Advanced

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:
author
organization
publishing date
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
id
7604026d-4945-410b-9742-62176b4c8f08 (old id 1109906)
date added to LUP
2008-07-24 08:40:15
date last changed
2017-08-06 03:48:15
@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},
  volume       = {35},
  year         = {1996},
}