Abstract
Fibronectin molecules are dimers composed of subunits whose primary structures may differ. This is due to alternative splicing in at least two regions (ED and IIICS) of the pre-mRNA. Using two monoclonal antibodies specific for two different epitopes of domain 5 (high affinity for heparin), we have quantitatively analyzed the expression of the IIICS sequence in human fibronectins from different sources. The results demonstrated that the percentage of fibronectin subunits containing the IIICS is higher in fibronectins from tumor-derived or simian virus 40-transformed human cells than in fibronectins from human plasma or normal human fibroblasts. Furthermore, we observed that 45-65% of fibronectin subunits from transformed cells or normal embryonic fibroblasts are sialylated on the heparin-binding domain 5, whereas this occurs in only 24-28% of fibronectin subunits from normal adult fibroblasts. On the contrary, no sialylation was observed on domain 5 in fibronectin from human plasma.
MeSH Terms
Amino Acid Sequence
Antibodies, Monoclonal
Cell Transformation, Neoplastic/metabolism
Fibronectins/genetics,immunology,metabolism
Humans
Neoplasms/metabolism
Peptide Fragments/immunology,metabolism
RNA Splicing
Sialoglycoproteins/metabolism
Simian virus 40
Thermolysin/metabolism
Chemicals
Antibodies, Monoclonal
Fibronectins
Peptide Fragments
Sialoglycoproteins
Thermolysin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Castellani P
Siri A
Rosellini C
Infusini E
Borsi L
Zardi L
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