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Summarizes advances with regard to hormone-sensitive lipase (HSL) structure and molecular mechanisms involved in regulating its activity and lipolysis. Identification of HSL in adipose tissue; Expression and role of HSL in tissues other than adipose tissue; Molecular mechanisms in regulated lipolysis.

Describes the characterization of a novel polymorphism in the hormone-sensitive lipase (HSL) gene. Hydrolysis of adipose tissue triglycerides into free fatty acids; Two-point linkage analysis performed between HSL and markers from Genethon.

Hormone-sensitive lipase (HSL) is an esterase and lipase, which are essential for spermatogenesis. Two HSL mRNAs are expressed in human testis. A long form is encoded by a testis-specific exon and nine exons common to testis and adipocyte HSL. Here we show that the short-form 3.3-kb mRNA possesses a unique 5′ end that is transcribed from a novel testis-specific exon. The corresponding protein is similar to the 775-amino-acid-long adipocyte HSL. Immunohistochemistry experiments on human testis sections revealed that the long form is strictly expressed in haploid germ cells whereas the short form is expressed in interstitial and tubular somatic cells as well as premeiotic germ cells. [Copyright &y& Elsevier]