HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via ISI Web of Science (1) Citing Articles via Google Scholar Google Scholar Articles by Hoa, N. K. Articles by Östenson, C.-G. Search for Related Content PubMed Articles by Hoa, N. K. Articles by Östenson, C.-G.

¹ Department of Molecular Medicine and Surgery, Karolinska Institute, Karolinska University Hospital, SE-171 76 Stockholm, Sweden
² Department of Pharmacology, Hanoi Medical University, Hanoi, Vietnam
³ Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden
⁴ Institute of Material Medica, Hanoi, Vietnam
⁵ Department of Medicine, Karolinska Institute, Karolinska University Hospital, Stockholm, Sweden

(Requests for offprints should be addressed to N K Hoa who is now at Department of Pharmacology, Hanoi Medical University, 1-Ton That Tung, Hanoi, Vietnam; Email: hoa.nguyen.khanh{at}ki.se)

We recently showed that phanoside, a gypenoside isolated from the plant Gynostemma pentaphyllum, stimulates insulin secretion from rat pancreatic islets. To study the mechanisms by which phanoside stimulates insulin secretion. Isolated pancreatic islets of normal Wistar (W) rats and spontaneously diabetic Goto-Kakizaki (GK) rats were batch incubated or perifused. At both 3.3 and 16.7 mM glucose, phanoside stimulated insulin secretion several fold in both W and diabetic GK rat islets. In perifusion of W islets, phanoside (75 and 150 µM) dose dependently increased insulin secretion that returned to basal levels when phanoside was omitted. When W rat islets were incubated at 3.3 mM glucose with 150 µM phanoside and 0.25 mM diazoxide to keep K-ATP channels open, insulin secretion was similar to that in islets incubated in 150 µM phanoside alone. At 16.7 mM glucose, phanoside-stimulated insulin secretion was reduced in the presence of 0.25 mM diazoxide (P<0.01). In W islets depolarized by 50 mM KCl and with diazoxide, phanoside stimulated insulin release twofold at 3.3 mM glucose but did not further increase the release at 16.7 mM glucose. When using nimodipine to block L-type Ca²⁺ channels in B-cells, phanoside-induced insulin secretion was unaffected at 3.3 mM glucose but decreased at 16.7 mM glucose (P<0.01). Pretreatment of islets with pertussis toxin to inhibit exocytotic G_e-protein did not affect insulin response to 150 µM phanoside. Phanoside stimulated insulin secretion from Wand GK rat islets. This effect seems to be exerted distal to K-ATP channels and L-type Ca²⁺ channels, which is on the exocytotic machinery of the B-cells.