| Literature DB >> 1560226 |
M Chen1, P Tempst, B A Yankner.
Abstract
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.Entities:
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Year: 1992 PMID: 1560226 DOI: 10.1111/j.1471-4159.1992.tb10042.x
Source DB: PubMed Journal: J Neurochem ISSN: 0022-3042 Impact factor: 5.372