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Cell adhesion proteins and α-fetoprotein. Similar structural motifs as prerequisites for common functions

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Abstract

This review summarizes and analyzes data on structural and functional relationships between cell adhesion proteins and α-fetoprotein (AFP), which play an important role in embryo-and carcinogenesis and act in synergism with growth factors. These two groups of proteins are mosaic, multimodular, and polyfunctional, and each of their modules can function independently through binding with its specific membrane receptor. Most cell adhesion proteins contain modules similar to epidermal growth factor (EGF) and also their repeats, which determine the involvement of these proteins in regulation of cell proliferation, differentiation, and apoptosis. These EGF-like modules are found to include short motifs similar to the fragment LDSYQCT of human AFP. Both direct and inverted AFP-like motifs are linked through a consensus octapeptide motif CXXGY/FXGX. Such AFP-like motifs of cell adhesion proteins and the tripeptide RGD found in AFP may be structural prerequisties for common functions of these groups of nonhomologous and unrelated proteins.

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Abbreviations

AFP:

α-fetoprotein

aa:

amino acid

BM:

basement membrane

ECM:

extracellular matrix

EGF:

epidermal growth factor

FAK:

focal adhesion kinase

ILK:

integrinlinked kinase

IGF:

insulin-like growth factor

MAPK:

mitogen-activated protein kinase

PDGF:

platelet-derived growth factor

PI-3K:

phosphatidylinositol-3-kinase

PKB:

protein kinase B

RGD:

arginyl-glycyl-aspartic acid

RTK:

receptor tyrosine kinase

TGF-α:

transforming growth factor-α

TNF-α:

tumor necrosis factor-α

VEGF:

vascular endothelial growth factor

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Original Russian Text © A. A. Terentiev, N. T. Moldogazieva, 2007, published in Biokhimiya, 2007, Vol. 72, No. 9, pp. 1133–1152.

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Terentiev, A.A., Moldogazieva, N.T. Cell adhesion proteins and α-fetoprotein. Similar structural motifs as prerequisites for common functions. Biochemistry Moscow 72, 920–935 (2007). https://doi.org/10.1134/S0006297907090027

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