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Difference in interaction of fibronectin with type I collagen and type IV collagen

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
In our studies on fibronectin, difference in binding to type I collagen and type IV collagen was observed and analysed. Four different fragments, which consist of I6-II1-II2-I7-I8-I9, I6-II1-II2-I7, I6-II1-II2, and I8-I9 within the collagen binding domain, have been isolated from proteolytic digests of fibronectin.
M, Shimizu   +3 more
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Binding domain for laminin on type IV collagen

Biochemical and Biophysical Research Communications, 1985
Binding of type IV collagen to laminin was studied by attaching one member of the ligand pair to a solid phase. When laminin was bound to a solid phase, type IV collagen exhibited saturable binding. Digestion of type IV collagen with high concentrations of pepsin destroyed the laminin binding activity.
C N, Rao, I M, Margulies, L A, Liotta
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The life cycle of type IV collagen

Matrix Biology
Type IV collagen is a large triple helical molecule that forms a covalently cross-linked network within basement membranes (BMs). Type IV collagen networks play key roles in mechanically supporting tissues, shaping organs, filtering blood, and cell signaling.
Sandhya Srinivasan, David R. Sherwood
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Collagen type IV in epithelial tumours of colon

Acta Histochemica, 2002
Collagen type IV in the lamina propria mucosae is one of the main components of the basement membrane of normal and transitional colon mucosa. The aim of the present study was to assess the use of anti-collagen type IV antibodies in the evaluation of biological activity of epithelial tumours of the colon.
Stefan, Galbavý   +8 more
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Basement membrane (type IV) collagen

Matrix Biology, 1995
The collagen IV molecule is 400 nm long and consists of two alpha 1 (IV) and one alpha 2 (IV) chains. Their genes COL4A1 and COL4A2 form a transcription unit in which they are arranged head-to-head and connected by a short common promoter region. Recently, four additional genes have been discovered.
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A nonradioactive assay for type IV collagen degradation

Analytical Biochemistry, 1990
A sensitive assay for type IV collagen degradation using an avidin-biotin sandwich technique is described. Biotinylated type IV collagen is allowed to bind to an avidin-coated microtiter plate. The solution to be assayed is incubated with the biotinylated collagen bound to the avidin plate.
M J, Wilkinson, R L, Cohen, M A, Shuman
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The Involvement of Type IV Collagen in Goodpasture's Syndromea

Annals of the New York Academy of Sciences, 1985
Goodpasture's syndrome, involving lung and kidney, is considered to be caused by autoantibodies to basement membranes. This paper has described the isolation and identification of the antigen, which is isolated from collagenase digests of glomerular basement membrane, as a monomer protein of 26,000 daltons and two dimers of about 50,000 daltons ...
J, Wieslander, D, Heinegård
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Type IV collagenase and immunostaining of type IV collagen in human thyroid tumors

Auris Nasus Larynx, 2000
Required stages in the processes of malignant tumor invasion and metastasis are known to include the destruction of cell stroma and vascular basement membrane. It has been suggested that type IV collagenase can degrade type IV collagen, a main component of basement membrane.
T, Kusunoki   +5 more
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The presence of EC collagen and type IV collagen in bovine Descemet's membranes

Biochemical and Biophysical Research Communications, 1983
When bovine Descemet's membranes (DMs) were characterized after limited pepsinization the major component in DM was found to be endothelial cell (EC) collagen. Phenol extractions of the undigested pepsin residue recovered only type IV collagen. This study provides evidence that EC collagen may be produced by corneal endothelial cells in vivo.
U, Labermeier, M C, Kenney
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Type IV collagen and diabetic kidney disease

Nature Reviews Nephrology, 2019
A new genome-wide association study of patients with type 1 diabetes mellitus reveals novel loci that are associated with the development of diabetic kidney disease. The most significant of these loci encodes the α3 chain of type IV collagen, which is an important component of the glomerular basement membrane.
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