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. 1982 Sep 15;206(3):499–503. doi: 10.1042/bj2060499

Regulation of proline 3-hydroxylation and prolyl 3-hydroxylase and 4-hydroxylase activities in transformed cells.

K Majamaa, R Myllylä, K Alitalo, A Vaheri
PMCID: PMC1158616  PMID: 6293467

Abstract

Prolyl 3-hydroxylase activity and the extent of collagen proline 3-hydroxylation were studied in six transformed and three control human cell lines. In the transformed cell lines, the enzyme activity was markedly high in two, similar to that in control cells in two and significantly low in two. The extent of proline 3-hydroxylation was markedly high in cell lines with high enzyme activity, but it was also significantly high in some transformed cell lines with enzyme activities similar to those in the controls. The results thus suggest that, in addition to the amount of enzyme activity present, the rate of collagen synthesis also affects the extent of proline 3-hydroxylation in the newly synthesized collagen. The effect of acute cell transformation on prolyl 3-hydroxylase and 4-hydroxylase activities was studied by infecting chick-embryo fibroblasts with Rous sarcoma virus mutant NY68, temperature-sensitive for transformation. At the permissive temperature prolyl 3-hydroxylase activity showed a more rapid increase and decrease than did prolyl 4-hydroxylase activity, the maximal activity for both enzymes being about 2.5 times that in the control chick fibroblasts. When the transformed cells were shifted to the non-permissive temperature the decays in the elevated enzyme activities were similar, suggesting identical half-lives.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alitalo K., Keski-Oja J., Vaheri A. Extracellular matrix proteins characterize human tumor cell lines. Int J Cancer. 1981 Jun 15;27(6):755–761. doi: 10.1002/ijc.2910270605. [DOI] [PubMed] [Google Scholar]
  2. Alitalo K. Production of both interstitial and basement membrane procollagens by fibroblastic WI-38 cells from human embryonic lung. Biochem Biophys Res Commun. 1980 Apr 14;93(3):873–880. doi: 10.1016/0006-291x(80)91157-2. [DOI] [PubMed] [Google Scholar]
  3. Arbogast B. W., Yoshimura M., Kefalides N. A., Holtzer H., Kaji A. Failure of cultured chick embryo fibroblasts to incorporate collagen into their extracellular matrix when transformed by Rous sarcoma virus. An effect of transformation but not of virus production. J Biol Chem. 1977 Dec 25;252(24):8863–8868. [PubMed] [Google Scholar]
  4. Hata R. I., Peterkofsky B. Specific changes in the collagen phenotype of BALB 3T3 cells as a result of transformation by sarcoma viruses or a chemical carcinogen. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2933–2937. doi: 10.1073/pnas.74.7.2933. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kamine J., Rubin H. Coordinate control of collagen synthesis and cell growth in chick embryo fibroblasts and the effect of viral transformation on collagen synthesis. J Cell Physiol. 1977 Jul;92(1):1–11. doi: 10.1002/jcp.1040920102. [DOI] [PubMed] [Google Scholar]
  6. Kawai S., Hanafusa H. The effects of reciprocal changes in temperature on the transformed state of cells infected with a rous sarcoma virus mutant. Virology. 1971 Nov;46(2):470–479. doi: 10.1016/0042-6822(71)90047-x. [DOI] [PubMed] [Google Scholar]
  7. Kivirikko K. I., Myllylä R. Collagen glycosyltransferases. Int Rev Connect Tissue Res. 1979;8:23–72. doi: 10.1016/b978-0-12-363708-6.50008-4. [DOI] [PubMed] [Google Scholar]
  8. Kivirikko K. I., Myllylä R. Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 1982;82(Pt A):245–304. doi: 10.1016/0076-6879(82)82067-3. [DOI] [PubMed] [Google Scholar]
  9. Krieg T., Timpl R., Alitalo K., Kurkinen M., Vaheri A. Type III procollagen is the major collageneous component produced by a continuous rhabdomyosarcoma cell line. FEBS Lett. 1979 Aug 15;104(2):405–409. doi: 10.1016/0014-5793(79)80863-7. [DOI] [PubMed] [Google Scholar]
  10. Myllylä R., Alitalo K., Vaheri A., Kivirikko K. I. Regulation of collagen post-translational modification in transformed human and chick-embryo cells. Biochem J. 1981 Jun 15;196(3):683–692. doi: 10.1042/bj1960683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pihlajaniemi T., Myllylä R., Alitalo K., Vaheri A., Kivirikko K. I. Posttranslational modifications in the biosynthesis of type IV collagen by a human tumor cell line. Biochemistry. 1981 Dec 22;20(26):7409–7415. doi: 10.1021/bi00529a014. [DOI] [PubMed] [Google Scholar]
  12. Risteli J., Tryggvason K., Kivirikko K. I. A rapid assay for prolyl 3-hydroxylase activity. Anal Biochem. 1978 Feb;84(2):423–431. doi: 10.1016/0003-2697(78)90060-x. [DOI] [PubMed] [Google Scholar]
  13. Risteli J., Tuderman L., Tryggvason K., Kivirikko K. I. Effect of hepatic injury on prolyl 3-hydroxylase and 4-hydroxylase activities in rat liver and on immunoreactive prolyl 4-hydroxylase concentrations in the liver and serum. Biochem J. 1978 Jan 15;170(1):129–135. doi: 10.1042/bj1700129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Risteli L., Risteli J., Salo L., Kivirikko K. I. Intracellular enzymes of collagen biosynthesis in 3T6 fibroblasts and chick-embryo tendon and cartilage cells. Eur J Biochem. 1979 Jun;97(1):297–303. doi: 10.1111/j.1432-1033.1979.tb13114.x. [DOI] [PubMed] [Google Scholar]
  15. Sandmeyer S., Bornstein P. Declining procollagen mRNA sequences in chick embryo fibroblasts infected with rous sarcoma virus. Correlation with procollagen synthesis. J Biol Chem. 1979 Jun 25;254(12):4950–4953. [PubMed] [Google Scholar]
  16. Tryggvason K., Majamaa K., Kivirikko K. I. Prolyl 3-hydroxylase and 4-hydroxylase activities in certain rat and chick-embryo tissues and age-related changes in their activities in the rat. Biochem J. 1979 Jan 15;178(1):127–131. doi: 10.1042/bj1780127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Vaheri A., Kurkinen M., Lehto V. P., Linder E., Timpl R. Codistribution of pericellular matrix proteins in cultured fibroblasts and loss in transformation: fibronectin and procollagen. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4944–4948. doi: 10.1073/pnas.75.10.4944. [DOI] [PMC free article] [PubMed] [Google Scholar]

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