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Gene Review

COL2A1  -  collagen, type II, alpha 1

Bos taurus

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Disease relevance of CB11


High impact information on CB11

  • Digestion with cyanogen bromide and trypsin yielded peptides which showed that approximately 30 additional amino acids were inserted at the equivalent of the amino acid at position 57 in the bovine 18.5K MBP sequence [6].
  • Reactivity of the antibodies with the carboxyterminal, cyanogen bromide fragment (CB-3) of R10 pilin allowed their classification into three groups [7].
  • Microsequencing of peptide fragments from a cyanogen bromide digest of p78 identified this protein as BiP and sequence analysis identified p74 as the peptidyl-prolyl cis-trans isomerase, FKPB65 [8].
  • To identify the posttranslational modifications responsible for this heterogeneity, a mixture of brain tubulins was treated with cyanogen bromide and the C-terminal fragments from the class III beta-tubulin isoforms were then isolated by binding them to the monoclonal antibody TuJ1 [9].
  • The protein glia maturation factor beta, isolated from bovine brain, has been sequenced by automated Edman degradation and tandem mass spectrometry of overlapped peptide fragments generated by cyanogen bromide cleavage and enzymatic digestion with trypsin, chymotrypsin, and endoproteinases Asp-N and Lys-C [10].

Chemical compound and disease context of CB11


Biological context of CB11

  • BN non-RT1 gene products moderated clinical arthritis but increased the levels of reactivity to CB11 in three strains carrying RT1l,n,av1 haplotypes [16].
  • Amino acid sequences coded by the other two clones, CB11 beta-7 and CB11 beta-20, were identical with that coded by a previously described cDNA, pcP-450(11 beta)-3 [Kirita et al. (1988) J. Biochem. 104, 683-686] [17].
  • Various deletion plasmids were constructed using the promoter region of CB11 beta-7, which is one of the two normal genes [18].
  • The nucleotide sequences revealed that three clones, CB11 beta-1, CB11 beta-3, and CB11 beta-21, were pseudogenes [17].
  • The induction rates of the recombinant plasmids carrying the promoters of normal genes, CB11 beta-7 and -20, were larger than those of pseudogenes, CB11 beta-1, -3, and -21 [17].

Anatomical context of CB11

  • The purpose of the study was to map the dominant T cell epitope of the CB11 sequence of CII in RTlu haplotype rats and to determine if, when used as a synthetic peptide, it would induce tolerance to protect against CIA [19].
  • The cDNA was isolated from a bovine adrenal gland cDNA library through the use of oligonucleotide probes whose sequences were based on partial amino acid sequence obtained from cyanogen bromide fragments of the purified cardiac enzyme [20].
  • The 125I-labeled CNBr II . DMPC complex also demonstrated high affinity, calcium-dependent saturable binding to solubilized bovine adrenal membranes [21].
  • The level of cross-linking between the polypeptide chains of the collagen molecules in bovine tendons of different ages has been assessed by measuring quantitatively through densitometry the changes in the ratios of individual cyanogen bromide peptides separated on polyacrylamide gels [22].
  • Preparation, isolation, and immunochemical studies of the cyanogen bromide peptides from a retinal photoreceptor cell autoantigen, S-antigen [23].

Associations of CB11 with chemical compounds


Physical interactions of CB11


Enzymatic interactions of CB11


Regulatory relationships of CB11

  • Conformational changes in the extradiscal regions of rhodopsin induced by illumination were investigated by modifying the visual pigment by mild treatment with cyanogen bromide prior to and after light exposure [32].
  • The peptide fragment of calcyclin, CNBr-3 (residues 1-57), digested with cyanogen bromide completely inhibited the interaction of native calcyclin with annexin XI, while CNBr-1 (residues 83-90) and CNBr-2 (residues 58-82) did not affect the binding [33].

Other interactions of CB11


Analytical, diagnostic and therapeutic context of CB11

  • Taken together, these findings indicate that multiple antibody-reactive epitopes on type II collagen may be instrumental in the initiation of collagen-induced arthritis in rats, particularly shared or cross-reactive epitopes located within CB11, CB9-7, CB12, and CB8 [39].
  • This evidence includes comigration during one-dimensional SDS-PAGE, cochromatography using ion exchange and hydrophobic matrices, similar isoelectric points, identical cyanogen-bromide peptide maps, and cochromatography of MAP kinase activity with the tyrosine-phosphorylated form of pp42 [40].
  • Gel filtration of a cyanogen bromide digest of the labeled beta subunit on Sephadex G-75 resolved a major 14C peak which contained 83% of the 14C recovered [41].
  • A single labeled cyanogen bromide peptide was isolated using reversed-phase high performance liquid chromatography [42].
  • One-dimensional peptide mapping following limited proteolysis under denaturing conditions or following cyanogen bromide cleavage demonstrates that the proteins are not closely related in primary structure [43].


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