Functional methionines in the collagen/gelatin binding domain of plasma fibronectin: Effects of chemical modification by chloramine T

Biochemistry ◽  
1993 ◽  
Vol 32 (32) ◽  
pp. 8168-8178 ◽  
Author(s):  
Allen M. Miles ◽  
Robert L. Smith
Keyword(s):  
Chemical Modification ◽  
Binding Domain ◽  
Plasma Fibronectin ◽  
Chloramine T

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

scholarly journals Probing the role of tryptophan residues in a cellulose-binding domain by chemical modification

1996 ◽  
Vol 5 (11) ◽  
pp. 2311-2318 ◽  
Author(s):  
Mark R. Bray ◽  
Neil R. Gilkes ◽  
Douglas G. Kilburn ◽  
R. Antony J. Warren ◽  
Lawrence P. Mcintosh ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Tryptophan Residues ◽  
Cellulose Binding

scholarly journals Collagen-binding domain of human plasma fibronectin contains a latent type-IV collagenase

1991 ◽  
Vol 201 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Smilja LAMBERT VIDMAR ◽  
Friedrich LOTTSPEICH ◽  
Istvan EMOD ◽  
Jean-Marie IMHOFF ◽  
Vera KEIL-DLOUHA
Keyword(s):  
Human Plasma ◽  
Binding Domain ◽  
Plasma Fibronectin ◽  
Type Iv Collagenase ◽  
Collagen Binding ◽  
Type Iv ◽  
Latent Type

Introduction of a specific binding domain on myoglobin surface by new chemical modification

2000 ◽  
Vol 82 (1-4) ◽  
pp. 133-139 ◽  
Author(s):  
Takashi Hayashi ◽  
Tsutomu Ando ◽  
Takaaki Matsuda ◽  
Hiroaki Yonemura ◽  
Sunao Yamada ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Specific Binding ◽  
Binding Domain

scholarly journals Human plasma fibronectin. Demonstration of structural differences between the A- and B-chains in the III CS region

1991 ◽  
Vol 274 (3) ◽  
pp. 731-738 ◽  
Author(s):  
T Tressel ◽  
J B McCarthy ◽  
J Calaycay ◽  
T D Lee ◽  
K Legesse ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rna Splicing ◽  
Single Gene ◽  
Cell Types ◽  
Binding Domain ◽  
Peptide Sequence ◽  
Heparin Binding ◽  
Plasma Fibronectin ◽  
Binding Domains ◽  
A Chain

Fibronectins are a class of cell-adhesion proteins produced from a single gene. The soluble plasma form is synthesized by hepatocytes and the insoluble cellular form by fibroblasts and other cell types. The proteins possess multiple binding domains for macromolecules including collagen, fibrin and heparin along with at least one cell-binding domain. Cellular as well as plasma fibronectins are dimers of similar but not identical polypeptides. Their differences are the result of internal amino acid sequence variability due to alternative RNA splicing in at least three regions (ED-A, ED-B and III CS). We have been studying this polymorphism at the protein level in plasma fibronectin (pFn). Cathepsin D-digested pFn applied to a heparin-agarose column and eluted with an NaCl stepwise gradient (0.1 M, 0.25 M and 0.5 M) released two polypeptides (75 kDa and 65 kDa) in the 0.5 M-NaCl peak. Immunoblots with monoclonal antibodies IST-2 (specific for the C-terminal heparin-binding domain) and AHB-3 (specific for the III CS domain) suggest that both peptides contain the C-terminal heparin-binding (Hep-2) domain, but that only the larger fragment possesses the III CS region. These two polypeptides (75 kDa and 65 kDa) were digested with trypsin, and the resulting peptides were analyzed by fast-atom-bombardment mass spectrometry and compared with the known cDNA-derived peptide sequence. Peptides that were unique to the III CS region were further characterized by micro sequence analysis. The 75 kDa fragment is derived from the A-chain and contains the III CS region (89 amino acid residues) along with the C-terminal heparin-binding (Hep-2) domain and the fibrin-binding (Fib-2) domain. A single galactosamine-based carbohydrate group was detected at Thr-73/74 of the III CS region present in the 75 kDa fragment. The 65 kDa fragment is derived from the B-chain and lacks the entire III CS region but does contain the Hep-2 and Fib-2 domains.

Effect of Lectins and Chemical Modification on the Hemagglutinin Activity of Human Plasma Fibronectin

1981 ◽  
Vol 36 (9-10) ◽  
pp. 863-868 ◽  
Author(s):  
Matti Vuento ◽  
Eija Salonen
Keyword(s):  
Chemical Modification ◽  
Human Plasma ◽  
Present Report ◽  
Red Cells ◽  
Carboxyl Groups ◽  
Plasma Fibronectin ◽  
Cell Surfaces ◽  
Serum Factors ◽  
Low Concentrations ◽  
Erythrocyte Surface

Abstract Purified hum an plasm a fibronectin has been shown to agglutinate protease-treated red cells [Vuento, Hoppe-Seyler's Z. Physiol. Chem. 360, 1327-1333, (1979)]. The present report shows that the activity is inhibited by low concentrations of lectins and by macrom olecular serum factors. Chemical m odification of carboxyl groups of fibronectin strongly inhibited the activity, but modification of am ino groups or guanidinium groups had little effect on the activity. The results suggest that fibronectin receptors on erythrocyte surface are carbohydrate-containing molecules. Humoral m acrom olecular factors may control the interaction of fibronectin with cell surfaces. Chemical m odification studies indicate that the parts of the fibronectin molecule responsible for the hem agglutinin activity are different from those mediating the binding of fibronectin to collagen.

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.

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