Tissue distribution and subcellular localization of mammalian myosin I

Mark C. Wagner, Barbara Barylko, Joseph P. Albanesi

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Abstract

Myosin I, a nonfilamentous single-headed actin-activated ATPase, has recently been purified from mammalian tissue (Barylko, B., M. C. Wagner, O. Reizes, and J. P. Albanesi. 1992. Proc. Natl. Acad. Sci. USA. 89:490-494). To investigate the distribution of this enzyme in cells and tissues mAbs were generated against myosin I purified from bovine adrenal gland. Eight antibodies were characterized, five of them (M4-M8) recognize epitope(s) on the catalytic "head" portion of myosin I while the other three (M1-MS) react with the "tail" domain. Immunoblot analysis using antiadrenal myosin I antibody M2 demonstrates the widespread distribution of the enzyme in mammalian tissues. Myosin I was immunolocalized in several cell types including bovine kidney (MDBK), rat kidney (NRK), rat brain, rat phaeochromocytoma (PC12), fibroblast (Swiss 3T3), and CHO cells. In all cases, myosin I was concentrated at the cell periphery. The most intense labeling was observed in regions of the cell usually associated with motile activity (i.e., filopodia, lamellipodia and growth cones). These results are consistent with earlier observations on protozoan myosin I that suggest a motile role for the enzyme at the plasma membrane.

Original languageEnglish (US)
Pages (from-to)163-170
Number of pages8
JournalJournal of Cell Biology
Volume119
Issue number1
DOIs
StatePublished - Oct 1992

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ASJC Scopus subject areas

  • Cell Biology

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