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

1983 ◽  
Vol 258 (20) ◽  
pp. 12670-12674 ◽  
Author(s):  
A Garcia-Pardo ◽  
E Pearlstein ◽  
B Frangione
Keyword(s):  
Human Plasma ◽  
Primary Structure ◽  
Plasma Fibronectin ◽  
Terminal Domain

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 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 Thermal stability of human plasma fibronectin and its constituent domains.

1984 ◽  
Vol 259 (19) ◽  
pp. 11901-11907 ◽  
Author(s):  
K C Ingham ◽  
S A Brew ◽  
T J Broekelmann ◽  
J A McDonald
Keyword(s):  
Thermal Stability ◽  
Human Plasma ◽  
Plasma Fibronectin ◽  
Thermal Stability Of

scholarly journals Human plasma fibronectin as a substrate for human urokinase

1989 ◽  
Vol 262 (2) ◽  
pp. 529-534 ◽  
Author(s):  
L I Gold ◽  
R Schwimmer ◽  
J P Quigley
Keyword(s):  
Extracellular Matrix ◽  
Human Plasma ◽  
Plasminogen Activator ◽  
Early Event ◽  
Plasma Fibronectin ◽  
Proteolytic Digestion ◽  
Enzyme Substrate ◽  
Tumour Cell Invasion ◽  
Substrate Ratio ◽  
Dose Dependent

An early event in malignant transformation is the increased expression of proteases, such as plasminogen activator, which can degrade surrounding extracellular matrices, thereby conferring an advantage for tumour cell invasion and metastasis. The present studies provide evidence that plasma fibronectin (Fn), which is a component of the extracellular matrix, is a direct substrate for the plasminogen activator urokinase (UK). Human plasma Fn was incubated with human UK under plasminogen-free conditions. Fn cleavage was both time- and dose-dependent and was evident within 30 min. The proteolytic digestion was limited and complete within 12 h at an enzyme/substrate ratio of 1:20. Analysis of the final proteolytic digestion products demonstrated the disappearance of the native dimeric 440 kDa structure of Fn with the concomitant appearance of three proteolytic fragments of 210, 200 and 25 kDa. Since two large fragments of similar size to the 220 kDa monomeric chains of Fn were obtained following proteolysis, it is proposed that UK cleaves Fn at two sites, one towards the N-terminal and one close to the C-terminal, but N-terminal to its interchain disulphide bonds. These studies suggest that the local proteolytic digestion and release of Fn from the extracellular matrix by tumour cells possessing high levels of UK may involve the direct proteolytic breakdown of Fn by UK.

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