Bioactivity of synthetic C-terminal fragment of rat pancreastatin on endocrine pancreas.
A C-terminal fragment of rat pancreastatin, 26-residue peptide amide was synthesized by the Fmoc-based solid phase method and its biological activity was evaluated for the first time in the conscious rat. Rat pancreastatin inhibited glucose-stimulated insulin secretion and elevated blood glucose levels in a concentration of 10 nmol/kg/h. The relative molar potency of that of porcine is equivalent. This study suggests that the synthetic rat pancreastatin has a biological activity, and may play a physiological role in the endocrine pancreas.
Funakoshi
A
A
National Kyushu Cancer Center, Fukuoka, Japan.
Miyasaka
K
K
Kitani
K
K
Tamamura
H
H
Funakoshi
S
S
Yajima
H
H
D000818:Animals; D001786:Blood Glucose / Q000378:metabolism; D053379:Chromogranin A; D005947:Glucose / Q000494:pharmacology; D007328:Insulin / Q000378:metabolism*; D000078790:Insulin Secretion; D007515:Islets of Langerhans / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D010187:Pancreatic Hormones / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013552:Swine
D001786:Blood Glucose; D053379:Chromogranin A; D007328:Insulin; D010187:Pancreatic Hormones; D010446:Peptide Fragments; C050836:pancreastatin; D005947:Glucose