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Human amnion epithelial cells assemble tenascins and three fibronectin isoforms in the extracellular matrix
Author(s) -
Linnala Auli,
Balzac Enrica,
Zardi Luciano,
Virtanen Ismo
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81494-k
Subject(s) - fibronectin , extracellular matrix , amnion , gene isoform , extracellular , microbiology and biotechnology , colocalization , glycoprotein , secretion , cell culture , monoclonal antibody , biology , chemistry , biochemistry , antibody , immunology , pregnancy , fetus , genetics , gene
Monoclonal antibodies (MAb) were used to show that cultured human amnion epithelial (HuA) cells produce tenascins (Tn) and isoforms of cellular fibronectin (cFn). Tn polypeptides of M r 280,000 and 190,000, assembled into extracellular matrix (ECM) but not secreted into the culture medium by HuA cells, were electrophoretically similar to those produced by human fibroblasts as revealed with domain‐specific MAbs. The results suggested that most Fn produced by HuA cells contained the extradomain (ED) A and an oncofetal domain but only a minor fraction EDB. In immunofluorescence Tn and Fn were seen in different cytoplasmie granules upon monensin‐induced intracellular accumulation. Tn appeared to be deposited in the ECM in colocalization with Fn but distinctly slower. The present results show that cultured normal human epithelial cells synthesize Tn and three isoforms of cFn and secrete them by using different cytoplasmie pathways.