Hormone-sensitive lipase, the rate-limiting enzyme in triglyceride hydrolysis, is expressed and active in beta-cells
(1999) In Diabetes 48(1). p.228-232- Abstract
- Triglycerides in the beta-cell may be important for stimulus-secretion coupling, through provision of a lipid-derived signal, and for pathogenetic events in NIDDM, where lipids may adversely affect beta-cell function. In adipose tissues, hormone-sensitive lipase (HSL) is rate-limiting in triglyceride hydrolysis. Here, we investigated whether this enzyme is also expressed and active in beta-cells. Northern blot analysis and reverse transcription-polymerase chain reaction demonstrated that HSL is expressed in rat islets and in the clonal beta-cell lines INS-1, RINm5F, and HIT-T15. Western blot analysis identified HSL in mouse and rat islets and the clonal beta-cells. In mouse and rat, immunocytochemistry showed a predominant occurrence of... (More)
- Triglycerides in the beta-cell may be important for stimulus-secretion coupling, through provision of a lipid-derived signal, and for pathogenetic events in NIDDM, where lipids may adversely affect beta-cell function. In adipose tissues, hormone-sensitive lipase (HSL) is rate-limiting in triglyceride hydrolysis. Here, we investigated whether this enzyme is also expressed and active in beta-cells. Northern blot analysis and reverse transcription-polymerase chain reaction demonstrated that HSL is expressed in rat islets and in the clonal beta-cell lines INS-1, RINm5F, and HIT-T15. Western blot analysis identified HSL in mouse and rat islets and the clonal beta-cells. In mouse and rat, immunocytochemistry showed a predominant occurrence of HSL in beta-cells, with a presumed cytoplasmic localization. Lipase activity in homogenates of the rodent islets and clonal beta-cells constituted 2.1 +/- 0.6% of that in adipocytes; this activity was immunoinhibited by use of antibodies to HSL. The established HSL expression and activity in beta-cells offer a mechanism whereby lipids are mobilized from intracellular stores. Because HSL in adipocytes is activated by cAMP-dependent protein kinase (PKA), PKA-regulated triglyceride hydrolysis in beta-cells may participate in the regulation of insulin secretion, possibly by providing a lipid-derived signal, e.g., long-chain acyl-CoA and diacylglycerol. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1114550
- author
- Mulder, Hindrik LU ; Stensson Holst, Lena ; Svensson, Håkan ; Degerman, Eva LU ; Sundler, Frank LU ; Ahrén, Bo LU ; Rorsman, Patrik LU and Holm, Cecilia LU
- organization
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Diabetes
- volume
- 48
- issue
- 1
- pages
- 228 - 232
- publisher
- American Diabetes Association Inc.
- external identifiers
-
- pmid:9892250
- ISSN
- 1939-327X
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Molecular Metabolism (013212001), Neuroendocrine Cell Biology (013212008), Medicine (Lund) (013230025), Islet cell physiology (013212142), Molecular Endocrinology (013212018), Insulin Signal Transduction (013212014)
- id
- 8450dc14-f655-4fc1-b707-a1b07407a16d (old id 1114550)
- alternative location
- http://diabetes.diabetesjournals.org/cgi/reprint/48/1/228.pdf
- date added to LUP
- 2016-04-01 15:40:56
- date last changed
- 2023-04-18 19:53:15
@article{8450dc14-f655-4fc1-b707-a1b07407a16d, abstract = {{Triglycerides in the beta-cell may be important for stimulus-secretion coupling, through provision of a lipid-derived signal, and for pathogenetic events in NIDDM, where lipids may adversely affect beta-cell function. In adipose tissues, hormone-sensitive lipase (HSL) is rate-limiting in triglyceride hydrolysis. Here, we investigated whether this enzyme is also expressed and active in beta-cells. Northern blot analysis and reverse transcription-polymerase chain reaction demonstrated that HSL is expressed in rat islets and in the clonal beta-cell lines INS-1, RINm5F, and HIT-T15. Western blot analysis identified HSL in mouse and rat islets and the clonal beta-cells. In mouse and rat, immunocytochemistry showed a predominant occurrence of HSL in beta-cells, with a presumed cytoplasmic localization. Lipase activity in homogenates of the rodent islets and clonal beta-cells constituted 2.1 +/- 0.6% of that in adipocytes; this activity was immunoinhibited by use of antibodies to HSL. The established HSL expression and activity in beta-cells offer a mechanism whereby lipids are mobilized from intracellular stores. Because HSL in adipocytes is activated by cAMP-dependent protein kinase (PKA), PKA-regulated triglyceride hydrolysis in beta-cells may participate in the regulation of insulin secretion, possibly by providing a lipid-derived signal, e.g., long-chain acyl-CoA and diacylglycerol.}}, author = {{Mulder, Hindrik and Stensson Holst, Lena and Svensson, Håkan and Degerman, Eva and Sundler, Frank and Ahrén, Bo and Rorsman, Patrik and Holm, Cecilia}}, issn = {{1939-327X}}, language = {{eng}}, number = {{1}}, pages = {{228--232}}, publisher = {{American Diabetes Association Inc.}}, series = {{Diabetes}}, title = {{Hormone-sensitive lipase, the rate-limiting enzyme in triglyceride hydrolysis, is expressed and active in beta-cells}}, url = {{http://diabetes.diabetesjournals.org/cgi/reprint/48/1/228.pdf}}, volume = {{48}}, year = {{1999}}, }