scholarly journals Human and sheep growth-plate cartilage type X collagen synthesis and the influence of tissue storage

1991 ◽  
Vol 277 (2) ◽  
pp. 513-520 ◽  
Author(s):  
G J Gibson ◽  
K T Francki ◽  
J J Hopwood ◽  
B K Foster
Keyword(s):  
Molecular Mass ◽  
Growth Plate ◽  
Collagen Synthesis ◽  
Chick Growth ◽  
Type X Collagen ◽  
Tissue Storage ◽  
Growth Plate Cartilage ◽  
Species Type ◽  
Peptide Maps ◽  
Helical Region

Direct comparison of type X collagen synthesized by human, sheep and chick growth-plate cartilage has shown that the human type X collagen is similar to the chick in both its molecular mass, containing component alpha-chains of 59 kDa with helical regions of 45 kDa, and apparent absence of disulphide-stabilized aggregates, whereas the sheep type X collagen has slightly larger alpha-chains (63 kDa) accounted for by a longer helical region (49 kDa) that contains cystine residues essential for the formation of the high-molecular-mass aggregates found with this species. Type X collagen from all three species showed heterogeneity in primary collagen structure as revealed by Staphylococcus aureus V8 proteinase-generated peptide maps. Collagen synthesis by growth-plate cartilage in culture, particularly synthesis of type IX and X collagen, was shown to be very sensitive to prior storage and suggests caution in the interpretation of changes detected when examining collagen synthesis by growth plates in culture.

The synthesis of type X collagen by bovine and human growth-plate chondrocytes

1991 ◽  
Vol 99 (3) ◽  
pp. 641-649 ◽  
Author(s):  
A. Marriott ◽  
S. Ayad ◽  
M.E. Grant
Keyword(s):  
Growth Plate ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Human Growth ◽  
Type I ◽  
Collagen Gels ◽  
Type X Collagen ◽  
Growth Plate Chondrocytes ◽  
Growth Plate Cartilage ◽  
Disulphide Bonds

Chondrocytes were isolated from bovine growth-plate cartilage and cultured within type I collagen gels. A major collagen with chains of Mr 59,000, decreasing to 47,000 on pepsinization, was synthesized and identified as type X collagen. This collagen was cleaved at two sites by mammalian collagenase, resulting in a major triple-helical fragment with chains of Mr 32,000. The species of Mr 59,000, 47,000 and 32,000 were not detected by SDS-polyacrylamide gel electrophoresis before reduction, indicating the presence of disulphide bonds within the triple helix. In contrast, similar biosynthetic studies with human growth-plate cartilage in organ culture, indicated that human type X collagen does not contain disulphide bonds. A polyclonal antiserum was raised to bovine type X collagen and used in immunolocalization studies to provide direct evidence for the association of type X collagen with the hypertrophic chondrocytes in both bovine and human growth plates during development.

Biosynthesis of a Disulfide-bonded Type X Collagen in Bovine Growth Plate Cartilage

1985 ◽  
Vol 460 (1 Biology, Chem) ◽  
pp. 392-394
Author(s):  
R. I. BASHEY ◽  
M. REMINGTON ◽  
C. T. BRIGHTON ◽  
S. A. JIMENEZ
Keyword(s):  
Growth Plate ◽  
Type X Collagen ◽  
Growth Plate Cartilage

scholarly journals Expression of a Truncated, Kinase-Defective TGF-β Type II Receptor in Mouse Skeletal Tissue Promotes Terminal Chondrocyte Differentiation and Osteoarthritis

1997 ◽  
Vol 139 (2) ◽  
pp. 541-552 ◽  
Author(s):  
Rosa Serra ◽  
Mahlon Johnson ◽  
Ellen H. Filvaroff ◽  
James LaBorde ◽  
Daniel M. Sheehan ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Transgenic Mice ◽  
Growth Plate ◽  
Dominant Negative Mutant ◽  
Type I ◽  
Type Ii ◽  
Type X Collagen ◽  
Skeletal Tissue ◽  
Hypertrophic Cartilage ◽  
Growth Plate Cartilage

Members of the TGF-β superfamily are important regulators of skeletal development. TGF-βs signal through heteromeric type I and type II receptor serine/threonine kinases. When over-expressed, a cytoplasmically truncated type II receptor can compete with the endogenous receptors for complex formation, thereby acting as a dominant-negative mutant (DNIIR). To determine the role of TGF-βs in the development and maintenance of the skeleton, we have generated transgenic mice (MT-DNIIR-4 and -27) that express the DNIIR in skeletal tissue. DNIIR mRNA expression was localized to the periosteum/perichondrium, syno-vium, and articular cartilage. Lower levels of DNIIR mRNA were detected in growth plate cartilage. Transgenic mice frequently showed bifurcation of the xiphoid process and sternum. They also developed progressive skeletal degeneration, resulting by 4 to 8 mo of age in kyphoscoliosis and stiff and torqued joints. The histology of affected joints strongly resembled human osteo-arthritis. The articular surface was replaced by bone or hypertrophic cartilage as judged by the expression of type X collagen, a marker of hypertrophic cartilage normally absent from articular cartilage. The synovium was hyperplastic, and cartilaginous metaplasia was observed in the joint space. We then tested the hypothesis that TGF-β is required for normal differentiation of cartilage in vivo. By 4 and 8 wk of age, the level of type X collagen was increased in growth plate cartilage of transgenic mice relative to wild-type controls. Less proteoglycan staining was detected in the growth plate and articular cartilage matrix of transgenic mice. Mice that express DNIIR in skeletal tissue also demonstrated increased Indian hedgehog (IHH) expression. IHH is a secreted protein that is expressed in chondrocytes that are committed to becoming hypertrophic. It is thought to be involved in a feedback loop that signals through the periosteum/ perichondrium to inhibit cartilage differentiation. The data suggest that TGF-β may be critical for multifaceted maintenance of synovial joints. Loss of responsiveness to TGF-β promotes chondrocyte terminal differentiation and results in development of degenerative joint disease resembling osteoarthritis in humans.

Characterisation of articular and growth plate cartilage collagens in porcine osteochondrosis

1994 ◽  
Vol 107 (1) ◽  
pp. 47-59 ◽  
Author(s):  
R.J. Wardale ◽  
V.C. Duance
Keyword(s):  
Articular Cartilage ◽  
Growth Plate ◽  
Normal Tissue ◽  
Collagen Type ◽  
Hypertrophic Chondrocytes ◽  
Type I ◽  
Type X Collagen ◽  
Growth Plate Cartilage ◽  
Cartilage Lesions ◽  
Articular Cartilage Lesions

The articular and growth plate cartilages of osteochondrotic pigs were examined and compared with those from clinically normal animals. Both types of osteochondrotic cartilage showed considerable localised thickening apparently due to a lack of ossification. Histological examination of cartilage lesions demonstrated a breakdown in the normal pattern of chondrocyte maturation. Articular cartilage lesions lacked mature clones of chondrocytes in the calcifying region. Growth plate cartilage showed an accumulation of disorganised hypertrophic chondrocytes rather than the well-defined columns seen in normal tissue. The overall percentages of collagen in osteochondrotic lesions from both articular and growth plate cartilage were significantly reduced compared with levels in unaffected cartilage. There were substantial increases in the proportion of type I collagen in lesions from both osteochondrotic articular and growth plate cartilages and a reduction in the proportion of type II collagen. Type X collagen was detected in osteochondrotic but not normal articular cartilage. The proportion of type X collagen was unchanged in osteochondrotic growth plate cartilage. The levels of the collagen cross-links, hydroxylysylpyridinoline, hydroxylysyl-ketonorleucine and dehydrohydroxylysinonorleucine were radically reduced in samples from osteochondrotic growth-plate cartilage lesions when compared with normal tissue. Less dramatic changes were observed in articular cartilage although there was a significant decrease in the level of hydroxylysylketonorleucine in osteochondrotic lesions. Immunofluorescence examination of osteochondrotic lesions showed a considerable disruption of the organisation of the collagenous components within both articular and growth-plate cartilages. Normal patterns of staining of types I and VI collagen seen at the articular surface in unaffected tissue were replaced by a disorganised, uneven stain in osteochondrotic articular cartilage lesions. Incomplete removal of cartilage at the ossification front of osteochondrotic growth plate was demonstrated by immunofluorescence staining of type IX collagen. Type X collagen was produced in the matrix of the calcifying region of osteochondrotic articular cartilage by small groups of hypertrophic chondrocytes, but was not detected in normal articular cartilage. The distribution of type X collagen was unchanged in osteochondrotic growth plate cartilage.

scholarly journals Identification of carbonic anhydrase in chick growth-plate cartilage.

1982 ◽  
Vol 30 (4) ◽  
pp. 391-394 ◽  
Author(s):  
C V Gay ◽  
R E Anderson ◽  
H Schraer ◽  
D S Howell
Keyword(s):  
Articular Cartilage ◽  
Carbonic Anhydrase ◽  
Growth Plate ◽  
Biochemical Assay ◽  
Activity Levels ◽  
Chick Growth ◽  
Growth Plate Cartilage ◽  
Wet Weight

Carbonic anhydrase has been localized by immunocytochemistry in the cells and territorial matrix of the hypertrophic and calcifying zones of chick growth-plate cartilage. Adjacent epiphyseal and articular cartilage were not stained. By biochemical assay the activity levels were 61.3, 1.8, 34.7, and 703.3 units/g wet weight for growth plate, epiphyseal/articular cartilage, spongiosa, and blood, respectively. The role of the enzyme in growth plate is discussed.

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