Human basement membrane collagen (type IV)

Brazel, D; Pollner, Reinhold; Oberbäumer, Ilse; Kühn, Klaus

doi:10.1111/j.1432-1033.1988.tb13852.x

Cited by 90 publications

(40 citation statements)

References 44 publications

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“…Position numbers of the aligned al(1V) and a2(IV) chains are indicated. They do not coincide with the residue numbers of the single chains (Brazel et al, 1988). The dots above the amino acid sequence indicate every 10th position along the sequence.…”

Section: Purification Of Receptorsmentioning

confidence: 99%

“…The column was washed with 50 mh4 TrisMCl, pH 7.4, 300 mM NaC1,l mM MnCl,, containing 0.1 % reduced Triton X-100. Triton X-100 was exchanged against n-octylglucoside by washing the I G P K G F I G D P G I P - Brazel et al, 1988). The non-triple-helical interruption of al(1V) and a2(IV) are indicated by lines below and above the sequences, respectively.…”

Section: Purification Of Receptorsmentioning

confidence: 99%

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Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Kern

Eble

Golbik

et al. 1993

European Journal of Biochemistry

199

188

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The triple-helical cyanogen-bromide-derived fragment CB3 [IV] of collagen IV, located 100 nm from the N-terminus of the molecule, contains the binding sites for the integrins alp1 and a2pl. To investigate the interaction of these integrins and collagen IV, we performed solid-phase and inhibition assays using as receptor isolated alp1 and a2pl. The ligands used were the binding-site-bearing trimeric peptide CB3 [IV] and its shorter tryptic fragments Fl-F4. Using titration curves, in which the binding of soluble receptors to coated ligands and the binding of soluble ligands to coated receptors were analyzed, the binding sites for alp1 and a2pl were in different but adjacent areas of CB3 [IV]. Triple-helical conformation and distinct primary structures were required for the interaction. Dissociation constants (Kd), for the affinity of integrins for collagen IV, were determined in the 1-nM range in the presence of Mn2+ and Mg". In the absence of Mn2+, the Kd values indicated a 30-60-fold decrease in the affinities, which for a2pl was further reduced by adding Ca". In the presence of Ca2+ and Mg2+ the affinity of collagen IV for alp1 was four-times higher than for a2pl.

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Section: Purification Of Receptorsmentioning

confidence: 99%

Section: Purification Of Receptorsmentioning

confidence: 99%

Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Kern

Eble

Golbik

et al. 1993

European Journal of Biochemistry

199

188

View full text Add to dashboard Cite

show abstract

“…These include Gly to Ala substitutions and interruptions of the repeats by 2 -24 amino acid residues. In human collagen IV [15,19,28,29] there are 21 interruptions in the al(1V) and 23 in the a2(IV) chain and these match each other in location in most cases, giving rise to a total number of 25 triple-helical imperfections rather evenly distributed along the helix (Fig. 1).…”

Section: Monomer Structure and Sequencementioning

confidence: 99%

“…The disulfide-bonded loop in the center is unique for the a2(IV) chain. Based on [29,461; (a) is reproduced with permission from [29] and tetramers depends initially on noncovalent contacts followed by a concerted disulfide-exchange reaction which stabilizes the final products. The order of reactions of NCI or 7s segments in the self-assembly of collagen IV and whether these interactions are the first molecular recognition events is unknown.…”

Section: Oligorner Structuresmentioning

confidence: 99%

Structure and biological activity of basement membrane proteins

Timpl

1989

European Journal of Biochemistry

926

394

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Collagen type IV, laminin, heparan sulfate proteoglycans, nidogen (entactin) and SPARC) represent major structural proteins of basement membranes. They are well-characterized in their domain structures, amino acid sequences and potentials for molecular interactions. Such interactions include self-assembly processes and heterotypic binding between individual constituents, as well as binding of calcium (laminin, and are likely to be used for basement membrane assembly. Laminin, collagen IV and nidogen also possess several cell-binding sites which interact with distinct cellular receptors. Some evidence exists that those interactions are involved in the control of cell behaviour. These observations have provided a more defined understanding of basement membrane function and the definition of new research goals in the future.All multicellular animals possess various extracellular matrices. They determine body shape and stability, compartmentalization of organs and several cellular activities. These matrices include ubiquitously occurring basement membranes which are 20 -200-nm-broad deposits of some specific proteins in close proximity to epithelial, muscle, fat and nerve cells. Basement membranes are found in vertebrates and invertebrates except sponges and are produced as the first matrix during embryonic development. They are considered to control cell phenotype, tissue invasion of cells and filtration of macromolecules through glomeruli [I -41. This implies a defined supramolecular architecture for basement membranes and a distinct repertoire of biological activities expressed as the sum of their individual constituents. Yet, electron microscopy has so far revealed few details of basement membrane structure which, after staining, presents as two amorphous zones (the lamina lucida and the lamina densa) distinguished by different electron densities [5].Basement membranes are normally but not exclusively produced and deposited by cells which then remain in close contact with these structures. These contacts are mediated by specific cellular receptors which bind to some defined extracellular ligands [l -31. Other noncovalent molecular interactions maintain the matrix structure and covalent cross-links make basement membranes rather insoluble even in denaturing solvents. The increasing use of tumor models, such as the Engelbreth-Holm-Swarm (EHS) mouse tumor [6], which produce large amounts of soluble basement-membrane material has over the past decade allowed a comprehensive characterization of the major components. The progress in our understanding of the structure, biology and pathology of basement membranes 11-5 , 7 -101 as well as some methodological aspects [lo, 111 have been recently reviewed. The preCorrespondence to R . Timpl.

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“…Type IV collagen, the major component of the mammalian BM assembly, can be further divided into six distinct poly peptide chains designated as α1(IV) to α6(IV) and are encoded by six distinct genes, COL4A1 to COL4A6 20,21,22,23) . The self-association of type IV collagen triple-helical molecules, composed of three α chains, forms the supramolecular network of the BM.…”

Section: Introductionmentioning

confidence: 99%