Creatine analogue β-guanidinopropionic acid alters skeletal muscle AMP deaminase activity

American Journal of Physiology - Cell Physiology

Volumn 270, Issue 1 39-1, 1996, Pages

  Tullson, Peter C ^a   Rundell, Kenneth W ^b   Sabina, Richard L ^b   Terjung, Ronald L ^b  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

^b NONE

Author keywords

adenine nucleotides; deamination; enzyme regulation; inosine 5' monophosphate; purine nucleotide cycle

Indexed keywords

3 GUANIDINOPROPIONIC ACID PHOSPHATE; ADENOSINE MONOPHOSPHATE DEAMINASE; CREATINE; CREATINE DERIVATIVE; CREATINE PHOSPHATE; GUANIDINE DERIVATIVE; GUANIDINOPROPIONIC ACID; INOSINE PHOSPHATE; LACTIC ACID; MESSENGER RNA; PURINE NUCLEOTIDE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DEPLETION; DIET SUPPLEMENTATION; ENZYME ACTIVITY; FAST MUSCLE; GASTROCNEMIUS MUSCLE; MALE; MUSCLE CONTRACTION; MUSCLE TONE; MUSCLE TWITCH; NONHUMAN; ORAL DRUG ADMINISTRATION; PLANTARIS MUSCLE; PRIORITY JOURNAL; RAT; SKELETAL MUSCLE; SLOW MUSCLE; SOLEUS MUSCLE;

EID: 0030023801     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1996.270.1.c76     Document Type: Article

References (39)

1. Chen, S. C., P. R. Brown, and D. M. Rosie. Extraction procedures for use prior to HPLC nucleotide analysis using microparticle chemically bonded packings. J. Chromatogr. Sci. 15: 218-221, 1977.
2. Chevli, R., and C. D. Fitch. β-Guanidinopropionate and phosphorylated β-guanidinopropionate as substrates for creatine kinase. Biochem. Med. 21: 162-167, 1979.
3. Dudley, G. A., and R. L. Terjung. Influence of acidosis on AMP deaminase activity in contracting fast-twitch muscle. Am. J. Physiol. 248 (Cell Physiol. 17): C43-C50, 1985.
4. Dudley, G. A., P. C. Tullson, and R. L. Terjung. Influence of mitochondrial content on the sensitivity of respiratory control. J. Biol. Chem. 262: 9109-9114, 1987.
5. Fitch, C. D., and R. Chevli. Measurement of β-guanidinopropionate and phosphorylated β-guanidinopropionate in tissues. Anal. Biochem. 68: 196-201, 1975.
6. Fitch, C. D., R. Chevli, J. S. Petrofsky, and S. J. Kopp. Sustained isometric contraction of skeletal muscle depleted of phosphocreatine. Life Sci. 23: 1285-1291, 1978.
7. Fitch, C. D., M. Jellinek, R. H. Fitts, K. M. Baldwin, and J. O. Holloszy. Phosphorylated β-guanidinopropionate as a substitute for phosphocreatine in rat muscle. Am. J. Physiol. 228: 1123-1125, 1975.
8. Foley, J. M., G. R. Adams, and R. A. Meyer. Different effects of gradual vs. acute adenine nucleotide depletion on ATP cost of muscle contraction. Am. J. Physiol. 267 (Cell Physiol. 36): C1177-C1184, 1994.
9. Gori, Z., V. De Tata, M. Pollera, and E. Bergamini. Mitochondrial myopathy in rats fed with a diet containing β-guanidine propionic acid, an inhibitor of creatine entry in muscle cells. Br. J. Exp. Pathol. 69: 639-650, 1988.
10. Hood, D. A., J. Gorski, and R. L. Terjung. Oxygen cost of twitch and tetanic isometric contractions of rat skeletal muscle. Am. J. Physiol. 250 (Endocrinol. Metab. 13): E449-E456, 1986.
11. Laskowski, M. B., R. Chevli, and C. D. Fitch. Biochemical and ultrastructural changes in skeletal muscle induced by a creatine antagonist. Metabolism 30: 1080-1085, 1981.
12. Lowenstein, J. M. The purine nucleotide cycle revisited. Int. J. Sports Med. 11, Suppl. 2: S37-S46, 1990. (Corrigenda. Int. J. Sports Med. 11: Ocotber 1990, p. 411.)
13. Mahanna, D. A., C. D. Fitch, and V. W. Fischer. Effects of β-guanidinopropionic acid on murine skeletal muscle. Exp. Neurol. 68: 114-121, 1980.
14. Mahnke-Zizelman, D. K., and R. L. Sabina. Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5′-exons. J. Biol. Chem. 267: 20866-20877, 1992.
15. Maniatis, T., E. F. Fritsch, and J. Sambrook. Molecular Cloning: a Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1982.
16. Marquetant, R., R. L. Sabina, and E. W. Holmes. Identification of a noncatalytic domain in AMP deaminase that influences binding to myosin. Biochemistry 28: 8744-8749, 1989.
17. Meyer, R. A., T. R. Brown, B. L. Krilowicz, and M. J. Kushmerick. Phosphagen and intracellular pH changes during contraction of creatine-depleted rat muscle. Am. J. Physiol. 250 (Cell Physiol. 19): C264-C274, 1986.
18. Meyer, R. A., and R. L. Terjung. Differences in ammonia and adenylate metabolism in contracting fast and slow muscle. Am. J. Physiol 237 (Cell Physiol. 6): C111-C118, 1979.
19. Mineo, L, P. R. Clarke, R. L. Sabina, and E. W. Holmes. A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5′ splice donor site not present in the primary transcript of AMPD1. Mol. Cell. Biol. 10: 5271-5278, 1990.
20. Moerland, T. S., and M. J. Kushmerick. Contractile economy and aerobic recovery metabolism in skeletal muscle adapted to creatine depletion. Am. J. Physiol. 267 (Cell Physiol. 36): C127-C137, 1994.
21. Moerland, T. S., N. G. Wolf, and M, J. Kushmerick. Administration of a creatine analogue induces isomyosin transitions in muscle. Am. J. Physiol. 257 (Cell Physiol. 26): C810-C816, 1989.
22. Ohira, Y., M. Kanzaki, and C. S. Chen. Intramitochondrial inclusions caused by depletion of creatine in rat skeletal muscles. Jpn. J. Physiol. 38: 159-166, 1988.
23. Petrofsky, J. S., and C. D. Fitch. Contractile characteristics of skeletal muscles depleted of phosphocreatine. Pfluegers Arch. 384: 123-129, 1980.
24. Ren, J. M., and J. O. Holloszy. Adaptation of rat skeletal muscle to creatine depletion: AMP deaminase and AMP deamination. J. Appl. Physiol. 73: 2713-2716, 1992.
25. Rowley, G. L., A. L. Greenleaf, and G. L. Kenyon. On the specificity of creatine kinase. New glycocyamines and glycocyamine analogs related to creatine. J. Am. Chem. Soc. 93: 5542-5551, 1971.
26. Rundell, K. W., P. C. Tullson, and R. L. Terjung. Altered kinetics of AMP deaminase by myosin binding. Am. J. Physiol. 263 (Cell Physiol. 32): C294-C299, 1992.
27. Rundell, K. W., P. C. Tullson, and R. L. Terjung. AMP deaminase binding in contracting rat skeletal muscle. Am. J. Physiol. 263 (Cell Physiol. 32): C287-C293, 1992.
28. Sabina, R. L., W. N. Fishbein, G. Pezeshkpour, P. R. Clarke, and E. W. Holmes. Molecular analysis of the myoadenylate deaminase deficiencies. Neurology 42: 170-179, 1992.
29. Sabina, R. L., R. Marquetant, N. M. Desai, K. Kaletha, and E. W. Holmes. Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for tissue-specific and developmental regulation. J. Biol. Chem. 262: 12397-12400, 1987.
30. Sabina, R. L., T. Morisaki, P. Clarke, R. Eddy, T. B. Shows, C. C. Morton, and E. W. Holmes. Characterization of the human and rat myoadenylate deaminase genes. J. Biol. Chem. 265: 9423-9433, 1990.
31. Sabina, R. L., N. Ogasawara, and E. W. Holmes. Expression of three stage-specific transcripts of AMP deaminase during myogenesis. Mol. Cell. Biol. 9: 2244-2246, 1989.
32. Shoubridge, E. A., R. A. Challiss, D. J. Hayes, and G. K. Radda. Biochemical adaptation in the skeletal muscle of rats depleted of creatine with the substrate analogue β-guanidinopropionic acid. Biochem. J. 232: 125-131, 1985.
33. 31P NMR study of tetanic contraction in rat muscle depleted of phosphocreatine. Am. J. Physiol. 252 (Cell Physiol. 21): C532-C542, 1987.
34. Thakkar, J. K., D. R. Janero, C. Yarwood, and H. M. Sharif. Modulation of mammalian cardiac AMP deaminase by protein kinase C-mediated phosphorylation. Biochem. J. 291: 523-527, 1993.
35. Tovmasian, E. K., R. L. Hairapetian, E. V. Bykova, S. E. J. Severin, and A. V. Haroutunian. Phosphorylation of the skeletal muscle AMP-deaminase by protein kinase C. FEBS Lett. 259: 321-323, 1990.
36. Tullson, P. C., and R. L. Terjung. Adenine nucleotide metabolism in contracting skeletal muscle. Exercise Sport Sci. Rev. 19: 507-537, 1991.
37. Tullson, P. C., D. M. Whitlock, and R. L. Terjung. Adenine nucleotide degradation in slow-twitch red muscle. Am. J. Physiol. 258 (Cell Physiol. 27): C258-C265, 1990.
38. Van Kuppevelt, T. H., J. H. Veerkamp, W. N. Fishbein, N. Ogasawara, and R. L. Sabina. Immunolocalization of AMP-deaminase isozymes in human skeletal muscle and cultured muscle cells: concentration of isoform M at the neuromuscular junction. J. Histochem. Cytochem. 42: 861-868, 1994.
39. Wiseman, R. W., T. S. Moerland, P. B. Chase, R. Stuppard, and M. J. Kushmerick. High-performance liquid Chromatographie assays for free and phosphorylated derivatives of the creatine analogues β-guanidopropionic acid and 1-carhoxymethyl-2-iminoimidazolidine (cyclocreatine). Anal. Biochem. 204: 383-389, 1992.