Pancreastatin: Characterization of biological activity

Tao Zhang, Tohru Mochizuki, Masafumi Kogire, Jin Ishizuka, Noboru Yanaihara, James C. Thompson, George H. Greeley

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Pancreastatin (PST) (1-49) was first isolated from the porcine pancreas and can inhibit glucose-induced insulin release. PST (33-49), a PST C-terminal fragment, can also inhibit insulin release. The purpose of this study was to determine the shortest C-terminal biologically active fragment of PST, in terms of inhibition of insulin release from the isolated perfused rat pancreas. Porcine PST (1-49) and C-terminal fragments, PST (33-49), PST (35-49), PST (37-49) and PST (39-49) were synthesized by solid-phase methodology. PST (1-49), PST (33-49) and PST (35-49), at 10 nM, significantly (p <0.05) inhibited insulin release from isolated perfused rat pancreas: the first phase was inhibited by 15.6±2.4, 24.4±6.5 and 12.5±1.9% and the second phase, 18.9±2.7, 25.7±4.8 and 20.1±1.9% by PST (1-49), PST (33-49) and PST (35-49), respectively. PST (35-49) shows a dose-dependent inhibition of insulin release. PST (37-49) and PST (39-49) were, however, inactive. Our results indicate that the shortest C-terminal biologically active fragment is PST (35-49). These data further indicate that the C-terminal portion of PST is primarily responsible for the biological activity of PST.

Original languageEnglish (US)
Pages (from-to)1157-1160
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Dec 31 1990
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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