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β 1 ‐Integrin‐Mediated Neuronal Responses to Extracellular Matrix Proteins
Author(s) -
TOMASELLI KEVIN J.
Publication year - 1991
Publication title -
annals of the new york academy of sciences
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1991.tb15600.x
Subject(s) - boulevard , citation , gateway (web page) , extracellular matrix , library science , integrin , computer science , cognitive science , world wide web , chemistry , psychology , biology , history , microbiology and biotechnology , biochemistry , cell , archaeology
Immunologic and biochemical studies demonstrate that beta 1-class integrin heterodimers mediate attachment and neurite outgrowth by primary neurons and neuronal cell lines in response to neurite-promoting ECM molecules. Individual cells are likely to express several alpha beta 1 integrins, each possessing unique ligand specificities. In some cases, a cell may express two beta 1 integrins that recognize different binding domains in a single ECM ligand, as appears to be the case for the alpha 3 beta 1 and alpha 1 beta 1 integrins on PC12 cells. Thus, the responses of a neuron to even a single ligand may be regulated by the combined action of several receptors. Finally, preliminary studies suggest that neurons can regulate the ligand specificity of individual integrin heterodimers (e.g., alpha 1 beta 1). Given the tremendous diversity in the extracellular matrix surrounding them, it is not surprising that neurons possess intrinsic factors that dictate if and how they respond to a particular ECM component.