scholarly journals Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity

1987 ◽  
Vol 241 (3) ◽  
pp. 923-928 ◽  
Author(s):  
A Garcia-Pardo ◽  
A Rostagno ◽  
B Frangione
Keyword(s):  
Human Plasma ◽  
Primary Structure ◽  
Terminal Segment ◽  
Molecular Heterogeneity ◽  
Heparin Binding ◽  
Plasma Fibronectin ◽  
Heparin Binding Site ◽  
Heparin Binding Domain ◽  
Polypeptide Chains

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.

scholarly journals Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin.

1985 ◽  
Vol 260 (22) ◽  
pp. 12136-12141 ◽  
Author(s):  
J Calaycay ◽  
H Pande ◽  
T Lee ◽  
L Borsi ◽  
A Siri ◽  
...  
Keyword(s):  
Human Plasma ◽  
Primary Structure ◽  
Binding Domain ◽  
Heparin Binding ◽  
Plasma Fibronectin ◽  
Heparin Binding Domain ◽  
Domain Iii

scholarly journals Structural domains of heparan sulphate for specific recognition of the C-terminal heparin-binding domain of human plasma fibronectin (HEPII)

1996 ◽  
Vol 317 (3) ◽  
pp. 871-877 ◽  
Author(s):  
Andrew WALKER ◽  
John T. GALLAGHER
Keyword(s):  
Human Plasma ◽  
Soft Tissues ◽  
Chondroitin Sulphate ◽  
Wide Spectrum ◽  
Heparan Sulphate ◽  
Binding Domain ◽  
Heparin Binding ◽  
Plasma Fibronectin ◽  
Heparin Binding Domain ◽  
And Migration

Heparan sulphate (HS) is an abundant polysaccharide component of the pericellular domain and is found in most soft tissues and all adherent cells in culture. It interacts with a wide spectrum of proteins including polypeptide growth factors and glycoproteins of the extracellular matrix. These interactions might influence fundamental cellular activities such as adhesion, growth and migration. HS might therefore represent a highly adaptive mechanism by which cells respond to their environment. The present study shows that the interaction between fibroblast HS, metabolically labelled with [3H]glucosamine, and the C-terminal heparin-binding domain of human plasma fibronectin (HEPII), is determined by distinct regions of the polysaccharide chain. By using a very sensitive affinity-chromatography method and specific polysaccharide scission it was shown that the HEPII-binding regions of HS reside within sulphated domains that are resistant to degradation by heparinase III. In addition, optimal binding was achieved with specific heparinase III-resistant fragments of 14–16 monosaccharides in length. The affinity of HS for HEPII was significantly decreased when the polysaccharide was cleaved with heparinase I. Chondroitin sulphate and dermatan sulphate were poor competitive inhibitors of [3H]HS binding to HEPII whereas unlabelled HS and heparin gave a strong inhibitory activity, with heparin being the most potent inhibitor. These findings suggest that the interaction between HEPII and HS is specific and requires extended sequences of seven to eight N-sulphated disaccharides in which a proportion of the iduronate residues are sulphated at C-2. The results have important implications for the functions of HS in cell adhesion and migration.

Structure Of Plasma Fibronectin. Gene Multiplication

1981 ◽  
Author(s):  
T E Petersen ◽  
H C Thøgersen ◽  
K Skorstengaard ◽  
K Vibe-Pedersen ◽  
P Sahl ◽  
...  
Keyword(s):  
Factor Xiiia ◽  
Acceptor Site ◽  
Heparin Binding ◽  
Plasma Fibronectin ◽  
Terminal Sequence ◽  
Heparin Binding Site ◽  
Cold Insoluble Globulin ◽  
Polypeptide Chains ◽  
Chymotrypsin A ◽  
Multiple Domain

Plasma fibronectin (cold insoluble globulin) is a multiple domain glycoprotein composed of two nearly identical disulphide bridged polypeptide chains with molecular weight of 220,000. It is a substrate for factor XIIIa and binds to gelatin and heparin. After digestion of bovine fibronectin with plasmin, four fragments with Mr 29,000, 170,000, 23,000 and 6,000 have been isolated. The N-terminal 29,000 Mr fragment (259 residues) has 10 disulphide bridges within five mutually homologous domains, called “fingers”. The sequence <Gln-Ala-Gln-Gln-Ile-Val-Gln-Pro-Gln- contains the acceptor site for factor XIIIa at position 3. The 170,000 Mr fragment contains both the gelatin and the heparin binding site. After further digestion with chymotrypsin a fragment (Mr 45,000) which binds to gelatin, and a fragment (Mr 30,000) which binds to heparin, have been isolated. The Mr 45,000 fragment consists of at least one more “finger” plus two other mutually homologous domains each with two disulphide bridges. The 23,000 Mr fragment (178 residues) consists of three “finger“- domains and has an N-terminal sequence Val-Arg-. The Mr 6,000 (C-terminal fragment) is a dimer of two identical 26-residue peptides linked by two disulphide bridges. 820 of the expected approx. 1800 residues have been placed in sequence.

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

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
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