Primary structure of human plasma fibronectin — Characterization of the 6,000 dalton C-terminal fragment containing the interchain disulfide bridges

The primary structure of a 38 kDa heparin-binding domain from human plasma fibronectin has been determined. This domain contains 380 residues arranged in three type-III homology regions of approx. 90 residues each, and a 67-amino-acid C-terminal segment. This segment has been shown to be encoded by certain mRNA species only, due to alternative splicing [Kornblihtt, Vibe-Pedersen & Baralle (1984) Nucleic Acids Research 12, 5853-5868], and therefore represents a region of heterogeneity in fibronectin. Our data indicate that at least one of the constituent polypeptide chains contains this region.

Download Full-text

Primary structure of human plasma fibronectin. Characterization of a 31,000-dalton fragment from the COOH-terminal region containing a free sulfhydryl group and a fibrin-binding site.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)39250-5 ◽

1985 ◽

Vol 260 (18) ◽

pp. 10320-10325 ◽

Cited By ~ 3

Author(s):

A Garcia-Pardo ◽

E Pearlstein ◽

B Frangione

Keyword(s):

Binding Site ◽

Human Plasma ◽

Primary Structure ◽

Sulfhydryl Group ◽

Terminal Region ◽

Plasma Fibronectin ◽

Free Sulfhydryl Group

Download Full-text

Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)89554-0 ◽

1985 ◽

Vol 260 (4) ◽

pp. 2301-2306

Author(s):

H Pande ◽

J Calaycay ◽

D Hawke ◽

C M Ben-Avram ◽

J E Shively

Keyword(s):

Dna Binding ◽

Human Plasma ◽

Primary Structure ◽

Binding Domain ◽

Dna Binding Domain ◽

Plasma Fibronectin

Download Full-text

Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)44228-1 ◽

1983 ◽

Vol 258 (20) ◽

pp. 12670-12674 ◽

Cited By ~ 6

Author(s):

A Garcia-Pardo ◽

E Pearlstein ◽

B Frangione

Keyword(s):

Human Plasma ◽

Primary Structure ◽

Plasma Fibronectin ◽

Terminal Domain

Download Full-text

Immunochemical characterization of human plasma fibronectin

Biochemical Journal ◽

10.1042/bj1910719 ◽

1980 ◽

Vol 191 (3) ◽

pp. 719-727 ◽

Cited By ~ 20

Author(s):

M Vuento ◽

E Salonen ◽

K Salminen ◽

M Pasanen ◽

U K Stenman

Keyword(s):

Human Plasma ◽

Antigenic Structure ◽

Antigenic Determinants ◽

Proteolytic Degradation ◽

Plasma Fibronectin ◽

Native Protein ◽

Covalent Interaction ◽

Antigenic Activity ◽

Haemagglutinating Activity

Human plasma fibronectin has been purified by a non-denaturing affinity chromatography procedure [Vuento & Vaheri, (1979) Biochem.J. 183, 331–337], and antisera have been raised by immunizing rabbits with the native protein. The antisera reacted strongly with native fibronectin, but only weakly with reduced and alkylated fibronectin or with heat-denaturated fibronectin. Denaturation also affected the haemagglutinating and gelatin-binding activities of fibronectin and increased its susceptibility to proteolytic degradation. The antisera reacted with fragments of fibronectin obtained by proteolysis with plasmin. Large fragments (mol.wt. 180000–200000), lacking the region harbouring the interchain disulphide bridges but containing the sites responsible for gelatin-binding and haemagglutinating activity, showed as intense a reaction with the antisera as intact fibronectin. Smaller peptides showed a weaker reaction. All fragments tested showed sensitivity to denaturation in their reaction with the antisera. The results were interpreted as showing that: (1) native fibronectin has an ordered conformation that is easily perturbed by denaturation; (2) most of the antigenic determinants of the protein are dependent on conformation; (3) the region of the fibronectin molecule containing the interchain disulphide bridges has only few antigenic determinants; and (4) covalent interaction of the two subunits does not contribute to the antigenic structure recognized by rabbit antisera. The observed correlation between the antigenic activity and a structural and functional intactness of fibronectin suggests that the antibodies to native fibronectin could be used as a conformational probe in studies on this protein.

Download Full-text