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-M3) 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.
MeSH Terms
Animals
Antibodies, Monoclonal/immunology
Cell Line
Cell Membrane/chemistry
Cytoplasm/chemistry
Fluorescent Antibody Technique
Hybridomas
Kidney/chemistry
Myosins/analysis,immunology
Neurons/chemistry
Rats
Chemicals
Antibodies, Monoclonal
Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wagner M C
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.
Barylko B
Albanesi J P
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