mRNA levels for α-subunit of prolyl 4-hydroxylase and fibrillar collagens in immobilized rat skeletal muscle

Journal of Applied Physiology

Volumn 87, Issue 1, 1999, Pages 90-96

  Han, Xiao Yan ^a   Wang, Wei ^a   Myllylä, Raili ^b   Virtanen, Paula ^b   Karpakka, Jarmo ^b   Takala, Timo E S ^a  

^a UNIVERSITY OF JYVÄSKYLÄ   (Finland)

^b UNIVERSITY OF OULU   (Finland)

Author keywords

Hydroxyproline; Muscle atrophy; Posttranslational modification; Pretranslational control

Indexed keywords

COLLAGEN; MESSENGER RNA; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE;

ALPHA CHAIN; ANIMAL TISSUE; ARTICLE; COLLAGEN METABOLISM; ENZYME ACTIVITY; ENZYME MODIFICATION; HYDROXYLATION; IMMOBILIZED CELL; MECHANICAL STRESS; MUSCLE CONTRACTION; NONHUMAN; PLANTARIS MUSCLE; PRIORITY JOURNAL; PROTEIN PROCESSING; RAT; RECEPTOR DOWN REGULATION; SKELETAL MUSCLE;

EID: 0032814336     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1999.87.1.90     Document Type: Article

References (39)

1. Babij, P., and F. W. Booth. α-Actin and cytochrome c mRNAs in atrophied adult rat skeletal muscle. Am. J. Physiol. 254 (Cell Physiol. 23): C651-C656, 1988.
2. Bennett, V. D., and S. L. Adams. Identification of a cartilage-specific promoter within intron 2 of the chick alpha 2(I) collagen gene. J. Biol. Chem. 265: 2223-2230, 1990.
3. Berg, R. A., W. W. Kao, and N. L. Kedersha. The assembly of tetrameric prolyl hydroxylase in tendon fibroblasts from newly synthesized alpha-subunits and from preformed cross-reacting protein. Biochem. J. 189: 491-499, 1980.
4. Blumenkrantz, N., and G. Asboe-Hansen. A quick and specific assay for hydroxyproline. Anal. Biochem. 55: 288-291, 1973.
5. Cheng, S.-Y., Q.-H. Gong, C. Parkison, E. A. Robinson, E. Appella, G. T. Merlino, and I. Pastan. The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J. Biol. Chem. 262: 11221-11227, 1987.
6. Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
7. Davis, L. G., M. D. Dibner, and J. F. Battey. Basic Methods in Molecular Biology. New York: Elsevier, 1986, p. 143-146.
8. Goldspink, G., A. Scutt, P. T. Loughna, D. J. Wells, T. Jaenicke, and G. F. Gerlach. Gene expression in skeletal muscle in response to stretch and force generation. Am. J. Physiol. 262 (Regulatory Integrative Comp. Physiol. 31): R356-R363, 1992.
9. Helaakoski, T., L. Pajunen, K. I. Kivirikko, and T. Pihlajaniemi. Increases in mRNA concentrations of the alpha and beta subunits of prolyl 4-hydroxylase accompany increased gene expression of type IV collagen during differentiation of mouse F9 cells. J. Biol. Chem. 265: 11413-11416, 1990.
10. Helaakoski, T., K. Vuori, R. Myllylä, K. I. Kivirikko, and T. Pihlajaniemi. Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc. Natl. Acad. Sci. USA 86: 4392-4396, 1989.
11. Henkel, W., and R. W. Glanville. Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha1(I) and alpha1 (III) chains in the formation of intermolecular crosslinks. Eur. J. Biochem. 122: 205-213, 1982.
12. Jozsa, L., J. Thoring, M. Jarvinen, P. Kannus, M. Lehto, and M. Kvist. Quantitative alterations in intramuscular connective tissue following immobilization: an experimental study in the rat calf muscles. Exp. Mol. Pathol. 49: 267-278, 1988.
13. Karpakka, J., K. Väänänen, S. Orava, and T. E. Takala. The effects of preimmobilization training and immobilization on collagen synthesis in rat skeletal muscle. Int. J. Sports Med. 11: 484-488, 1990.
14. Karpakka, J., P. Virtanen, K. Väänänen, S. Orava, and T. E. Takala. Collagen synthesis in rat skeletal muscle during immobilization and remobilization. J. Appl. Physiol. 70: 1775-1780, 1991.
15. Kedersha, N. L., J. S. Tkacz, and R. A. Berg. Biosynthesis of prolyl hydroxylase: evidence for two separate dolichol-media pathways of glycosylation. Biochemistry 24: 5960-5967, 1985.
16. Keene, D. R., L. Y. Sakai, H. P. Bachinger, and R. E. Burgeson. Type III collagen can be present on banded collagen fibrils regardless of fibril diameter. J. Cell Biol. 105: 2393-2402, 1987.
17. + RNA, and mRNA in skeletal muscle. Am. J. Physiol. 260 (Cell Physiol. 29): C409-C416, 1991.
18. Kivirikko, K. I., T. Helaakoski, K. Tasanen, K. Vuori, R. Myllylä, T. Parkkonen, and T. Pihlajaniemi. Molecular biology of prolyl 4-hydroxylase. Ann. NY Acad. Sci. 580: 132-142, 1990.
19. Kivirikko, K. I., and R. Myllylä. The hydroxylation of prolyl and lysyl residues. In: The Enzymology of Post-Translational Modification of Protein, edited by R. B. Freedman and H. Hawkins. London: Academic, 1980, p. 53-104.
20. Kivirikko, K. I., and R. Myllylä. Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 82: 245-304, 1982.
21. Kivirikko, K. I., R. Myllylä, and T. Pihlajaniemi. Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit. FASEB J. 3: 1609-1617, 1989.
22. Koivu, J., R. Myllyla, T. Helaakoski, T. Pihlajaniemi, K. Tasanen, and K. I. Kivirikko. A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. J. Biol. Chem. 262: 6447-6449, 1987.
23. Kovanen, V. Effects of ageing and physical training on rat skeletal muscle. An experimental study on the properties of collagen, laminen, and fibre types in muscle serving different functions. Acta Physiol. Scand. 135, Suppl. 577: S1-S56, 1989.
24. Ku, Z., and D. B. Thomason. Soleus muscle nascent polypeptide chain elongation slows protein synthesis rate during non-weight-bearing activity. Am. J. Physiol. 267 (Cell Physiol. 36): C115-C126, 1994.
25. Laurent, G. J. Dynamic state of collagen: pathways of collagen degradation in vivo and their possible role in regulation of collagen mass. Am. J. Physiol. 252 (Cell Physiol. 21): C1-C9, 1987.
26. Loidl, H. R., J. M. Brinker, M. May, T. Pihlajaniemi, S. Morrow, J. Rosenbloom, and J. C. Myers. Molecular cloning and carboxyl-propeptide analysis of human type III procollagen. Nucleic Acids Res. 12: 9383-9394, 1984.
27. Majamaa, K., E.-R. Kuutti-Savolainen, L. Tuderman, and K. I. Kivirikko. Turnover of prolyl hydroxylase tetramers and the monomer-size protein in chick-embryo cartilaginous bone and lung in vivo. Biochem. J. 178: 313-322, 1979.
28. Mayne, R. Collagen in Health and Disease. New York: Churchill Livingstone, 1982, p. 445-455.
29. Morrison, P. R., G. W. Muller, and F. W. Booth. Actin synthesis rate and mRNA level increase during early recovery of atrophied muscle. Am. J. Physiol. 253 (Cell Physiol. 22): C205-C209, 1987.
30. Pihlajaniemi, T., T. Helaaskoski, K. Tasanen, R. Myllylä, M.-L. Huhtala, J. Koivu, and K. I. Kivirikko. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6: 643-649, 1987.
31. Reeds, P. J., R. M. Palmer, and R. H. Smith. Protein and collagen synthesis in rat diaphragm muscle incubated in vitro and the effect of alterations in tension produced by electrical or mechanical means. Int. J. Biochem. 11: 7-14, 1980.
32. Sandberg, M., M. Tamminen, H. Hirvonen, E. Vuorio, and T. Pihlajaniemi. Expression of mRNAs coding for the 1 chain of type XIII collagen in human fetal tissues: comparison with expression of mRNAs for collagen types I, II and III. J. Cell Biol. 109: 1371-1379, 1989.
33. Savolainen, J., V. Myllylä, R. Myllylä, V. Vihko, K. Väänänen, and T. E. S. Takala. Effects of denervation and immobilization on collagen synthesis in rat skeletal muscle and tendon. Am. J. Physiol. 254 (Regulatory Integrative Comp. Physiol. 23): R897-R902, 1988.
34. Savolainen, J., K. Väänänen, J. Puranen, T. E. Takala, J. Komulainen, and V. Vihko. Collagen synthesis and proteolytic activities in rat skeletal muscles: effect of cast-immobilization in the lengthened and shortened positions. Arch. Phys. Med. Rehabil. 69: 964-969, 1988.
35. Savolainen, J., K. Väänänen, V. Vihko, J. Puranen, and T. E. S. Takala. Effect of immobilization on collagen synthesis in rat skeletal muscles. Am. J. Physiol. 252 (Regulatory Integrative Comp. Physiol. 21): R883-R888, 1987.
36. Thomason, D. B., R. B. Biggs, and F. W. Booth. Protein metabolism and β-myosin heavy-chain mRNA in unweighted soleus muscle. Am. J. Physiol. 257 (Regulatory Integrative Comp. Physiol. 26): R300-R305, 1989.
37. Walchli, C., M. Koch, M. Chiquet, B. F. Odermatt, and B. Trueb. Tissue-specific expression of the fibril-associated collagens XII and XIV. J. Cell Sci. 107: 669-681, 1994.
38. Watson, P. A., J. P. Stein, and F. W. Booth. Changes in actin synthesis and α-actin-mRNA content in rat muscle during immobilization. Am. J. Physiol. 247 (Cell Physiol. 16): C39-C44, 1984.
39. Yeowell, H. N., S. Murad, and S. R. Pinnell. Hydralazine differentially increases mRNAs for the alpha and beta subunits of prolyl 4-hydroxylase whereas it decreases pro alpha 1(I) collagen mRNAs in human skin fibroblasts. Arch. Biochem. Biophys. 289: 399-404, 1991.