Species variation in pancreatic islet monoamine uptake and action
- 1 April 1977
- journal article
- research article
- Published by American Diabetes Association in Diabetes
- Vol. 26 (4), 257-261
- https://doi.org/10.2337/diabetes.26.4.257
Abstract
There are conflicting data in the literature regarding the role of monoamines in the secretion of insulin. In order to clarify the contribution that species variation may make to these divergent results, the uptake of serotonin (5-HT), dopamine (DA), and their precursor amino acids, 5-hydroxytryptophan (5-HTP) and L-dopa, into islets was studied. Islets from golden hamsters, rabbits, guinea pigs, and obese, hyperglycemie mice were isolated by the collagenase technique. The islets were incubated in Krebs-Ringer buffer in the presence of 14C-labeled monoamines or their precursors. At 30-minute intervals after initiating the study, the incubation mixture was passed through a Millipore filter. The retained islets were disrupted by sonication and the radioactivity counted. The ratio of the uptake of 5-HTP to 5-HT was at least 3:1 in the hamster, guinea pig, and mouse. In the rabbit the ratio was 1:1. A similar relationship was noted for the uptake of L-dopa and DA. The in-vitro results were confirmed by the in-vivo studies, in which hamsters were injected with 14C 5-HT or 5-HTP, followed by isolation of the islets. We conclude that there is significant species variation in the uptake of these monoamines and their precursors.This publication has 5 references indexed in Scilit:
- Preparation of islets of langerhans from rabbits and hamsters by the collagenase digestion techniqueActa Diabetologica, 1975
- Radioisotopic studies of the binding, exchange, and distribution of 5-hydroxytryptamine synthesized from its radioactivity precursorThe Journal of Physiology, 1966
- Coated Charcoal Immunoassay of InsulinJournal of Clinical Endocrinology & Metabolism, 1965
- Autoradiographic distribution of 5-hydroxytryptamine and 5-hydroxytryptophan in the mouseBiochemical Pharmacology, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951