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Secretogranin I/Chromogranin B Is a Heparin‐Binding Adhesive Protein
Author(s) -
Chen Ming,
Tempst Paul,
Yankner Bruce A.
Publication year - 1992
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1992.tb10042.x
Subject(s) - chromogranin a , neurite , extracellular matrix , hippocampal formation , microbiology and biotechnology , heparin , cell adhesion , chemistry , adhesion , in vitro , extracellular , binding protein , biochemistry , biology , cell , immunohistochemistry , immunology , neuroscience , organic chemistry , gene
The major heparin‐binding protein secreted by PC12 cells was purified from conditioned medium. Amino‐terminal sequencing of the purified protein identified it as secretogranin I/chromogranin B (SgI/ChmB). The protein showed the same electrophoretic mobility and biochemical characteristics as previously reported for SgI/ChmB and could be purified in high yield using a simple procedure. In vitro experiments demonstrated that SgI/ChmB effectively promoted cell‐substratum adhesion of NIH 3T3 and PC12 cells and supported neurite outgrowth in primary hippocampal neurons. Thus, SgI/ChmB may be a new member of the family of heparin‐binding extracellular matrix proteins that mediate cell adhesion and support neurite outgrowth.