Isolation and characterization of the chains of type V/type XI collagen present in bovine vitreous

Mayne, Richard; Brewton, Randolph G.; Mayne, Pauline M.; Baker, John

doi:10.1016/s0021-9258(18)98361-4

Cited by 163 publications

(14 citation statements)

References 37 publications

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“…For example, the proa1(II) chain of type II collagen also interacts with the proa1(XI) and proa2(XI) to form type XI collagen (Eyre & Wu 1987). In the vitreous body, the proa2(V) chain substitutes for the proa2(XI) chain (Mayne et al 1993).…”

Section: Initial Assembly Of the Procollagen Moleculementioning

confidence: 99%

Folding defects in fibrillar collagens

Byers

2001

Phil. Trans. R. Soc. Lond. B

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Fibrillar collagens have a long triple helix in which glycine is in every third position for more than 1000 amino acids. The three chains of these molecules are assembled with speci¢city into several di¡erent molecules that have tissue-speci¢c distribution. Mutations that alter folding of either the carboxy-terminal globular peptides that direct chain association, or of the regions of the triple helix that are important for nucleation, or of the bulk of the triple helix, all result in identi¢able genetic disorders in which the phenotype re£ects the region of expression of the genes and their tissue-speci¢c distribution. Mutations that result in changed amino-acid sequences in any of these regions have di¡erent e¡ects on folding and may have di¡erent phenotypic outcomes. Substitution for glycine residues in the triple helical domains are among the most common e¡ects of mutations, and the nature of the substituting residue and its location in the chain contribute to the e¡ect on folding and also on the phenotype. More complex mutations, such as deletions or insertions of triple helix, also a¡ect folding, probably because of alterations in helical pitch along the triple helix. These mutations all interfere with the ability of these molecules to form the characteristic ¢brillar array in the extracellular matrix and many result in intracellular retention of abnormal molecules.

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Section: Initial Assembly Of the Procollagen Moleculementioning

confidence: 99%

Folding defects in fibrillar collagens

Byers

2001

Phil. Trans. R. Soc. Lond. B

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“…Some authors argue that eye examination is crucial for the identification of affected individuals with STL types I and II, who tend to display specific anomalies of the vitreous body (Ang et al, 2007; Poulson et al, 2004; Richards et al, 2010; Snead et al, 2011). STL type III is considered nonocular, due to the fact that COL11A2 is not expressed in the eye (Mayne et al, 1993; van Steensel et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Clinical and genetic characterization of autosomal recessive stickler syndrome caused by novel compound heterozygous mutations in the COL9A3 gene

Маркова

Sparber

Borovikov

et al. 2021

Molec Gen & Gen Med

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Background Stickler syndrome (STL) is a clinically variable and genetically heterogeneous collagenopathy characterized by ophthalmic, auditory, skeletal, and orofacial abnormalities. STL is mainly inherited in an autosomal dominant pattern with mutations in the COL2A1, COL11A1, and COL11A2 genes. Autosomal recessive forms are rare. However, 19 patients have been reported to date, with STL caused by homozygous or compound heterozygous mutations in genes that encode for the three chains of type IX collagen: COL9A1, COL9A2, and COL9A3. Methods Genetic analysis was performed using the next‐generation sequencing of 166 genes associated with skeletal disorders and sequenced on an Ion Torrent S5 system with a minimum coverage of 100X. The two variants in the COL9A3 gene identified in the proband and the parents were confirmed by Sanger sequencing on an ABI3130xl sequencer. Results We describe a novel case of autosomal recessive Stickler syndrome caused by two undescribed mutations in the COL9A3 gene: c.268C>T (p.Arg90Ter) and c.1729C>T (p.Arg577Ter). The clinical features included severe sensorineural hearing loss, high myopia, vitreoretinal degeneration, and early‐onset arthropathy of the lower limbs. Radiography revealed mild spondyloepiphyseal dysplasia. Conclusion This case further expands the mutational and phenotypic spectrum of COL9A‐associated STL with a more severe presentation.

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“…Collagen type XI belongs to the fibrillar class of collagens [24] and polymerizes with collagen type II and IX to produce heterotypic collagen fibrils [25] found in fetal and adult cartilage [26]. Col11a1 gene expression is reported widely beyond cartilage, to include the nucleus pulposus of the intervertebral disc, the developing notochord, the vitreous humour of the mammalian eye, skeletal muscle, brain tissue, tendons, heart valves, skin, the tectorial membrane of the inner ear, intestinal epithelia and smooth muscle of the intestine, the calvaria, and endochondral bones [26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Col11a1a Expression Is Required for Zebrafish Development

Hardy

Reeck

Fang

et al. 2020

JDB

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The autosomal dominant chondrodystrophies, the Stickler type 2 and Marshall syndromes, are characterized by facial abnormalities, vision deficits, hearing loss, and articular joint issues resulting from mutations in COL11A1. Zebrafish carry two copies of the Col11a1 gene, designated Col11a1a and Col11a1b. Col11a1a is located on zebrafish chromosome 24 and Col11a1b is located on zebrafish chromosome 2. Expression patterns are distinct for Col11a1a and Col11a1b and Col11a1a is most similar to COL11A1 that is responsible for human autosomal chondrodystrophies and the gene responsible for changes in the chondrodystrophic mouse model cho/cho. We investigated the function of Col11a1a in craniofacial and axial skeletal development in zebrafish using a knockdown approach. Knockdown revealed abnormalities in Meckel’s cartilage, the otoliths, and overall body length. Similar phenotypes were observed using a CRISPR/Cas9 gene-editing approach, although the CRISPR/Cas9 effect was more severe compared to the transient effect of the antisense morpholino oligonucleotide treatment. The results of this study provide evidence that the zebrafish gene for Col11a1a is required for normal development and has similar functions to the mammalian COL11A1 gene. Due to its transparency, external fertilization, the Col11a1a knockdown, and knockout zebrafish model systems can, therefore, contribute to filling the gap in knowledge about early events during vertebrate skeletal development that are not as tenable in mammalian model systems and help us understand Col11a1-related early developmental events.

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Isolation and characterization of the chains of type V/type XI collagen present in bovine vitreous

Cited by 163 publications

References 37 publications

Folding defects in fibrillar collagens

Folding defects in fibrillar collagens

Clinical and genetic characterization of autosomal recessive stickler syndrome caused by novel compound heterozygous mutations in the COL9A3 gene

Col11a1a Expression Is Required for Zebrafish Development

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