Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase
Stenson, Lena LU ; Langin, Dominique ; Mulder, Hindrik LU
; Laurell, Henrik
; Grober, Jacques
; Bergh, Anders
; Mohrenweiser, Harvey W.
; Edgren, Gudrun
and Holm, Cecilia
(1996)
In Genomics
35(3).
p.441-447
- Abstract
- By catalyzing the rate-limiting step in adipose tissue lipolysis, hormone-sensitive lipase (HSL) is an important regulator of energy homeostasis. The role and importance of HSL in tissues other than adipose are poorly understood. We report here the cloning and expression of a testicular isoform, designated HSLtes. Due to an addition of amino acids at the NH2-termini, rat and human HSLtes consist of 1068 and 1076 amino acids, respectively, compared to the 768 and 775 amino acids, respectively, of the adipocyte isoform (HSLadi). A novel exon of 1.2 kb, encoding the human testis-specific amino acids, was isolated and mapped to the HSL gene, 16 kb upstream of the exons encoding HSLadi. The transcribed mRNA of 3.9 kb was specifically expressed... (More)
- By catalyzing the rate-limiting step in adipose tissue lipolysis, hormone-sensitive lipase (HSL) is an important regulator of energy homeostasis. The role and importance of HSL in tissues other than adipose are poorly understood. We report here the cloning and expression of a testicular isoform, designated HSLtes. Due to an addition of amino acids at the NH2-termini, rat and human HSLtes consist of 1068 and 1076 amino acids, respectively, compared to the 768 and 775 amino acids, respectively, of the adipocyte isoform (HSLadi). A novel exon of 1.2 kb, encoding the human testis-specific amino acids, was isolated and mapped to the HSL gene, 16 kb upstream of the exons encoding HSLadi. The transcribed mRNA of 3.9 kb was specifically expressed in testis. No significant similarity with other known proteins was found for the testis-specific sequence. The amino acid composition differs from the HSLadi sequence, with a notable hydrophilic character and a high content of prolines and glutamines. COS cells, transfected by the 3.9-kb human testis cDNA, expressed a protein of the expected molecular mass (M(r) approximately 120,000) that exhibited catalytic activity similar to that of HSLadi. Immunocytochemistry localized HSL to elongating spermatids and spermatozoa; HSL was not detected in interstitial cells. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1109906
- author
- Stenson, Lena
LU
; Langin, Dominique
; Mulder, Hindrik
LU
; Laurell, Henrik
; Grober, Jacques
; Bergh, Anders
; Mohrenweiser, Harvey W.
; Edgren, Gudrun
and Holm, Cecilia
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Genomics
- volume
- 35
- issue
- 3
- pages
- 441 - 447
- publisher
- Academic Press
- external identifiers
-
- pmid:8812477
- scopus:0000537214
- ISSN
- 1089-8646
- DOI
- 10.1006/geno.1996.0383
- 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: Insulin Signal Transduction (013212014), Molecular Medicine (013031200), Diabetes, Metabolism and Endocrinology (LUR000004)
- id
- 7604026d-4945-410b-9742-62176b4c8f08 (old id 1109906)
- date added to LUP
- 2016-04-01 12:26:42
- date last changed
- 2022-03-21 04:27:40
@article{7604026d-4945-410b-9742-62176b4c8f08,
abstract = {{By catalyzing the rate-limiting step in adipose tissue lipolysis, hormone-sensitive lipase (HSL) is an important regulator of energy homeostasis. The role and importance of HSL in tissues other than adipose are poorly understood. We report here the cloning and expression of a testicular isoform, designated HSLtes. Due to an addition of amino acids at the NH2-termini, rat and human HSLtes consist of 1068 and 1076 amino acids, respectively, compared to the 768 and 775 amino acids, respectively, of the adipocyte isoform (HSLadi). A novel exon of 1.2 kb, encoding the human testis-specific amino acids, was isolated and mapped to the HSL gene, 16 kb upstream of the exons encoding HSLadi. The transcribed mRNA of 3.9 kb was specifically expressed in testis. No significant similarity with other known proteins was found for the testis-specific sequence. The amino acid composition differs from the HSLadi sequence, with a notable hydrophilic character and a high content of prolines and glutamines. COS cells, transfected by the 3.9-kb human testis cDNA, expressed a protein of the expected molecular mass (M(r) approximately 120,000) that exhibited catalytic activity similar to that of HSLadi. Immunocytochemistry localized HSL to elongating spermatids and spermatozoa; HSL was not detected in interstitial cells.}},
author = {{Stenson, Lena and Langin, Dominique and Mulder, Hindrik and Laurell, Henrik and Grober, Jacques and Bergh, Anders and Mohrenweiser, Harvey W. and Edgren, Gudrun and Holm, Cecilia}},
issn = {{1089-8646}},
language = {{eng}},
number = {{3}},
pages = {{441--447}},
publisher = {{Academic Press}},
series = {{Genomics}},
title = {{Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase}},
url = {{http://dx.doi.org/10.1006/geno.1996.0383}},
doi = {{10.1006/geno.1996.0383}},
volume = {{35}},
year = {{1996}},
}