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Prolonged exercise causes an increase in the activity of galactosylhydroxylysyl glucosyltransferase and in the concentration of type III procollagen aminopropeptide in human serum

  • Heart, Circulation, Respiration and Blood; Environmental and Exercise Physiology
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Abstract

The effect of prolonged heavy physical exercise on serum galactosylhydroxylysyl glucosyltransferase activity (S-GGT) and serum type III procollagen aminoterminal propeptide (S-Pro(III)-N-P) concentration was studied in healthy male long-distance runners. S-GGT increased gradually by about 70% (p<0.01) during a competitive 24-h run, and a rising trend was also observed in S-Pro(III)-N-P. After the termination of the run S-GGT was normalized in two days, but the increase in S-Pro(III)-N-P continued up to one day after the race, reaching nearly 40% (p<0.005). The alterations in S-GGT and S-Pro(III)-N-P showed no significant correlation with S-CK, S-LDH or the distance run. The most likely explanation for the increases in S-GGT and S-Pro(III)-N-P is that prolonged heavy exercise injures the collagen-synthesizing cells of the connective tissue, leading to a short-term increase in type III procollagen production.

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References

  • Anttinen H (1977) Collagen glucosyltransferase activity in human serum. Clin Chim Acta 77:323–330

    Google Scholar 

  • Anttinen H, Järvensivu PM, Savolainen E-R (1981) Serum galactosylhydroxylysyl glucosyltransferase in acute myocardial infarction and during subsequent collagen scar formation. Eur J Clin Invest 11:375–379

    Google Scholar 

  • Bolarin D, Savolainen E-R, Kivirikko KI (1982) Enzymes of collagen synthesis and type III procollagen amino-propeptide in serum from Nigerians with hepatocellular carcinoma and other malignant diseases Int J Cancer 29:401–405

    Google Scholar 

  • Bolarin D, Savolainen E-R, Kivirikko KI (1984) Three serum markers of collagen biosynthesis in Nigerians with eirrhosis and various infections disease. Eur J Clin Invest 14:90–95

    Google Scholar 

  • Greenberg I, Arneson L (1967) Exertional rhabdomyolysis with myoglobinemia in a large group of military trainees Neurology 17:216–222

    Google Scholar 

  • Higman B, Altland PD (1963) Effects of exercise and training on serum enzyme and tissue changes in rats. Am J Physiol 38:162–166

    Google Scholar 

  • Kivirikko KI, Kuivaniemi H (1986) Post-translational modifications of collagen and their alterations in heritable diseases. In: Uitto J, Perejda AJ (eds) Diseases of connective tissue. The molecular pathology of the extracellular matrix. Marcel Dekker, New York, pp 263–292

    Google Scholar 

  • Kivirikko KI, Myllylä R (1979) Collagen glycosyltransferases. Int Rev Conn Tissue Res 8:23–72

    Google Scholar 

  • Kivirikko KI, Myllylä R (1982) Post-translational modifications. In: Weiss JB, Jayson MIV (eds) Collagen in health and disease. Churchill Livingstone, Edinburgh, pp 101–120

    Google Scholar 

  • Kuutti-Savolainen E-R (1979) Enzymes of collagen biosynthesis in skin and serum in dermatological diseases. II. Serum enzymes. Clin Chim Acta 96:53–58

    Google Scholar 

  • Kuutti-Savolainen E-R, Risteli J, Miettinen TA, Kivirikko KI (1979b) Collagen biosynthesis enzymes in serum and hepatic tissue in liver disease. I. Prolyl hydroxylase. Eur J Clin Invest 9:89–95

    Google Scholar 

  • Kuutti-Savolainen E-R, Anttinen H, Miettinen TA Kivirikko KI (1979a) Collagen biosynthesis enzymes in serum and hepatic tissue in liver disease. II. Galactosylhydroxylysyl glucosyltransferase. Eur J Clin Invest 9:97–101

    Google Scholar 

  • Mayne R (1982) Muscle. In: Weiss JB, Jayson MIV (eds) Collagen in health and disease. Churchill Livingstone, Edinburgh, pp 445–455

    Google Scholar 

  • Menashi S, Grant ME (1979) Studies on the collagen glucosyltransferase activity present in platelets and plasma. Biochem J 178:777–784

    Google Scholar 

  • Myllylä R, Risteli L, Kivirikko KI (1975) Assay of collagen-glucosyltransferase activities and preliminary characterization of enzymic reactions with transferases from chick embryo cartilage. Eur J Biochem 52:401–410

    Google Scholar 

  • Myllylä R, Risteli L, Kivirikko KI (1976) Collagen glucosyltransferase. Partial purification and characterization of the enzyme from whole chick embryos and chick embryo cartilage. Eur J Biochem 61:59–67

    Google Scholar 

  • Myllylä R, Myllylä VV, Tolonen U, Kivirikko KI (1982) Changes in collagen metabolism in diseased muscle. I. Biochemical studies. Arch Neurol 39:752–755

    Google Scholar 

  • Myllylä R, Salminen A, Peltonen L, Takala TES, Vihko V (1986) Collagen metabolism of mouse skeletal muscle during the repair of exercise injuries. Pflügers Arch 407:64–70

    Google Scholar 

  • Niemelä K, Palatsi I, Ikäheimo M, Takkunen J, Vuori J (1984) Evidence of impaired left ventricular performance after an uninterrupted competitive 24-hour run. Circulation 70:350–356

    Google Scholar 

  • Peltonen L, Myllylä R, Tolonen U, Myllylä VV (1982) Changes in collagen metabolism in diseased muscle. II. Immunohistochemical studies. Arch Neurol 39:756–759

    Google Scholar 

  • Prockop DJ, Kivirikko KI, Tuderman L, Guzman N (1979) The biosynthesis of collagen and its disorders. N Engl J Med 301:13–23, 77–85

    Google Scholar 

  • Risteli L, Risteli J (1986) Radioimmunoassays for monitoring connective tissue metabolism. Rheumatology 10:216–245

    Google Scholar 

  • Rojkind M (1984) The blue glass and predictive value of serum aminoterminal propeptide of type III procollagen as a marker of liver fibrosis. Hepatology 4:977–978

    Google Scholar 

  • Rohde H, Vargas L, Hahn E, Kalbfleisch H, Bruguera M, Timpl R (1979) Radioimmunoassay for type III procollagen peptide and its application to human liver disease. Eur J Clin Invest 9:451–459

    Google Scholar 

  • Rohde H, Langer I, Krieg T, Timpl R (1983) Serum and urine analysis of the aminoterminal procollagen peptide type III by radioimmunoassay with antibody Fab fragments. Coll Rel Res 3:371–379

    Google Scholar 

  • Savolainen E-R, Goldberg B, Leo MA, Velez M, Lieber CS (1984) Diagnostic value of serum procollagen peptide measurements in alcoholic liver disease. Alcoholism: clinical and experimental research 8:384–389

    Google Scholar 

  • Savolainen E-R, Micttinen TA, Pikkarainen P, Salaspuro M, Kivirikko KI (1983) Enzymes of collagen synthesis and type III procollagen amino-propeptide in the evaluation ofd-penicillamine and medroxyprogesterone treatments of primary biliary eirrhosis. Gut 24:136–142

    Google Scholar 

  • Takala TES, Myllylä R, Salminen A, Anttinen H, Vihko V (1983) Increased activities of prolyl 4-hydroxylase and galactosylhydroxylysyl glucosyltransferase enzymes of collagen biosynthesis, in skeletal muscle of endurance trained mice. Pflügers Arch 399:271–274

    Google Scholar 

  • Vihko V, Salminen A, Rantamäki J (1978) Acid hydrolase activity in red and white skeletal muscle of mice during a two-week period following exhausting exercise. Pflügers Arch 378:99–106

    Google Scholar 

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Takala, T.E.S., Vuori, J., Anttinen, H. et al. Prolonged exercise causes an increase in the activity of galactosylhydroxylysyl glucosyltransferase and in the concentration of type III procollagen aminopropeptide in human serum. Pflugers Arch. 407, 500–503 (1986). https://doi.org/10.1007/BF00657507

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  • DOI: https://doi.org/10.1007/BF00657507

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