title: Secretogranin I/chromogranin B is a heparin-binding adhesive protein.
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.
authors.affiliation: Department of Neurology, Harvard Medical School, Boston, Massachusetts.
authors.forename: M
authors.initials: M
authors.lastname: Chen
authors.forename: P
authors.initials: P
authors.lastname: Tempst
authors.forename: B A
authors.initials: BA
authors.lastname: Yankner
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D002864:Chromogranins; D006493:Heparin / Q000378:metabolism*; D008969:Molecular Sequence Data; D016501:Neurites / Q000187:drug effects / Q000502:physiology; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology*; D014407:Tumor Cells, Cultured
chemical_list: D002864:Chromogranins; D011506:Proteins; D006493:Heparin