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binding of collagen VI to NG2 is essential for the direction of tendon fibroblasts migration in vitro.
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Genetic study showed a missense mutation in COL6A2 (c.820 G>A, p.Gly268Ser) that causes a glycine substitution in the Gly-X-Y collagenous motif, at the beginning of the collagenous triple helical domain. The c.820 G>A mutation segregated in all the affected patients.
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Parental mosaicism was confirmed in the four families through quantitative analysis of the ratio of mutant versus wild-type allele (COL6A1, COL6A2, and COL6A3) in genomic DNA from various tissues; consistent with somatic mosaicism, parental samples had lower ratios of mutant versus wild-type allele compared with the fully heterozygote offspring.
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Mutations in COL6A2 gene are associated with aberrant mitochondria in Bethlem myopathy.
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In UCMD, 8 mutations were identified in COL6A2 in Chinese patients.
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Mutations in each of the three collagen VI genes, COL6A1, COL6A2 and COL6A3, cause four types of muscle disorders: Ullrich congenital muscular dystrophy, Bethlem myopathy, limb-girdle muscular dystrophy, and autosomal recessive myosclerosis. (Review)
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COL6A2 is overexpressed in Down syndrome-affected umbilical cords at early and term gestational ages.
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Homozygous COL6A2 mutation, p.Asp215Asn, was identified in both affected siblings. We conclude that the COL6A2 p.Asp215Asn mutation is likely to be responsible for PME (Progressive Myoclonus Epilepsy) in this family.
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A deletion within intron 1A of the COL6A2 gene, occurring in compound heterozygosity with a small deletion in exon 28, was identified in a BM patient.
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the C2A splice variant has a role in recessive COL6A2 C-globular missense mutations in Ullrich congenital muscular dystrophy
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The alpha2(VI) chain modulates matrix-metalloproteinase (MMP) availability by sequestering proMMPs in the extracellular matrix, blocking proteolytic activity.
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Haplotype analysis clearly suggested linkage of Ullrich muscular dystrophy to the COL6A1/2 locus in two cases and to the COL6A3 loci in the third case. In the remaining nine patients, primary collagen VI involvement was excluded
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the C-terminal globular domain of COL6A2 is not essential for triple-helix formation but is critical for microfibrillar assembly in Ullrich congenital muscular dystrophy
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A case of Ullrich disease is associated with complete deficiency of collagen VI and compound heterozygous mutations in the collagen VI alpha 2 gene with absence of microfibrils on electron microscopy.
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Bethlem myopathy is an autosomal dominantly inherited myopathy with contractures, caused by mutations in COL6A1 gene, COL6A2 gene or COL6A3 gene.
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In Ullrich syndrome, a heterozygous G-to-A substitution at position +5 in intron 23 & the corresponding heterozygous 6-bp deletion in exon 26 which deleted 1 of the 2 tandem repeats of the sequence CATCGG in nt 2268-2273 & 2274-2279 in COL6A2 ORF.
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dominant mutations are common in Ullrich congenital muscular dystrophy (UCMD).
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diminished COL6A2 mRNA expression found to be primary pathogenic mechanism in UCMD patient
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This study demonstrates a homogenoeous overexpression of the genes encoding for alpha1 and alpha2 chains of collagen type VI in nuchal skin of human trisomy 21 fetuses.
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Study reports 10 unrelated patients with a Ullrich congenital muscular dystrophy clinical phenotype and de novo dominant negative heterozygous splice mutations in COL6A1, COL6A2 and COL6A3.
