alphaB-crystallin is the structural protein of vertebrate lens, which is widely expressed in non-lens tissue. As one of the heat shock protein family members, alphaB-crystallin possesses biological properties of molecular chaperones and anti-apoptotic effects. Multi-factor injuries, such as retinopathy, inflammation and nervous system diseases, have a closely relationship with alphaB-crystallin. This paper reviews the research progress of the expression and mechanism of alphaB-crystallin in retina and extraocular tissues and organs.
Crystallins ; Gene Expression Regulation, Developmental ; Heat-Shock Proteins/metabolism* ; Humans ; Lens, Crystalline ; Retina ; alpha-Crystallin B Chain/metabolism*

<b>OBJECTIVEb>To identify the disease-causing gene mutations in three Chinese pedigrees affected with congenital inherited cataract, in ordre to provide genetic counseling and prenatal diagnosis.

<b>METHODSb>Using exons combined target region capture sequencing chip to screen the candidate disease-causing mutations, Sanger sequencing was used to confirm the disease-causing mutations.

<b>RESULTSb>Family 1 was polymorphic cataract, family 2 was cerulean cataract, family 3 was coralliform cataract. The inheritance mode of the three pedigrees consisted with autosomal dominant inheritance. In family 1, a nonsense mutation of CRY&beta;B2 gene c.463C>T in exon 6 result in a p.Q155X amino acid change. In family 2, a missense mutation of of CRYGD gene c.43C>T in exon 2 result in a p.R14C amino acid change. In family 3, a missense mutation of CRYGD gene c.70C>A in exon 2 result in a p.P23T amino aid change. No above-mentioned mutations were found in normal individuals.

<b>CONCLUSIONb>The nonsense mutation c.463C>T (p.Q155X) of CRY&beta;B2 gene, the heterozygous mutations c.43C>T(p.R14C) of CRYGD gene and c.70C>A( p.P23T) of CRYGD gene was the disease-causing gene mutation in family 1, 2 and 3 respectively, our results provid genetic counseling and prenatal diagnosis for these three families.

Cataract ; genetics ; Genetic Counseling ; Humans ; Mutation ; Pedigree ; Prenatal Diagnosis ; beta-Crystallin B Chain ; genetics ; gamma-Crystallins ; genetics

<b>OBJECTIVEb>To identify the genetic defect causing automosal dominant congenital cataracts (ADCC) with nuclear opacities in a Chinese pedigree.

<b>METHODSb>Linkage analysis was carried out with the short tandem repeat polymorphisms flanking the candidate genes. Mutation analysis of the candidate gene in the critical region was performed to detect the potential mutation.

<b>RESULTSb>The cataract locus in this pedigree was mapped to 17q11.1-12, an 11.78 cM interval between markers D17S933 and D17S 1288. By means of sequencing the candiate gene, betaA1-crystallin (CRYBA1), a deletion mutation DeltaG91 in exon 4 was detected. This change cosegregated with the patients in the family but was not found in 50 normal unrelated individuals.

<b>CONCLUSIONb>It is a deletion mutation DeltaG91 of CRYBA1 gene that causes autosomal dominant congenital nuclear cataract. This is the first report of an autosomal dominant congenital nuclear cataract caused by the mutation in this gene.

Cataract ; congenital ; genetics ; Crystallins ; genetics ; Gene Deletion ; Genetic Linkage ; Humans ; Mutation ; Polymerase Chain Reaction ; beta-Crystallin A Chain

The present study was performed to evaluate the effect of tetracycline-HCL on the change of implant surface microstructure according to application time. Implant with pure titanium machined surface, double coated FBR(R) surface and oxidized CellNest surface were utilized. Implant surface was rubbed with 50mg/ml tetracycline-HCL solution for 1/2, 1, 1 1/2, 2 and 2 1/2min. respectively in the test group. Then, specimens were processed for scanning electron microscopic observation. The results of this study were as follows. 1. Both test and control group showed a few shallow grooves and ridges in pure titanium machined surface implants. There were not significant differences between two groups. 2. The double coated FBR(R) surfaces showed fine crystalline structures. The roughness of surfaces conditioned with tetracycline-HCL was lessened relative to the application time. 3. The oxidized CellNest surfaces showed the porous structures. The surface conditioning with tetracycline-HCl influenced on its micro-morphology. In conclusion, the detoxification of the affected implant surface with 50mg/ml tetracycline-HCL should be applied respectively with different time according to various implant surfaces.
Crystallins ; Titanium

<b>OBJECTIVEb>To detect the disease-causing mutation in a pedigree affected with autosomal dominant congenital cataract.

<b>METHODSb>Genomic DNA was extracted and purified from peripheral blood samples from members of the pedigree and 100 healthy controls. Coding regions of 18 candidate genes were screened with PCR and Sanger sequencing. Identified mutations were verified among 100 healthy individuals to exclude single nucleotide polymorphisms.

<b>RESULTSb>A heterozygous nonsense mutation c.471G>A of the CRYGD gene, which resulted in p.Trp157Term, was identified in all three patients. The same mutation was not found in the two normal individuals from the family and 100 healthy controls. The nonsense mutation was predicted to be "disease causing" by Mutation t@sting program.

<b>CONCLUSIONb>The nonsense mutation c.471G>A of the CRYGD gene probably underlies the congenital cataract in the pedigree.

Cataract ; etiology ; genetics ; Child ; Codon, Nonsense ; Humans ; Male ; Sequence Analysis, DNA ; gamma-Crystallins ; genetics

OBJECTIVE: To explore the genetic basis for a Chinese pedigree affected with congenital cataracts. METHODS: Clinical data and peripheral blood samples were collected for the pedigree. Following extraction of genomic DNA, whole exome sequencing was carried out to detect genetic variants. Candidate variants were verified by familial co-segregation analysis and Sanger sequencing. Bioinformatics analysis was carried out to predict the function of mutant genes. RESULTS: By comparing variants identified among affected and unaffected individuals, a heterozygous variant, c.110 G>C (p.R37P), was identified in exon 2 of the CRYGC gene among all patients, which also matched the criteria for potential disease-causing mutations. The result was confirmed by Sanger sequencing. CONCLUSION The c.110G>C variant of the CRYGC gene probably underlay the congenital cataracts in this pedigree.
Asian Continental Ancestry Group ; Cataract ; congenital ; genetics ; China ; Heterozygote ; Humans ; Mutation ; Pedigree ; gamma-Crystallins ; genetics

<b>OBJECTIVEb>To observe the correlation of gammaD-crystallin P23T mutant with lens ultrastructure of the hereditary coralliform cataract.

<b>METHODSb>Complete ophthalmologic examinations were performed before lens extraction and lens samples were studied by transmission and scanning electric microscope respectively. Protein molecular modeling was performed using SWISS-MODEL(version 2.0).

<b>RESULTSb>Protein structure modeling demonstrated that the mutant caused a decrease in molecular final total energy and changes in the surface structure of gammaD-crystallin. Ultrastructure study revealed crystals deposited in lens, extensive granules dispersed in uncommon oval structure and the disorganization of lens epithelial cells.

<b>CONCLUSIONb>It is possible that the gammaD-crystallin P23T mutant is associated with abnormal crystals in lens and disorganization of lens epithelial cells.

Cataract ; congenital ; genetics ; pathology ; Female ; Humans ; Lens, Crystalline ; ultrastructure ; Male ; Pedigree ; Phenotype ; Point Mutation ; gamma-Crystallins ; genetics

<b>BACKGROUNDb>Gammad-crystallin plays an important role in human cataract formation. Being highly stable, gammaD-crystallin proteins are composed of two domains. In this study we constructed and analyzed protein models of the mutant gammaD-crystallin gene, which caused a special fasciculiform congenital cataract affecting a large Chinese family.

<b>METHODSb>gammaD-crystallin protein structure was predicted by Swiss-Model software using bovine gammaD-crystallin as a template and Prospect software using human betab2-crystallin as a template. The models were observed with a Swiss-Pdb viewer.

<b>RESULTSb>The mutant gammaD-crystallin structure predicted by the Swiss-Model software showed that proline23 was an exposed surface residue and P23T change made a decreased hydrogen bond distance between threonine23 and asparagine49. The mutant gammaD-crystallin structure predicted by the Prospect software showed that the P23T change exerted a significant effect on the protein's tertiary structure and yielded hydrogen bonds with aspartic acid21, asparagine24, asparagine49 and serine74.

<b>CONCLUSIONb>The mutant gammaD-crystallin gene has a significant effect on the protein's tertiary structure, supporting that alteration of gamma-crystallin plays an important role in human cataract formation.

Animals ; Cattle ; Computer Simulation ; Hydrogen Bonding ; Models, Molecular ; Mutation ; Protein Structure, Tertiary ; gamma-Crystallins ; chemistry ; genetics ; physiology

Crystallins are the major proteins found in the lens, and the localization of specific crystallins is well known. Overexpression and accumulation of alphaB-crystallin has been observed in response to stress conditions or in certain diseases, such as brain tumors and neurodegenerative diseases. The purpose of this study was to examine whether alpha-crystallins are modified during pathological myofibroblastic changes in lens epithelial cells. Lens epithelial cells attached to the anterior capsules of patients with nuclear or anterior polar cataracts were analyzed quantitatively for alpha-crystallin proteins and mRNAs using Western blot and RT-PCR analysis., respectively. The degree of modification of alpha-crystallins was determined by 2-dimensional gel electrophoresis followed by Western blotting. Higher molecular weight protein bands that were immunoreactive to anti-alphaA- and anti-alphaB-crystallin antibodies around 45 kDa accumulated more in the anterior polar cataract samples than in those with the nuclear type of cataracts. Also monomeric alphaB-crystallins accumulated more in lens epithelial cells of patients with anterior polar cataracts. By comparison, no significant changes were found in the levels of the mRNAs encoding alphaA- and alphaB-crystallins in the different types of cataracts. Both alphaA- and alphaB-crystallin proteins seemed to undergo more extensive modification in anterior polar cataracts. Conclusion. In addition to fibrotic changes, which accompany increased levels of extracellular matrix molecules, accumulation and abnormal modification of alpha-crystallins might be implicated in the pathogenic mechanism of this type of cataract.
Adult ; Cataract/*genetics/metabolism ; Epithelial Cells/metabolism ; Female ; Human ; Lens, Crystalline/metabolism ; Male ; Middle Aged ; RNA, Messenger/analysis ; Reverse Transcriptase Polymerase Chain Reaction ; Support, Non-U.S. Gov't ; alpha-Crystallin A Chain/*genetics/metabolism ; alpha-Crystallin B Chain/*genetics/metabolism

No abstract available.
Crystallins* ; Wounds and Injuries*