1988
DOI: 10.1159/000157111
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Abnormal Type II Collagen in the Spondyloepiphyseal Dysplasias

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Cited by 52 publications
(38 citation statements)
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“…The present study establishes the importance of intracellular vesicle traffic in mammalian postnatal bone formation, a highly organized process involving chondrocyte proliferation, differentiation, apoptosis, and calcification (1,2). In principle, transport defects could affect endochondral bone formation at a number of levels, including the synthesis, processing, secretion, or uptake of growth factors, extracellular matrix, and matrix-remodeling proteases (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16). Such factors also spatially regulate chondrocyte proliferation and apoptosis within the growth plate, consistent with reductions in BrdU and caspase 3-positive cells and growth plate histology in Dym-mutant mice.…”
Section: Discussionsupporting
confidence: 66%
See 1 more Smart Citation
“…The present study establishes the importance of intracellular vesicle traffic in mammalian postnatal bone formation, a highly organized process involving chondrocyte proliferation, differentiation, apoptosis, and calcification (1,2). In principle, transport defects could affect endochondral bone formation at a number of levels, including the synthesis, processing, secretion, or uptake of growth factors, extracellular matrix, and matrix-remodeling proteases (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16). Such factors also spatially regulate chondrocyte proliferation and apoptosis within the growth plate, consistent with reductions in BrdU and caspase 3-positive cells and growth plate histology in Dym-mutant mice.…”
Section: Discussionsupporting
confidence: 66%
“…Inherited defects in bone formation, or osteochondrodysplasias, are responsible for more than 200 clinically distinct diseases that occur with a cumulative incidence exceeding 1 in 10,000 live births (3,4) caused by mutations in processes critical for osseous bone formation and maintenance. These include growth factor signaling (5), extracellular matrix synthesis (6)(7)(8)(9)(10)(11)(12)(13) and remodeling (14)(15)(16), protein sorting (17)(18)(19)(20), and vesicle traffic (21,22).…”
mentioning
confidence: 99%
“…The major CNBr-peptides from the patient's type II collagen also ran more slowly than their counterparts from control cartilage (Fig. 5 b), which suggests from past experience a degree ofposttranslational overmodification (18). Peptides CB1O and CB 1 1, which lie respectively COOH-terminal and NH2-terminal to the peptide a 1(II)CB8 containing the mutation (19), were both affected.…”
Section: Resultsmentioning
confidence: 94%
“…Since type II collagen is found in a restricted set of tissues that includes articular cartilage, the nucleus pulposus of the spine, and the vitreous of the eye (2), the concordance between the clinical findings and the distribution of the protein suggests that a primary defect of type II collagen may be responsible for some of these disorders. Structurally abnormal type II collagen has been isolated from cartilage ofindividuals with SED (3, 4), spondyloepimetaphyseal dysplasia (3,4), and achondrogenesishypochondrogenesis (5). Combined with the demonstration of linkage of markers in the COL2AJ gene with a form of familial osteoarthritis (6) and with Stickler syndrome (7,8), these studies have suggested that mutations in the type II collagen gene may underlie a spectrum of disorders that span a broad range of clinical severity.…”
mentioning
confidence: 99%
“…Biochemical studies have shown that cartilage from individuals with either SED (3,4) or achondrogenesis-hypochondrogenesis (5) contains type II collagen with both slowly migrating and normally migrating al(II) chains. Amino acid analyses of the abnormal type II collagen from the affected individuals have shown that there is increased lysyl hydroxylation (3)(4)(5), suggesting that the more slowly migrating population is derived from molecules containing a chain with a defect that affects triple-helix structure and/or assembly. These results are conceptually homologous to the consequences of defects in type I collagen that produce osteogenesis imperfecta, in which mutations that alter triple-helix structure result in excessive posttranslational modification of all chains in molecules that incorporate at least one abnormal chain (10,11).…”
mentioning
confidence: 99%