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. 1982 Sep;79(17):5438–5442. doi: 10.1073/pnas.79.17.5438

Redistribution of amylase activity accompanying its secretion by the pancreas.

K Miyasaka, S S Rothman
PMCID: PMC346913  PMID: 6182564

Abstract

Amylase activity in several tissue and body fluid compartments in the rat changed markedly when the secretion of digestive enzyme was augmented over a 3-hr period with a cholinergic agonist. As a result of stimulation, the pancreas was depleted of about one-third of its amylase activity and accounted for only 75% of the amount recovered from the animal, compared to 92% in the fasted state. Despite the continuous augmented secretion of the enzyme into the small intestine, no increase in amylase activity was detected there at the end of 3 hr. On the other hand, amylase activity in plasma and extracellular fluid increased by about an order of magnitude and accounted for 13% of the total pool, compared to approximately 1% in the fasted state. Amylase activity in several solid tissues also increased, including a 50- to 100-fold increase in parotid gland and an almost 10-fold increase in submandibular gland and kidney. The potential sources of the increased amylase activity in blood, the endocrine secretion of the enzyme by the pancreas, and its absorption from the intestine are considered. Changes in the amylase content of various tissues appear to reflect increased uptake due to increased plasma levels.

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Selected References

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

  1. Ceska M., Birath K., Brown B. A new and rapid method for the clinical determination of alpha-amylase activities in human serum and urine. Optimal conditions. Clin Chim Acta. 1969 Dec;26(3):437–444. doi: 10.1016/0009-8981(69)90071-0. [DOI] [PubMed] [Google Scholar]
  2. Geokas M. C., Largman C., Brodrick J. W., Fassett M. Molecular forms of immunoreactive pancreatic elastase in canine pancreatic and peripheral blood. Am J Physiol. 1980 Mar;238(3):G238–G246. doi: 10.1152/ajpgi.1980.238.3.G238. [DOI] [PubMed] [Google Scholar]
  3. Götze H., Rothman S. S. Amylase transport across ileal epithelium in vitro. Biochim Biophys Acta. 1978 Sep 11;512(1):214–220. doi: 10.1016/0005-2736(78)90231-6. [DOI] [PubMed] [Google Scholar]
  4. Götze H., Rothman S. S. Enteropancreatic circulation of digestive enzyme as a conservation mechanism. Nature. 1975 Oct 16;257(5527):607–609. doi: 10.1038/257607a0. [DOI] [PubMed] [Google Scholar]
  5. Heinrich H. C., Gabbe E. E., Brüggemann J., Icagić F., Classen M. Enteropancreatic circulation of trypsin in man. Klin Wochenschr. 1979 Dec 3;57(23):1295–1297. doi: 10.1007/BF01492985. [DOI] [PubMed] [Google Scholar]
  6. Isenman L. D., Rothman S. S. Transpancreatic transport of digestive enzyme. Biochim Biophys Acta. 1979 Jul 4;585(3):321–332. doi: 10.1016/0304-4165(79)90077-1. [DOI] [PubMed] [Google Scholar]
  7. Isenman L. D., Rothman S. S. Transport of alpha-amylase across the basolateral membrane of the pancreatic acinar cell. Proc Natl Acad Sci U S A. 1977 Sep;74(9):4068–4072. doi: 10.1073/pnas.74.9.4068. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Lake-Bakaar G., Rubio C. E., McKavanagh S., Potter B. J., Summerfield J. A. Metabolism of 125I-labelled trypsin in man: evidence of recirculation. Gut. 1980 Jul;21(7):580–586. doi: 10.1136/gut.21.7.580. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Leibow C., Rothman S. S. Enteropancreatic circulation of digestive enzymes. Science. 1975 Aug 8;189(4201):472–474. doi: 10.1126/science.1154022. [DOI] [PubMed] [Google Scholar]
  10. Levitt M. D., Ellis C. J., Murphy S. M., Schwartz M. L. Study of the possible enteropancreatic circulation of pancreatic amylase in the dog. Am J Physiol. 1981 Jul;241(1):G54–G58. doi: 10.1152/ajpgi.1981.241.1.G54. [DOI] [PubMed] [Google Scholar]
  11. Miyasaka K., Rothman S. S. Endocrine secretion of alpha-amylase by the pancreas. Am J Physiol. 1981 Aug;241(2):G170–G175. doi: 10.1152/ajpgi.1981.241.2.G170. [DOI] [PubMed] [Google Scholar]
  12. Papp M., Fehér S., Németh E. P., Somogyi J., Folly G. Exit routes for secretory proteins from the dog pancreas. Acta Physiol Acad Sci Hung. 1980;56(4):401–410. [PubMed] [Google Scholar]
  13. Rothman S. S. Enzyme secretion in the absense of zymogen granules. Am J Physiol. 1975 Jun;228(6):1828–1834. doi: 10.1152/ajplegacy.1975.228.6.1828. [DOI] [PubMed] [Google Scholar]
  14. Saito A., Kanno T. Concentration of pancreozymin as a determinant of the exocrine-endocrine partition of pancreatic enzymes. Jpn J Physiol. 1973 Oct;23(5):477–495. doi: 10.2170/jjphysiol.23.477. [DOI] [PubMed] [Google Scholar]

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