Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
The carboxypropeptide trimer of type II collagen is a prominent component of immature cartilages and intervertebral-disc tissue
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Biochemical and immuno-histochemical localization of type IIA procollagen in annulus fibrosus of mature bovine intervertebral disc
2021, Matrix Biology PlusCitation Excerpt :As fetal type II collagen containing tissue develops, exon 2 in the N-propeptide is spliced out [30,33,37] and/or the N-propeptide of type IIA/B collagen is processed by ADAMTS-2/3 [65] and although thought to be rapidly degraded by metalloproteinase or internalized by cells [66,67], we have shown type XI collagen molecules with a chain composition of α1(XI) α2(XI) pro α1(IIA) can exist [36]. Interestingly, the C-propeptide trimer of type II collagen has been shown to be a prominent matrix component of immature cartilages and intervertebral disc tissue [42]. Whether the type IIA procollagen detected in the adult AF is part of an existing network of type II/type I collagen fibrils and is somehow exposed or is newly synthesized type IIA procollagen is not clear from our data and will need further investigation.
Chondrocalcin is internalized by chondrocytes and triggers cartilage destruction via an interleukin-1β-dependent pathway
2013, Matrix BiologyCitation Excerpt :Chondrocalcin was significantly internalized at concentrations about 100-fold lower than peptide D4. While peptide D4 remains presumably under a monomeric state in solution, chondrocalcin is a disulfide-stabilized homotrimer, as earlier described (Niyibizi et al., 1987) and verified in the course of its purification (Fig. 6A & B). Therefore, a single chondrocalcin trimer possesses 3 physically linked copies of peptide D4 (Figs. 5E & 6B).
Biomarkers of cartilage turnover. Part 1: Markers of collagen degradation and synthesis
2010, Veterinary JournalReview: Collagen markers in early arthritic diseases
2006, Clinica Chimica ActaRegional differences of type II collagen synthesis in the human temporomandibular joint disc: Immunolocalization study of carboxy-terminal type II procollagen peptide (chondrocalcin)
2003, Archives of Oral BiologyCitation Excerpt :Considerable amounts of carboxy-terminal type II procollagen peptide (pCOL-II-C) have been extracted and purified from the growth plates of fetal bovine long bones, suggesting that pCOL-II-C plays important roles in cartilage mineralisation and endochondral bone formation.8 The substance was first identified as chondrocalcin,9 but was subsequently found to be identical to pCOL-II-C.10,11 The measurement of pCOL-II-C reflected the rate of type II collagen synthesis and was useful for both in vitro and in vivo studies of articular cartilage in healthy and diseased states.12 In the present study, the regional distributions of pCOL-II-C and type II collagen were investigated in human TMJ discs using immunohistochemical techniques.
Structure of Growth Plate and Bone Matrix
2003, Pediatric Bone: Biology & Diseases