scholarly journals Identification of the NC1 Domain of α3 Chain as Critical for α3α4α5 Type IV Collagen Network Assembly

2010 ◽  
Vol 285 (53) ◽  
pp. 41874-41885 ◽  
Author(s):  
Valerie LeBleu ◽  
Malin Sund ◽  
Hikaru Sugimoto ◽  
Gabriel Birrane ◽  
Keizo Kanasaki ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Collagen Network ◽  
Type Iv ◽  
Nc1 Domain

scholarly journals Identification of a multifunctional, cell-binding peptide sequence from the a1(NC1) of type IV collagen.

1990 ◽  
Vol 111 (4) ◽  
pp. 1583-1591 ◽  
Author(s):  
E C Tsilibary ◽  
L A Reger ◽  
A M Vogel ◽  
G G Koliakos ◽  
S S Anderson ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Solid Phase ◽  
Peptide Sequence ◽  
Cell Binding ◽  
Type Iv ◽  
Specific Manner ◽  
Dose Dependent ◽  
Nc1 Domain

We have previously identified three distinctive amino acid sequences from type IV collagen which specifically bound to heparin and also inhibited the binding of heparin to intact type IV collagen. One of these chemically synthesized domains, peptide Hep-I, has the sequence TAGSCLRKFSTM and originates from the a1(noncollagenous [NC1]) chain of type IV collagen (Koliakos, G. G., K. K. Koliakos, L. T. Furcht, L. A. Reger, and E. C. Tsilibary. 1989. J. Biol. Chem. 264:2313-2323). We describe in this report that this same peptide also bound to intact type IV collagen in solid-phase assays, in a dose-dependent and specific manner. Interactions between peptide Hep-I and type IV collagen in solution resulted in inhibition of the assembly process of this basement membrane glycoprotein. Therefore, peptide Hep-I should represent a major recognition site in type IV collagen when this protein polymerizes to form a network. In addition, solid phase-immobilized peptide Hep-I was able to promote the adhesion and spreading of bovine aortic endothelial cells. When present in solution, peptide Hep-I competed for the binding of these cells to type IV collagen- and NC1 domain-coated substrata in a dose-dependent manner. Furthermore, radiolabeled peptide Hep-I in solution also bound to endothelial cells in a dose-dependent and specific manner. The binding of radiolabeled Hep-I to endothelial cells could be inhibited by an excess of unlabeled peptide. Finally, in the presence of heparin or chondroitin/dermatan sulfate glycosaminoglycan side chains, the binding of endothelial cells to peptide Hep-I and NC1 domain-coated substrates was also inhibited. We conclude that peptide Hep-I should have a number of functions. The role of this type IV collagen-derived sequence in such diverse phenomena as self-association, heparin binding and cell binding and adhesion makes Hep-I a crucial domain involved in the determination of basement membrane ultrastructure and cellular interactions with type IV collagen-containing matrices.

The 160k  1(IV) Chain, a Short Form of a Type IV Collagen Polypeptide, of Bovine Lens Capsule Retains the NC1 Domain

1996 ◽  
Vol 120 (1) ◽  
pp. 133-137 ◽  
Author(s):  
M. Iwata ◽  
Y. Sado ◽  
T. Sasaki ◽  
Y. Imamura ◽  
Y. Ninomiya ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Short Form ◽  
Lens Capsule ◽  
Bovine Lens ◽  
Type Iv ◽  
Nc1 Domain

scholarly journals Patients with Goodpasture's disease have two normal COL4A3 alleles encoding the NC1 domain of the type IV collagen  3 chain

2004 ◽  
Vol 19 (8) ◽  
pp. 2030-2035 ◽  
Author(s):  
U. Persson ◽  
J. M. Hertz ◽  
M. Carlsson ◽  
T. Hellmark ◽  
I. Juncker ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Type Iv ◽  
Goodpasture's Disease ◽  
Goodpasture’S Disease ◽  
Nc1 Domain

Sera from patients with anti-GBM nephritis including Goodpasture syndrome show heterogenous reactivity to recombinant NC1 domain of type IV collagen   chains

1996 ◽  
Vol 11 (11) ◽  
pp. 2215-2222 ◽  
Author(s):  
P. Dehan ◽  
M. Weber ◽  
X. Zhang ◽  
S. T. Reeders ◽  
J.-M. Foidart ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Goodpasture Syndrome ◽  
Type Iv ◽  
Nc1 Domain

Complexity of type IV collagens: from network assembly to function

2019 ◽  
Vol 400 (5) ◽  
pp. 565-574 ◽  
Author(s):  
Yuexin Wu ◽  
Gaoxiang Ge
Keyword(s):  
Type Iv Collagen ◽  
Network Formation ◽  
Basement Membranes ◽  
Structural Components ◽  
Collagen Network ◽  
Complex Type ◽  
Form Complex ◽  
Structural Support ◽  
Type Iv ◽  
Covalent Crosslinking

Abstract Collagens form complex networks in the extracellular space that provide structural support and signaling cues to cells. Network-forming type IV collagens are the key structural components of basement membranes. In this review, we discuss how the complexity of type IV collagen networks is established, focusing on collagen α chain selection in type IV collagen protomer and network formation; covalent crosslinking in type IV collagen network stabilization; and the differences between solid-state type IV collagen in the extracellular matrix and soluble type IV collagen fragments. We further discuss how complex type IV collagen networks exert their physiological and pathological functions through cell surface integrin and nonintegrin receptors.

scholarly journals Binding of laminin to type IV collagen: a morphological study.

1985 ◽  
Vol 100 (6) ◽  
pp. 1848-1853 ◽  
Author(s):  
A S Charonis ◽  
E C Tsilibary ◽  
P D Yurchenco ◽  
H Furthmayr
Keyword(s):  
Electron Microscopy ◽  
Morphological Study ◽  
Type Iv Collagen ◽  
Specific Binding ◽  
Terminal Region ◽  
The Other ◽  
Heat Denaturation ◽  
Type Iv ◽  
Nc1 Domain ◽  
Rotary Shadowing

A mixture of laminin and type IV collagen was analyzed by rotary shadowing using carbon/platinum and electron microscopy. Laminin was found to form distinct complexes with type IV collagen: one site of interaction is located 140 nm from the COOH-terminal, noncollagenous (NC1) domain and the other is located within the NH2-terminal region. The isolated NC1 fragment of type IV collagen does not appear to interact with laminin, while pepsin-treated type IV collagen, which lacks the NC1 domain, retains its ability to form complexes with laminin. Analysis of the laminin-type IV complexes indicates that laminin binds to type IV collagen via the globular regions of either of its four arms. This finding is supported by experiments using fragment P1 of laminin which lacks the globular regions and which does not bind to type IV collagen in a specific way. In addition, after heat-denaturation of laminin no specific binding is observed.

scholarly journals Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network.

1987 ◽  
Vol 105 (6) ◽  
pp. 2559-2568 ◽  
Author(s):  
P D Yurchenco ◽  
G C Ruben
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Thin Sheet ◽  
Great Part ◽  
Molecular Architecture ◽  
Branch Points ◽  
Collagen Network ◽  
Type Iv

To determine molecular architecture of the type IV collagen network in situ, the human amniotic basement membrane has been studied en face in stereo relief by high resolution unidirectional metal shadow casting aided by antibody decoration and morphometry. The appearance of the intact basement membrane is that of a thin sheet in which there are regions of branching strands. Salt extraction further exposes these strands to reveal an extensive irregular polygonal network that can be specifically decorated with gold-conjugated anti-type IV collagen antibody. At high magnification one sees that the network, which contains integral (9-11 nm net diameter) globular domains, is formed in great part by lateral association of monomolecular filaments to form branching strands of variable but narrow diameters. Branch points are variably spaced apart by an average of 45 nm with 4.4 globular domains per micron of strand length. Monomolecular filaments (1.7-nm net diameter) often appear to twist around each other along the strand axis; we propose that super helix formation is an inherent characteristic of lateral assembly. A previous study (Yurchenco, P. D., and H. Furthmayr. 1984. Biochemistry. 23:1839) presented evidence that purified murine type IV collagen dimers polymerize to form polygonal arrays of laterally as well as end-domain-associated molecules. The architecture of this polymer is similar to the network seen in the amnion, with lateral binding a major contributor to each. Thus, to a first approximation, isolated type IV collagen can reconstitute in vitro the polymeric molecular architecture it assumes in vivo.

Crystals of the NC1 domain of human type IV collagen

1990 ◽  
Vol 211 (4) ◽  
pp. 683-684 ◽  
Author(s):  
Milton Stubbs ◽  
Lesley Summers ◽  
Irmgard Mayr ◽  
Monika Schneider ◽  
Wolfram Bode ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Human Type ◽  
Type Iv ◽  
Nc1 Domain

scholarly journals A novelCOL4A1frameshift mutation in familial kidney disease: the importance of the C-terminal NC1 domain of type IV collagen

2016 ◽  
Vol 31 (11) ◽  
pp. 1908-1914 ◽  
Author(s):  
Daniel P. Gale ◽  
D. Deren Oygar ◽  
Fujun Lin ◽  
P. Derin Oygar ◽  
Nadia Khan ◽  
...  
Keyword(s):  
Kidney Disease ◽  
Type Iv Collagen ◽  
Type Iv ◽  
Nc1 Domain
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