Clinical Chemistry
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Clinical Chemistry 19: 387-389, 1973;
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Clinical Chemistry, Vol 19, 387-389, Copyright © 1973 by the American Association for Clinical Chemistry

Interpretation of Hyperamylasemia in Diabetic Coma

Francesco Belfiore 1 and Elena Napoli 1

1 I° Istituto di Clinica Medica dell'Università di Catania, Ospedale Garibaldi, 95123 Catania, Italy.

In sera of patients with diabetic coma, amylase activity was markedly elevated and closely correlated with the activity of some lysosomal enzymes, including beta-glucuronidase, N-acetyl-beta-glucosaminidase, and acid phosphatase. All these enzyme activities returned to normal with the normalization of glycemia. Activities of serum lipase, aspartate and alanine aminotransferases, aldolase, and lactate dehydrogenase were not changed. Since liver amylase, although primarily contained in microsomes, shows "latency" and is activated by several agents as are lysosomal enzymes, these findings might be regarded as a further evidence of a similarity between amylase and lysosomal enzymes, and make probable the hypothesis that a process of "activation" occurring in liver might be the cause of increased amylase activity in serum as well as of lysosomal enzymes.


Key Words: lysosomal enzymes • source of amylase in serum and mechanism of supranormal activity • "activation" of enzymes in tissue

Submitted on December 12, 1972
Accepted on January 5, 1973




The following articles in journals at HighWire Press have cited this article:


Home page
 ANN INTERN MEDHome page
F. VINICOR, L. M. LEHRNER, R. C. KARN, and A. D. MERRITT
Hyperamylasemia in Diabetic Ketoacidosis: Sources and Significance
Ann Intern Med, August 1, 1979; 91(2): 200 - 204.
[Abstract] [PDF]

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 JAMAHome page
E. vanSonnenberg and C. S. Pitchumoni
Prolonged Hyperamylasemia in Diabetic Ketoacidosis
JAMA, August 2, 1976; 236(5): 482 - 483.
[Abstract] [PDF]


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Copyright © 1973 by the American Association for Clinical Chemistry.