scholarly journals Type X collagen biosynthesis and expression in avian tibial dyschondroplasia

1998 ◽  
Vol 6 (2) ◽  
pp. 125-136 ◽  
Author(s):  
Anthony M. Reginato ◽  
Reza I. Bashey ◽  
Gaston Rosselot ◽  
Ronald M. Leach ◽  
Carol V. Gay ◽  
...  
Keyword(s):  
Collagen Biosynthesis ◽  
Type X Collagen ◽  
Tibial Dyschondroplasia

scholarly journals Promoter and Transcription of Type X Collagen Gene in Broiler Chickens with Tibial Dyschondroplasia

1996 ◽  
Vol 75 (6) ◽  
pp. 691-694 ◽  
Author(s):  
X. ZHANG ◽  
G.R. MCDANIEL ◽  
J.J. GIAMBRONE ◽  
E. SMITH
Keyword(s):  
Broiler Chickens ◽  
Collagen Gene ◽  
Type X Collagen ◽  
Tibial Dyschondroplasia

scholarly journals Quantitative analysis of type X-collagen biosynthesis by embryonic-chick sternal cartilage

1986 ◽  
Vol 233 (2) ◽  
pp. 357-367 ◽  
Author(s):  
S A Jimenez ◽  
R Yankowski ◽  
A M Reginato
Keyword(s):  
Quantitative Analysis ◽  
Hyaline Cartilage ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Embryonic Chick ◽  
Collagen Biosynthesis ◽  
Molecular Aggregate ◽  
Type X Collagen ◽  
Organ Cultures ◽  
Disulphide Bonds

We have performed a quantitative analysis of the various collagens biosynthesized by organ cultures of whole embryonic-chick sternum and its separate anatomical regions corresponding to the zones of permanent hyaline and presumptive-calcification cartilages. Our studies demonstrated that embryonic-chick sternum devotes a large portion of its biosynthetic commitment towards production of Type X collagen, which represented approx. 18% of the total newly synthesized collagen. Comparison of the collagens biosynthesized by the permanent hyaline cartilage and by the cartilage from the presumptive-calcification zone demonstrated that Type X-collagen production was strictly confined to the presumptive-calcification region. Sequential extraction of the newly synthesized Type X collagen demonstrated the existence of two separate populations. One population (approx. 20%) was composed of easily extractable molecules that were solubilized with 1.0 m-NaCl/50 mM-Tris/HCI buffer, pH 7.4. The second population was composed of molecules that were not extractable even after repeated pepsin digestion, but became completely solubilized after treatment with 20 mM-dithiothreitol/0.15 M-NaCl buffer at neutral pH. These results suggest that most of the Type X collagen normally exists in the tissue as part of a pepsin-resistant molecular aggregate that may be stabilized by disulphide bonds. Quantitative analysis of the proportion of Type X collagen relative to the other collagens synthesized in the cultures indicated that this collagen was a major biosynthetic product of the presumptive-calcification cartilage, since it represented about 35% of the total collagen synthesized by this tissue. In contrast, the permanent hyaline cartilage did not display any detectable synthesis of Type X collagen. When compared on a per-cell basis, the chondrocytes from the presumptive-calcification zone synthesized approx. 33% more Type X collagen than the amount of Type II collagen synthesized by the chondrocytes from the permanent-hyaline-cartilage zone. Subsequently, it was demonstrated that Type X collagen is a structural component of chick sternum matrix, since quantitative amounts could be extracted from the region of presumptive calcification of 17-day-old chick-embryo sterna and from the calcified portion of adult-chick sterna. The strict topographic distribution in the expression of Type X collagen biosynthesis to the zone of presumptive calcification suggests that this collagen may play an important role in initiation or progression of tissue calcification.

Collagen expression in chicken tibial dyschondroplasia

1996 ◽  
Vol 109 (5) ◽  
pp. 1119-1131
Author(s):  
R.J. Wardale ◽  
V.C. Duance
Keyword(s):  
Growth Plate ◽  
Type I Collagen ◽  
Normal Growth ◽  
Type I ◽  
Type X Collagen ◽  
Growth Plate Chondrocytes ◽  
Growth Plate Cartilage ◽  
Tibial Dyschondroplasia ◽  
Collagen Expression

Collagen expression in growth plate cartilage derived from broiler chickens with tibial dyschondroplasia was studied and compared with samples from unaffected birds. Normal growth plate contains 12% collagen (dry weight) and dyschondroplastic growth plate 19% collagen compared with articular cartilage, which contains 55%. Dyschondroplastic growth plate collagens were more resistant to extraction by pepsin treatment than were those from unaffected growth plate. Normal and dyschondroplastic growth plate cartilages contain similar amounts of type I collagen (5% of the total collagen) but dyschondroplastic growth plate cartilage contains slightly less type II and type XI collagens, and significantly more type X collagen (25% as compared to 11%) than in normal growth plate. The levels of the mature collagen cross-link, hydroxylysyl-pyridinoline, are very low in normal growth plate but are six times higher in dyschondroplastic lesions. Immunolocalisation studies show that there is little change to the normal patterns of collagen organisation in dyschondroplastic growth plate. Investigation of metalloproteinase activity showed there to be a reduction in MMP-2 levels in dyschondroplastic growth plate compared to normal growth plate. In vitro studies on articular, normal growth plate and dyschondroplastic growth plate chondrocytes cultured in alginate or on plastic revealed differences between the cell types. When plated on plastic, articular chondrocytes rapidly assume a fibroblastic morphology. In contrast, normal growth plate chondrocytes retain their polygonal morphology whereas chondrocytes derived from dyschondroplastic cartilage initially exhibit both fibroblastic and polygonal phenotypes but gradually change to totally fibroblastic. These morphological changes are reflected by the collagen synthesis in vitro. Chondrocytes derived from normal articular cartilage synthesised collagen types I, II and X when cultured in alginate but type X synthesis was lost when cultured on plastic. Chondrocytes derived from normal growth plate cartilage synthesised predominantly type X collagen when cultured in either system. Chondrocytes derived from dyschondroplastic growth plate exhibited a similar phenotype to normal growth plate chondrocytes when cultured in alginate beads, but showed signs of dedifferentiation with reduced type X collagen and increased type I collagen when plated on plastic. These results suggest that the chondrocytes in dyschondroplastic growth plate cartilage are at a different stage of maturity than normal resulting in a cartilage that is failing to turn over at a normal rate.

Intracellular enzymes of collagen biosynthesis in rat kidney in streptozotocin diabetes

Diabetes ◽  
1976 ◽  
Vol 25 (11) ◽  
pp. 1066-1070 ◽  
Author(s):  
J. Risteli ◽  
V. A. Koivisto ◽  
H. K. Akerblom ◽  
K. I. Kivirikko
Keyword(s):  
Rat Kidney ◽  
Streptozotocin Diabetes ◽  
Collagen Biosynthesis ◽  
Intracellular Enzymes

scholarly journals Collagen metabolism as a regulator of proline dehydrogenase/proline oxidase-dependent apoptosis/autophagy

Amino Acids ◽  
2021 ◽  
Author(s):  
Jerzy Palka ◽  
Ilona Oscilowska ◽  
Lukasz Szoka
Keyword(s):  
Cell Metabolism ◽  
Underlying Mechanism ◽  
Collagen Biosynthesis ◽  
Proline Metabolism ◽  
Proline Dehydrogenase ◽  
Histone Demethylases ◽  
Proline Oxidase ◽  
Prolyl Hydroxylases ◽  
Transport Chain ◽  
And Control

AbstractRecent studies on the regulatory role of amino acids in cell metabolism have focused on the functional significance of proline degradation. The process is catalysed by proline dehydrogenase/proline oxidase (PRODH/POX), a mitochondrial flavin-dependent enzyme converting proline into ∆1-pyrroline-5-carboxylate (P5C). During this process, electrons are transferred to electron transport chain producing ATP for survival or they directly reduce oxygen, producing reactive oxygen species (ROS) inducing apoptosis/autophagy. However, the mechanism for switching survival/apoptosis mode is unknown. Although PRODH/POX activity and energetic metabolism were suggested as an underlying mechanism for the survival/apoptosis switch, proline availability for this enzyme is also important. Proline availability is regulated by prolidase (proline supporting enzyme), collagen biosynthesis (proline utilizing process) and proline synthesis from glutamine, glutamate, α-ketoglutarate (α-KG) and ornithine. Proline availability is dependent on the rate of glycolysis, TCA and urea cycles, proline metabolism, collagen biosynthesis and its degradation. It is well established that proline synthesis enzymes, P5C synthetase and P5C reductase as well as collagen prolyl hydroxylases are up-regulated in most of cancer types and control rates of collagen biosynthesis. Up-regulation of collagen prolyl hydroxylase and its exhaustion of ascorbate and α-KG may compete with DNA and histone demethylases (that require the same cofactors) to influence metabolic epigenetics. This knowledge led us to hypothesize that up-regulation of prolidase and PRODH/POX with inhibition of collagen biosynthesis may represent potential pharmacotherapeutic approach to induce apoptosis or autophagic death in cancer cells. These aspects of proline metabolism are discussed in the review as an approach to understand complex regulatory mechanisms driving PRODH/POX-dependent apoptosis/survival.

Morinda officinalis polysaccharides improve meat quality by reducing oxidative damage in chickens suffering from tibial dyschondroplasia

2020 ◽  
pp. 128688
Author(s):  
Shu-cheng Huang ◽  
Qin-qin Cao ◽  
Ya-bing Cao ◽  
Yu-rong Yang ◽  
Ting-ting Xu ◽  
...  
Keyword(s):  
Oxidative Damage ◽  
Meat Quality ◽  
Tibial Dyschondroplasia
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