UNSPECIFIED. (2004) Expression of 25-hydroxyvitamin D-3-1 alpha-hydroxylase in pancreatic islets. Journal of Molecular Biology, 89-90 (1-5 Sp. Iss. SI). pp. 121-125. ISSN 0960-0760

Full text not available from this repository.

Abstract

A number of studies have suggested that Vitamin D has a potential role in the development/treatment of diabetes. These effects may be mediated by circulating levels of I alpha,25(OH)(2)D-3, but local production of 1alpha,25(OH)2D3, catalysed by the enzyme 25-hydroxyvitamin D-3-1alpha-hydroxylase (1alpha-OHase), is also likely to be important. RT-PCR analyses demonstrated that both isolated rat islets and MIN6 cells (mouse insulin-secreting cell line, characteristic of P cells) expressed 1alpha-OHase mRNA. The transcript in both cell types was similar to that seen in HKC-8 cells (a renal cell line, which expresses 1alpha-OHase). Western blot analysis and immunolocalisation identified I alpha-OHase protein in MIN6 cells and human pancreatic tissue. In addition, suspensions of rat islets were able to convert [H-3]-25-hydroxyvitamin D-3 to [H-3]-1alpha,25(OH)(2)D-3, demonstrating 1alpha-OHase activity. Both cell systems expressed the Vitamin D receptor and 1alpha,25(OH)(2)D-3 (50 nM) evoked a rapid rise in [Ca2+], in MIN6 cells. This data clearly demonstrates islets are able to produce 1alpha,25(OH)(2)D-3 and respond rapidly to treatment with 1alpha,25(OH)(2)D-3. Therefore, we would postulate that local production of 1alpha,25(OH)(2)D-3 maybe an important autocrine link between Vitamin D status and pancreatic function. (C) 2004 Elsevier Ltd. All rights reserved.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry R Medicine > RC Internal medicine
Journal or Publication Title:	Journal of Molecular Biology
Publisher:	PERGAMON-ELSEVIER SCIENCE LTD
ISSN:	0960-0760
Date:	May 2004
Volume:	89-90
Number:	1-5 Sp. Iss. SI
Number of Pages:	5
Page Range:	pp. 121-125
Identification Number:	10.1016/j.jsbmb.2004.03.115
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/8198

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item