scholarly journals Submicrosomal localization of prolyl hydroxylase from chick embryo limb bone.

1976 ◽  
Vol 251 (15) ◽  
pp. 4770-4777 ◽  
Author(s):  
B Peterkofsky ◽  
R Assad
Keyword(s):  
Chick Embryo ◽  
Prolyl Hydroxylase ◽  
Limb Bone

scholarly journals Effect of cortisol acetate on collagen biosynthesis and on the activities of prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase in chick-embryo tendon cells

1977 ◽  
Vol 164 (3) ◽  
pp. 533-539 ◽  
Author(s):  
A Oikarinen
Keyword(s):  
Chick Embryo ◽  
Enzyme Activities ◽  
Collagen Synthesis ◽  
Enzyme Synthesis ◽  
Prolyl Hydroxylase ◽  
Chick Embryos ◽  
Isolated Cells ◽  
Lysyl Hydroxylase ◽  
Tendon Cells

Collagen synthesis and the activities of prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase were studied in isolated chick-embryo tendon cells after the administration of cortisol acetate to the chick embryos. When the steroid was injected 1 day before isolation of the tendon cells, collagen synthesis was decreased, even though the enzyme activities were not changed. When cortisol acetate was given as repeated injections over a period of 4 days, both collagen synthesis and the enzyme activities decreased. The hydroxylase activities decreased even more than the two collagen glycosyltransferase activities, both in isolated cells and in whole chick embryos. The amount of prolyl hydroxylase protein diminished to the same extent as the enzyme activity, indicating that cortisol acetate inhibits enzyme synthesis. The inhibitory effect of cortisol acetate on collagen synthesis and on the enzyme activities was partially reversible in 3 days. Total protein synthesis was completely restored within this time. Only massive doses of cortisol acetate inhibited collagen synthesis in vitro. Additional experiments indicated that cortisol acetate did not decrease the rate of the enzyme reactions when added directly to the enzyme incubation mixtures. The results suggest that cortisol acetate decreases collagen synthesis both by its direct effect on collagen polypeptide-chain synthesis and by decreasing the activities of enzymes involved in post-translational modifications.

scholarly journals Underhydroxylated minor cartilage collagen precursors cannot form stable triple helices

1988 ◽  
Vol 250 (1) ◽  
pp. 65-70 ◽  
Author(s):  
C C Clark ◽  
C F Richards
Keyword(s):  
Chick Embryo ◽  
Triple Helix ◽  
Iron Chelator ◽  
Prolyl Hydroxylase ◽  
Type Ii ◽  
Native Structure ◽  
Lysyl Hydroxylase ◽  
Free Cells ◽  
Triple Helices ◽  
Matrix Free

Matrix-free cells from chick-embryo sterna were incubated with various concentrations of 2,2′-bipyridyl, an iron chelator that inhibits prolyl hydroxylase and lysyl hydroxylase. At concentrations in the region of 0.1 mM, significant effects on cartilage collagen hydroxylation and secretion were observed. When the underhydroxylated collagens were subsequently digested with chymotrypsin or chymotrypsin plus trypsin at 4 degrees C for 15 min, the minor cartilage collagen precursors (namely types IX and XI) were extensively degraded; type II procollagen was only partially susceptible and was converted into underhydroxylated collagen. The results demonstrate that there were significant differences in triple-helix stability among cartilage collagens such that the underhydroxylated minor collagen precursors were unable to attain a native structure under conditions where type II procollagen was successful.

scholarly journals Regulation of collagen post-translational modification in transformed human and chick-embryo cells

1981 ◽  
Vol 196 (3) ◽  
pp. 683-692 ◽  
Author(s):  
R Myllylä ◽  
K Alitalo ◽  
A Vaheri ◽  
K I Kivirikko
Keyword(s):  
Chick Embryo ◽  
Cell Lines ◽  
Rous Sarcoma Virus ◽  
Collagen Synthesis ◽  
Prolyl Hydroxylase ◽  
Post Translational Modification ◽  
Hydroxylase Activity ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Human Sarcoma

Changes in the regulation of collagen post-translational modification in transformed cells were studied in three established human sarcoma cell lines and in chick-embryo fibroblasts freshly transformed by Rous sarcoma virus. The collagens synthesized by all but one of these and by all the control human and chick-embryo cell lines were almost exclusively of types I and/or III. The relative rate of collagen synthesis and the amounts of prolyl hydroxylase activity and immunoreactive protein were markedly low in all the transformed human cell lines. The other enzymes studied, lysyl hydroxylase, hydroxylysyl galactosyltransferase and galactosylhydroxylysyl glucosyltransferase, never showed as large a decrease in activity as did prolyl hydroxylase, suggesting a more efficient regulation of the last enzyme than of the three others. The chick-embryo fibroblasts freshly transformed by Rous sarcoma virus differed from the human sarcoma cells in that prolyl hydroxylase activity was distinctly increased, whereas the decreases in immunoreactive prolyl hydroxylase protein and the three other enzyme activities were very similar to those in the simian-virus-40-transformed human fibroblasts. It seems possible that this increased prolyl hydroxylase activity is only a temporary phenomenon occurring shortly after the transformation, and may be followed by a decrease in activity later. The newly synthesized collagens of all the transformed cells that produced almost exclusively collagen types I and/or III had high extents of lysyl hydroxylation, and there was also an increase in the ratio of glycosylated to non-glycosylated hydroxylysine. The data suggest that one critical factor affecting modification is the rate of collagen synthesis, which affects the ratio of enzyme to substrate in the cell.

scholarly journals Labelling of prolyl hydroxylase tetrameric subunits in freshly isolated chick-embryo tendon cells and in certain chick-embryo tissues in vivo

1982 ◽  
Vol 204 (3) ◽  
pp. 737-742 ◽  
Author(s):  
K Majamaa ◽  
J Oikarinen
Keyword(s):  
Chick Embryo ◽  
Prolyl Hydroxylase ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Beta Subunits ◽  
Chase Period ◽  
Tendon Cells ◽  
Alpha Radioactivity ◽  
A Minor

The labelling of the subunits of prolyl 4-hydroxylase tetramers was studied in freshly isolated chick-embryo tendon cells and in chick-embryo tissues. In the former both the alpha- and beta-subunits of the tetramer were labelled during a 4 h labelling and 2 h chase period, although the radioactivity in the beta-subunit was much lower than in the alpha-subunit. The corresponding subunits of the enzyme from 12-day chick-embryo cartilaginous bone and heart were labelled in 7 h, again the beta-subunit much less than the alpha-subunit, the ratio of radioactivity in the beta-subunit to that in the alpha-subunit (beta/alpha-radioactivity) being 0.20 and 0.32 respectively. The beta/alpha-radioactivity then increased almost linearily with time between 7 and 24 h, by 9.5-fold in the cartilaginous bone and 3-fold in the heart, and beta/alpha-radioactivity values above 1.0 were reached. The free beta-subunit-size protein (the beta'-protein), which is also present in cells, had been labelled quite heavily by 7 h. The beta/alpha-radioactivity at 7h, determined in four tissues with different ratios of prolyl hydroxylase tetramers to total immunoreactive protein (tetramer percentage), was low in tissues with a high tetramer percentage. It is thus proposed that only a minor fraction of the beta'-protein must be processed to the tetrameric beta-subunit and utilized in the synthesis of the prolyl 4-hydroxylase tetramers.

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