The Stickler syndrome: Evidence for close linkage to the structural gene for type II collagen

Francomano, Clair A.; Liberfarb, Ruth M.; Hirose, Tatsuo; Maumenee, Irene H.; Streeten, Elizabeth A.; Meyers, Deborah A.; Pyeritz, Reed E.

doi:10.1016/0888-7543(87)90027-9

Cited by 163 publications

(49 citation statements)

References 20 publications

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“…Subsequent analysis of such families linked the disorder to COL2A1 the gene for type II collagen, a major constituent of both cartilage and vitreous. 2 Thus Stickler syndrome was related to other chondrodysplasias such as achondrogenesis, hypochondrogenesis, splondyloepiphyseal dysplasia and Kniest dysplasia, which result from dominant negative mutations in the COL2A1 gene. 3 The first mutations characterised in Stickler syndrome all lead to premature termination codons (PTC), and so resulted in haploinsufficiency of type II collagen.…”

Section: Stickler Syndrome (Mim 108300 604841)mentioning

confidence: 99%

Molecular genetics of rhegmatogenous retinal detachment

Richards

Scott

Snead

2002

Eye

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Rhegmatogenous retinal detachment (RRD) most commonly occurs as a spontaneous event resulting from posterior vitreous detachment, typically between the ages of 40-70 yrs. It is also a feature in some inherited disorders, most commonly Stickler syndrome. The relationship between these inherited disorders and the spontaneous cases is unclear. Here in particular we review Stickler syndrome, and discuss the differential diagnosis of Stickler, Wagner and Marshall syndromes. Other rare inherited disorders associated with RRD are also briefly reviewed.

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Section: Stickler Syndrome (Mim 108300 604841)mentioning

confidence: 99%

Molecular genetics of rhegmatogenous retinal detachment

Richards

Scott

Snead

2002

Eye

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“…Early genetic studies demonstrated linkage of the type II collagen gene locus, COL2A1, and Stickler syndrome, 18 and the identification of a mutation in this gene in Stickler syndrome subsequently confirmed this as the causative gene. 19,20 A variety of mutations spread throughout the entire COL2A1 gene have been identified in families with the Stickler syndrome.…”

mentioning

confidence: 99%

The Stickler syndrome: Genotype/phenotype correlation in 10 families with Stickler syndrome resulting from seven mutations in the type II collagen gene locus COL2A1

Liberfarb

Levy

Rose

et al. 2003

Genetics in Medicine

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“…It has been suggested that achondroplasia is associated with type I1 collagen [6,7] and mutations in the gene are responsible for several human diseases, such as hereditary arthro-ophthalmopathy or osteoarthritis in some families [5]. Characterization of the genomic structure of this gene presented here will make it possible to identify genetic disorders of human cartilage where an abnormality of the procollagen al(I1) gene is the primary defect.…”

Section: Discussionmentioning

confidence: 99%

Genomic organization of the human procollagen α1 (II) collagen gene

Huang

Seyer

Thompson

et al. 1991

European Journal of Biochemistry

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The nucleotide sequence of the human procollagen a1 (11) collagen gene extending from within the first intron through exon 15, and part of the 15th intron has been determined. This sequence analysis (7056 bases) identifies the intron/exon organization of the region of this gene encoding the N-propeptide and part of the triple-helical domain. Structural comparison of this with the genes of other human fibrillar collagens shows considerable diversity in terms of size and number of introns and exons that encodes the N-propeptide domain. Although the genomic structure of the human procollagen al(I1) gene is quite different from the rat procollagen al(1I) gene, the nucleotide coding sequences are 89% identical.Type I1 collagen is the major structural component of cartilage. It represents a genetically distinct member of fibrillar collagen family and is comprised of three identical aI(11) chains [l -31. Fibrillar procollagens are synthesized in precursor forms containing propeptides at both the amino and carboxyl ends of the molecules. Propeptides are thought to be involved in alignment of the three procollagens chains during triple-helix formation and in their secretion [l -31. Propeptides are cleaved after secretion of the native type I1 collagen molecule [l -31. This process and the coordinated expression of collagen genes are vitally important during vertebrate development [4]. Recently, genetic lesions in the procollagen al(I1) gene have been identified as the basis of several human diseases [5 -81.The human procollagen al(I1) gene has been isolated and characterized using a cosmid clone and a series of overlapping genomic clones [8, 91. The entire gene spans six large EcoRI fragments with sizes of 4.8, 7.3, 5.2, 9.2, 3.7 and 4.3 kb in the order of 5' end to 3' end of the gene. The nucleotide sequence of the 3' region of the gene encoding the C-propeptide has been determined [9]. Recently, overlapping cDNA clones encoding the complete helical region of the human procollagen al(I1) gene were isolated and identified [5]. Analysis of the cDNAs revealed the nucleotide sequence of the mRNA and the deduced amino acid sequence. Exons in the triple-helical and the C-propeptide region of human type I1 collagen are identical in size to exons of the chicken gene [ intronic structure in the triple-helical and the N-propeptide region has not been fully identified [12, 131. In this study, we present genomic nucleotide sequence of 6885 residues of the human procollagen a1 (11) gene encoding the 3' end of the first intron continuously through the 5' end of the 15th intron. This area covers the complete N-propeptide (except exon I) and residues 1-272 of the triple-helical domain of this gene. This information, for the first time, identified the genomic organization of the human type I1 collagen gene. Structural comparison of this gene with other human fibril-forming collagen genes and the rat type I1 collagen gene is presented. MATERIALS AND METHODS PlusmidThe 7.3-kb and 9.2-kb EcoRI fragments containing portions of the human ...

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The Stickler syndrome: Evidence for close linkage to the structural gene for type II collagen

Cited by 163 publications

References 20 publications

Molecular genetics of rhegmatogenous retinal detachment

Molecular genetics of rhegmatogenous retinal detachment

The Stickler syndrome: Genotype/phenotype correlation in 10 families with Stickler syndrome resulting from seven mutations in the type II collagen gene locus COL2A1

Genomic organization of the human procollagen α1 (II) collagen gene

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