Literature DB >> 2912453

alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues.

S P Bhat1, C N Nagineni.   

Abstract

alpha-Crystallin, a tissue specific structural protein of the ocular lens, is known to be composed of two subunits, alpha A and alpha B. By using a specific antibody in an immunoblotting procedure we have found that one of the subunits, alpha B is present in a number of non-lenticular tissues including the retina, heart, skeletal muscle, skin, brain, spinal cord and lungs. Interestingly, in the rat, this protein is present in significantly higher concentrations in adult than in fetal tissues and, with the exception of the lens, fetal and adult heart has the highest concentration among the tissues examined. That the protein in question is, in fact, alpha B, was confirmed a) by the remarkable similarity of Staphylococcus aureus protease peptide maps of the protein in the heart and purified alpha-crystallin and b) by the sequence analysis of a rat heart cDNA clone identified by the alpha B antibody. Based on these observations we conclude that while alpha A has a tissue-specific role, alpha B is a polypeptide of independent function not restricted to the ocular lens.

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Year:  1989        PMID: 2912453     DOI: 10.1016/s0006-291x(89)80215-3

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  135 in total

1.  Exon shuffling mimicked in cell culture.

Authors:  A A van Rijk; W W de Jong; H Bloemendal
Journal:  Proc Natl Acad Sci U S A       Date:  1999-07-06       Impact factor: 11.205

2.  Characterization of alpha-crystallin-plasma membrane binding.

Authors:  B A Cobb; J M Petrash
Journal:  J Biol Chem       Date:  2000-03-03       Impact factor: 5.157

3.  Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation.

Authors:  S Goenka; B Raman; T Ramakrishna; C M Rao
Journal:  Biochem J       Date:  2001-11-01       Impact factor: 3.857

4.  Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of alphaB-crystallin.

Authors:  N P Shroff; S Bera; M Cherian-Shaw; E C Abraham
Journal:  Mol Cell Biochem       Date:  2001-04       Impact factor: 3.396

5.  Expression of betaB(2)-crystallin mRNA and protein in retina, brain, and testis.

Authors:  K S Magabo; J Horwitz; J Piatigorsky; M Kantorow
Journal:  Invest Ophthalmol Vis Sci       Date:  2000-09       Impact factor: 4.799

6.  Alpha-crystallin can function as a molecular chaperone.

Authors:  J Horwitz
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-01       Impact factor: 11.205

Review 7.  A superfamily in the mammalian eye lens: the beta/gamma-crystallins.

Authors:  G L van Rens; W W de Jong; H Bloemendal
Journal:  Mol Biol Rep       Date:  1992-02       Impact factor: 2.316

8.  AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells.

Authors:  Rajendra K Gangalum; Ivo C Atanasov; Z Hong Zhou; Suraj P Bhat
Journal:  J Biol Chem       Date:  2010-11-19       Impact factor: 5.157

Review 9.  Novel roles for α-crystallins in retinal function and disease.

Authors:  Ram Kannan; Parameswaran G Sreekumar; David R Hinton
Journal:  Prog Retin Eye Res       Date:  2012-06-18       Impact factor: 21.198

Review 10.  Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.

Authors:  Christine Slingsby; Graeme J Wistow
Journal:  Prog Biophys Mol Biol       Date:  2014-02-28       Impact factor: 3.667

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