Literature DB >> 2753045

Crystallin gene expression during rat lens development.

H J Aarts1, N H Lubsen, J G Schoenmakers.   

Abstract

The analysis of the developmental pattern of the alpha A-, alpha B-, beta B1-, beta B2-, beta B3-, beta A3/A1-, and beta s-crystallin genes during fetal and postnatal development of the rat shows that the differential regulation of crystallin synthesis relies on differential gene shutdown rather than differential gene activation; that is, all crystallin genes are active during early development but turn off at different stages. The only two exceptions to this rule are the alpha B- and beta s-crystallin genes. The alpha B-crystallin gene transcript becomes first detectable at 18 days of fetal development, while the beta s-crystallin gene appears to be active only in the postnatal period. We also determined the absolute numbers of the alpha A-, alpha B-, beta B1-, beta B2-, beta B3-, beta A3/A1-, beta s-, and gamma-crystallin gene transcripts present in the lens at various times after birth. Comparison of these RNA data with the published protein data shows that the alpha B- and beta B2-crystallin RNAs are relatively overrepresented, suggesting the possibility that these two RNA species are not used as efficiently as other crystallin mRNAs. Examination of the known (hamster) alpha B-crystallin sequence and elucidation of the (rat) beta B2-crystallin sequence yielded no evidence for aberrant codon usage. These two RNAs have one sequence motif in common: they are the only crystallin mRNAs in which the translation initiation codon is preceded by CCACC.

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Year:  1989        PMID: 2753045     DOI: 10.1111/j.1432-1033.1989.tb14892.x

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


  23 in total

1.  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

Review 2.  Protein interactions in the calf eye lens: interactions between beta-crystallins are repulsive whereas in gamma-crystallins they are attractive.

Authors:  A Tardieu; F Vérétout; B Krop; C Slingsby
Journal:  Eur Biophys J       Date:  1992       Impact factor: 1.733

Review 3.  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

Review 4.  Overview of the Lens.

Authors:  J Fielding Hejtmancik; Alan Shiels
Journal:  Prog Mol Biol Transl Sci       Date:  2015-05-27       Impact factor: 3.622

5.  Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.

Authors:  Ishara A Mills; Shannon L Flaugh; Melissa S Kosinski-Collins; Jonathan A King
Journal:  Protein Sci       Date:  2007-09-28       Impact factor: 6.725

Review 6.  Biophysical chemistry of the ageing eye lens.

Authors:  Nicholas J Ray
Journal:  Biophys Rev       Date:  2015-08-23

7.  Tissue- and species-specific promoter elements of rat gamma-crystallin genes.

Authors:  R Peek; P van der Logt; N H Lubsen; J G Schoenmakers
Journal:  Nucleic Acids Res       Date:  1990-03-11       Impact factor: 16.971

8.  Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.

Authors:  Payel Das; Jonathan A King; Ruhong Zhou
Journal:  Proc Natl Acad Sci U S A       Date:  2011-06-13       Impact factor: 11.205

9.  A deletion mutation in the betaA1/A3 crystallin gene ( CRYBA1/A3) is associated with autosomal dominant congenital nuclear cataract in a Chinese family.

Authors:  Yanhua Qi; Hongyan Jia; Shangzhi Huang; Hui Lin; Jingzhi Gu; Hong Su; Tieying Zhang; Ya Gao; Lijun Qu; Dandan Li; Ying Li
Journal:  Hum Genet       Date:  2003-11-04       Impact factor: 4.132

10.  beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin.

Authors:  Payel Das; Jonathan A King; Ruhong Zhou
Journal:  Protein Sci       Date:  2010-01       Impact factor: 6.725

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