Bioactivity of human pancreastatin and its localization in pancreas.
Synthetic human pancreastatin and its C-terminal fragment were first evaluated with respect to the biological activity on the insulin secretion in the isolated rat islets. Both these pancreastatins inhibited glucose-stimulated insulin secretion at a concentration of 100 nM. The relative molar potency of human pancreastatin compared to that of porcine pancreastatin was equivalent. The pancreastatin-reactive cells were widely located in the islets of Langerhans, and not observed in exocrine acinar cells by immunocytochemistry using human pancreastatin C-terminal specific antibody. These results suggest that human pancreastatin may modulate endocrine function of the pancreas, especially insulin secretion.
Funakoshi
A
A
National Kyushu Cancer Center, Fukuoka, Japan.
Jimi
A
A
Yasunami
Y
Y
Tateishi
K
K
Funakoshi
S
S
Tamamura
H
H
Yajima
H
H
D000595:Amino Acid Sequence; D000818:Animals; D053379:Chromogranin A; D005947:Glucose / Q000494:pharmacology; D006801:Humans; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism*; D000078790:Insulin Secretion; D007515:Islets of Langerhans / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D008969:Molecular Sequence Data; D010187:Pancreatic Hormones / Q000032:analysis / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology; D051381:Rats; D013045:Species Specificity; D013552:Swine
D053379:Chromogranin A; D007328:Insulin; D010187:Pancreatic Hormones; D010446:Peptide Fragments; C050836:pancreastatin; D005947:Glucose