Literature DB >> 3311751

Completion of the amino acid sequence of the alpha 1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain.

D Brazel1, I Oberbäumer, H Dieringer, W Babel, R W Glanville, R Deutzmann, K Kühn.   

Abstract

The cDNA and protein sequences of the N-terminal half of human basement membrane collagen (type IV) have been determined. Overlapping cDNA clones were constructed by repeated primer extension with synthetic oligonucleotides. They cover 2953 bp, beginning at the 5' end of the corresponding mRNA. At the protein level, the sequence of the cyanogen bromide peptide CB6 adjacent to the 7S domain has been additionally elucidated. The data presented here complete the protein sequence and nearly the entire cDNA sequence of the human alpha 1(IV) chain. The amino-terminal half of the alpha 1(IV) chain contains 8 cysteine residues involved in intramolecular and intermolecular cross-links. The entire triple-helical domain of alpha 1(IV) is interrupted by 21 non-triplet regions.

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Year:  1987        PMID: 3311751     DOI: 10.1111/j.1432-1033.1987.tb13450.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  19 in total

Review 1.  Alport syndrome, basement membranes and collagen.

Authors:  C E Kashtan; M M Kleppel; R J Butkowski; A F Michael; A J Fish
Journal:  Pediatr Nephrol       Date:  1990-09       Impact factor: 3.714

2.  Evolution of collagen IV genes from a 54-base pair exon: a role for introns in gene evolution.

Authors:  G Butticè; P Kaytes; J D'Armiento; G Vogeli; M Kurkinen
Journal:  J Mol Evol       Date:  1990-06       Impact factor: 2.395

3.  A novel chain of basement membrane-associated collagen as revealed by biochemical and immunohistochemical characterizations of the epitope recognized by a monoclonal antibody against human placenta basement membrane collagen.

Authors:  J Kino; E Adachi; T Yoshida; C Asamatsu; K Nakajima; K Yamamoto; T Hayashi
Journal:  Am J Pathol       Date:  1991-04       Impact factor: 4.307

4.  Nephritogenicity and alpha-chain composition of NC1 fractions of type IV collagen from bovine renal basement membrane.

Authors:  S Rauf; M Kagawa; Y Kishiro; S Inoue; I Naito; T Oohashi; M Sugimoto; Y Ninomiya; Y Sado
Journal:  Virchows Arch       Date:  1996-07       Impact factor: 4.064

5.  Molecular and ultrastructural studies of a fibrillar collagen from octocoral (Cnidaria).

Authors:  Joseph P R O Orgel; Ido Sella; Rama S Madhurapantula; Olga Antipova; Yael Mandelberg; Yoel Kashman; Dafna Benayahu; Yehuda Benayahu
Journal:  J Exp Biol       Date:  2017-07-13       Impact factor: 3.312

6.  NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.

Authors:  Jianxi Xiao; Xiuxia Sun; Balaraman Madhan; Barbara Brodsky; Jean Baum
Journal:  J Biol Chem       Date:  2015-07-24       Impact factor: 5.157

7.  Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.

Authors:  J Y Exposito; R Garrone
Journal:  Proc Natl Acad Sci U S A       Date:  1990-09       Impact factor: 11.205

8.  Antibodies to β1 integrins inhibit dendritic growth in rat sympathetic neurons.

Authors:  Pamela Lein; Dennis Higgins
Journal:  Biomed Res (Aligarh)       Date:  1996

9.  Establishment by the rat lymph node method of epitope-defined monoclonal antibodies recognizing the six different alpha chains of human type IV collagen.

Authors:  Y Sado; M Kagawa; Y Kishiro; K Sugihara; I Naito; J M Seyer; M Sugimoto; T Oohashi; Y Ninomiya
Journal:  Histochem Cell Biol       Date:  1995-10       Impact factor: 4.304

10.  Beta-sheet secondary structure of the trimeric globular domain of C1q of complement and collagen types VIII and X by Fourier-transform infrared spectroscopy and averaged structure predictions.

Authors:  K F Smith; P I Haris; D Chapman; K B Reid; S J Perkins
Journal:  Biochem J       Date:  1994-07-01       Impact factor: 3.857

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