesting a possible evolutionary or functional relationship. [Reproduced with permission from M. S. Brown and J. L. Goldstein, A receptor-mediated pathway for cholesterol homeostasis. Science 232, 34 (1986).]...

The four common motifs found within the amino terminal regions of the proteinase precursors and proteinases are kringles, epidermal growth factor (EGF)-like motifs, fibronectin motifs, and apple motifs (Figure 36-5). The kringle is so named because in two dimensions, i.e., on paper prior to determination of its three-dimensional structure, it has the shape of a Danish pretzel. Similarly, apple motifs resemble drawings of apples. 

CHAPTER 36, FIGURE 5 Motif structures within coagulation proteins. Common motifs are found in the amino terminal regions of the proteinase precursor molecules. Shown are the kringle motifs and EGF-like motifs found in the vitamin K-dependent proteins and in plasminogen. Fibronectin (types I and II) motifs and apple motifs (named from their two-dimensional representations) are also present but not shown. Some epidermal growth factor-like domains contain P-hydroxylated Asp residues. The cartoon structures for the motifs are derived from three-dimensional structures determined by x-ray crystallography or by two-dimensional NMR spectroscopy. 

The epidermal growth factor (EGF) domain is one example of a module that is present in several proteins (Figure 3-8). EGF is a small, soluble peptide hormone that binds to cells in the embryo and in skin and connective tissue in adults, causing them to divide. It is generated by proteolytic cleavage between repeated EGF domains in the EGF precursor protein, which is anchored in the cell membrane by a membrane-spanning domain. EGF modules are also present in other proteins and are liberated by proteolysis these proteins include tissue plasminogen activator (TPA), a protease that is used to dissolve blood clots In heart attack victims ... 

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