Abstract

1. 1. Human amniotic fluid fibronectin (aFn) was studied by using a monoclonal antibody 52DH1 (DH) that recognizes the extra domain (ED-A) sequence of cellular Fn (cFn). 2. 2. In immunoblotting the DH antibody reacted with a sharp polypeptide band at the top of the bulk of the diffuse aFn. Another monoclonal antibody 52BF12 (BF) against the cell binding site of Fn, recognized the whole aFn. 3. 3. The ED-A sequence containing cFn (EcFn) formed a constant proportion in aFns from all amniotic fluid preparations studied. 4. 4. In amniotic membranes the DH antibody revealed bright subepithelial immunofluorescence. 5. 5. Also isolated and cultured human amnion epithelial cells were strongly positive in immunofluorescence 0and secreted EcFn into the culture medium as revealed by immunoblotting. 6. 6. The results indicate that aFn is a composition of at least two different Fn subtypes of which the EcFn most probably originates from amnion epithelial cells.

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