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Nonmuscle Myosin Heavy Chain B Is Recognized by a Monoclonal Antibody that Inhibits GM1‐Enhanced Neuritogenesis
Author(s) -
Mummert Christine M.,
Schengrund CaraLynne
Publication year - 1997
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 - 10.1046/j.1471-4159.1997.68020596.x
Subject(s) - ganglioside , neurite , monoclonal antibody , myosin , antibody , microbiology and biotechnology , neuroblastoma , chemistry , in vitro , cell culture , biology , biochemistry , immunology , genetics
Addition of gangliosides to neuroblastoma cells maintained in vitro has been shown to enhance neuritogenesis. Although the mechanism by which they exert this effect is unknown, it has been postulated that they may act by adhering to cell surface proteins. In this article, we describe the isolation and identification of an S20Y murine neuroblastoma cell protein recognized by a monoclonal antibody that was prepared against putative GM1‐binding proteins and shown to inhibit GM1‐enhanced neuritogenesis. The protein identified was nonmuscle myosin heavy chain B, which appears to function in neurite formation but may not adhere to gangliosides.