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DJ Tweardy, M Sasaki, JJ Cardamone , JP McCoy , MJ Bonidie and AP Signorella
Department of Medicine, University of Pittsburgh School of Medicine, PA.
Laminin is a heterotrimeric glycoprotein that plays a central role in
promoting neutrophil chemotaxis, motility, and attachment to basement
membrane. Rabbit peritoneal exudate neutrophils stain positively for
laminin, which is presumed to be of exogenous origin and bound to laminin
receptors on the cell surface. We examined 32Dc13 cells, a murine
neutrophil precursor cell line, by immunoprecipitation. Northern blot
analysis, flow cytometry, and electron microscopy for the endogenous
production of laminin. Our results demonstrate that 32Dc13 cells
endogenously produce a laminin B2 chain protein and messenger RNA (mRNA)
without producing any detectable A or B1 chain protein or mRNA. The B2
chain protein was not secreted by the cells; rather it could be detected on
the cell surface after treatment of cells with neuraminidase. These
findings suggest the possibility of a novel role for the laminin B2 chain
in myeloid development and function.
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