Limits...
Genetic variations in GJA3, GJA8, LIM2, and age-related cataract in the Chinese population: a mutation screening study.

Zhou Z, Wang B, Hu S, Zhang C, Ma X, Qi Y - Mol. Vis. (2011)

Bottom Line: We found five novel variations in 145 patients and none of them presented in the 156 controls.There are two variations in GJA3 (c.-39C>G, c. 415G>A); one in GJA8 (c. 823G>A), and two in LIM2 (c.57G>A, c.67A>C).PolyPhen predicted that the LIM2 c.67A>C mutation may have potential pathogenicity.

View Article: PubMed Central - PubMed

Affiliation: Department of Ophthalmology, the Second Affiliated Hospital of Harbin Medical University, Harbin, China.

ABSTRACT

Purpose: To investigate the role of genetic variations in three known cataract-associated genes, gap junction protein α3 (GJA3), gap junction protein α8 (GJA8), lens intrinsic membrane protein 2 (LIM2), encoding lens fiber cell membrane proteins in the development of age-related cataracts.

Methods: One hundred and forty-five sporadic age-related cataract patients and one hundred and fifty-six unrelated random healthy controls participated in this study. Genomic DNA was extracted from peripheral blood leukocytes. All exons of GJA3, GJA8, and LIM2 were sequenced after being amplified by polymerase chain reaction (PCR). The functional consequences of the mutations were analyzed using PolyPhen.

Results: We found five novel variations in 145 patients and none of them presented in the 156 controls. There are two variations in GJA3 (c.-39C>G, c. 415G>A); one in GJA8 (c. 823G>A), and two in LIM2 (c.57G>A, c.67A>C). PolyPhen predicted that the LIM2 c.67A>C mutation may have potential pathogenicity.

Conclusions: The genetic mutation in GJA3, GJA8, and LIM2 may slightly contribute to the development of age-related cataracts. This study showed a potential relationship between lens fiber cell membrane protein genes and the development of age-related cataracts in the Chinese population.

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Related in: MedlinePlus

Cross species conservation analysis. The black bars highlight the interesting positions of the proteins. A: Multiple alignment indicates that valine at position 139 in gap junction protein α3 (GJA3) is medium conserved. B: Valine at codon 275 in gap junction protein α8 (GJA8) is highly conserved. C: At lens intrinsic membrane protein 2 (LIM2) position 23, methionine was not a conserved amino acid residue compared to threonine.
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f2: Cross species conservation analysis. The black bars highlight the interesting positions of the proteins. A: Multiple alignment indicates that valine at position 139 in gap junction protein α3 (GJA3) is medium conserved. B: Valine at codon 275 in gap junction protein α8 (GJA8) is highly conserved. C: At lens intrinsic membrane protein 2 (LIM2) position 23, methionine was not a conserved amino acid residue compared to threonine.

Mentions: We aligned the amino acid sequences of GJA3, GJA8, and LIM2 from several species. The valine at codon 139 in GJA3 is medium conserved (Figure 2A) and the valine at position 275 in GJA8 is highly conserved (Figure 2B). In LIM2, tyrosine is more conservative in other species compared with methionine at codon 23 in human (Figure 2C).


Genetic variations in GJA3, GJA8, LIM2, and age-related cataract in the Chinese population: a mutation screening study.

Zhou Z, Wang B, Hu S, Zhang C, Ma X, Qi Y - Mol. Vis. (2011)

Cross species conservation analysis. The black bars highlight the interesting positions of the proteins. A: Multiple alignment indicates that valine at position 139 in gap junction protein α3 (GJA3) is medium conserved. B: Valine at codon 275 in gap junction protein α8 (GJA8) is highly conserved. C: At lens intrinsic membrane protein 2 (LIM2) position 23, methionine was not a conserved amino acid residue compared to threonine.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3049737&req=5

f2: Cross species conservation analysis. The black bars highlight the interesting positions of the proteins. A: Multiple alignment indicates that valine at position 139 in gap junction protein α3 (GJA3) is medium conserved. B: Valine at codon 275 in gap junction protein α8 (GJA8) is highly conserved. C: At lens intrinsic membrane protein 2 (LIM2) position 23, methionine was not a conserved amino acid residue compared to threonine.
Mentions: We aligned the amino acid sequences of GJA3, GJA8, and LIM2 from several species. The valine at codon 139 in GJA3 is medium conserved (Figure 2A) and the valine at position 275 in GJA8 is highly conserved (Figure 2B). In LIM2, tyrosine is more conservative in other species compared with methionine at codon 23 in human (Figure 2C).

Bottom Line: We found five novel variations in 145 patients and none of them presented in the 156 controls.There are two variations in GJA3 (c.-39C>G, c. 415G>A); one in GJA8 (c. 823G>A), and two in LIM2 (c.57G>A, c.67A>C).PolyPhen predicted that the LIM2 c.67A>C mutation may have potential pathogenicity.

View Article: PubMed Central - PubMed

Affiliation: Department of Ophthalmology, the Second Affiliated Hospital of Harbin Medical University, Harbin, China.

ABSTRACT

Purpose: To investigate the role of genetic variations in three known cataract-associated genes, gap junction protein α3 (GJA3), gap junction protein α8 (GJA8), lens intrinsic membrane protein 2 (LIM2), encoding lens fiber cell membrane proteins in the development of age-related cataracts.

Methods: One hundred and forty-five sporadic age-related cataract patients and one hundred and fifty-six unrelated random healthy controls participated in this study. Genomic DNA was extracted from peripheral blood leukocytes. All exons of GJA3, GJA8, and LIM2 were sequenced after being amplified by polymerase chain reaction (PCR). The functional consequences of the mutations were analyzed using PolyPhen.

Results: We found five novel variations in 145 patients and none of them presented in the 156 controls. There are two variations in GJA3 (c.-39C>G, c. 415G>A); one in GJA8 (c. 823G>A), and two in LIM2 (c.57G>A, c.67A>C). PolyPhen predicted that the LIM2 c.67A>C mutation may have potential pathogenicity.

Conclusions: The genetic mutation in GJA3, GJA8, and LIM2 may slightly contribute to the development of age-related cataracts. This study showed a potential relationship between lens fiber cell membrane protein genes and the development of age-related cataracts in the Chinese population.

Show MeSH
Related in: MedlinePlus