Endogenous fibronectin of blood polymorphonuclear leukocytes: immunochemical characterization and subcellular localization

Experimental Cell Research
R SalcedoM Patarroyo

Abstract

Fibronectin, a large dimeric glycoprotein synthesized and secreted by several cell types, mediates cell adherence to surfaces. In infections and inflammatory responses, blood polymorphonuclear leukocytes (PMNs) adhere to cells and matrix proteins during extravasation and accumulation at inflammatory sites. The presence of fibronectin in blood PMNs has been poorly studied, and the characteristics and subcellular localization of this endogenous adhesive molecule are practically unknown. By immunofluorescence flow cytometry, purified rabbit antibodies and a monoclonal antibody to plasma fibronectin reacted with isolated blood PMNs, only after permeabilization of the cells. By Western blot analysis, the antibodies recognized, under reducing conditions, a protein with an apparent molecular mass of 230 kDa in the cell lysate. Eleven monoclonal antibodies to common frame fibronectin epitopes, including the RGD-containing cell-binding domain, also reacted with PMN fibronectin by Western blotting. In contrast, two antibodies to ED-A, the alternatively spliced region characteristic of "cellular" fibronectin, were unreactive, but recognized platelet fibronectin. On average, 1 million PMNs contained 6.8 ng +/- 1.4 (SD) of fibronectin, as m...Continue Reading

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Citations

May 7, 1999·Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology·G HalldénJ Lundahl
Jul 11, 2006·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Dejiang GaoAimin Yu
Jan 7, 2000·Experimental Cell Research·T GeberhiwotM Patarroyo
Aug 31, 1999·Immunopharmacology and Immunotoxicology·M A Panaro, V Mitolo
Jun 22, 2006·The Journal of Biological Chemistry·Kotaro SakamotoKazuhisa Sugimura

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