Literature DB >> 2428690

Newly synthesized amylase, lipase and serine proteases are transported at different rates in rat pancreas.

J Iovanna, D Giorgi, J C Dagorn.   

Abstract

The rates of intracellular transport of newly synthesized amylase, lipase, trypsinogen and chymotrypsinogen were compared in the anaesthesized rat pancreas by measuring their rates of secretion while keeping their relative rates of synthesis in a steady state. It is concluded that pancreatic proteins are not transported all at the same rate through the acinar cell. Among the four enzymes studied, proteolytic enzymes are transported faster than lipase, and amylase is the slowest. The relative rates of transport of these enzymes are not altered by secretory stimulation, since similar results were obtained in the basal state and under constant caerulein infusion (300 ng/kg/h).

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Year:  1986        PMID: 2428690     DOI: 10.1159/000199327

Source DB:  PubMed          Journal:  Digestion        ISSN: 0012-2823            Impact factor:   3.216


  2 in total

Review 1.  The asynchronous transport of secretory proteins in the exocrine pancreas. Compatibility with the hypothesis of a paragranular pathway?

Authors:  A R Beaudoin
Journal:  Int J Pancreatol       Date:  1988-12

2.  Nonparallel patterns of circadian pancreatic and biliary secretions in fasting rats.

Authors:  B Glasbrenner; L Dürrschnabel; M Büchler; P Malfertheiner
Journal:  Int J Pancreatol       Date:  1992-06
  2 in total

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