Fat Mobilization in Adipose Tissue Is Promoted by Adipose Triglyceride Lipase

Zimmermann, R.; Strauß, Juliane Gertrude; Haemmerle, Guenter; Schoiswohl, Gabriele; Birner‐Gruenberger, Ruth; Riederer, Monika; Lass, Achim; Neuberger, Georg; Eisenhaber, Frank; Hermetter, Albin; Zechner, Rudolf

doi:10.1126/science.1100747

Cited by 1,766 publications

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“…The recently discovered ATGL (iPLA 2 ζ, desnutrin) is abundantly expressed in adipose tissue of both mice and humans [9]. We have recently demonstrated that subcutaneous adipose tissue ATGL expression levels are strongly correlated to the levels of HSL [11].…”

Section: Discussionmentioning

confidence: 95%

“…HSL and ATGL glyceride hydrolase activities HSL and ATGL both possess triglyceride hydrolase activity [9,10,17]. We wished to determine the relative contribution of the two enzymes to the in vitro hydrolysis of triolein.…”

Section: Hsl and Atgl Gene Expression In Obesitymentioning

confidence: 99%

“…However, HSL knock-out mice have residual lipolytic activity [4,5], which may be attributed to an additional lipase with high affinity for triglycerides [6,7]. Accordingly, a novel adipocyte-specific lipase termed adipose triglyceride lipase (ATGL, now known as patatin-like phospholipase domain containing 2 [PNPLA2]), the product of Pnpla2, and alternatively designated iPLA 2 ζ or desnutrin, was recently identified using different strategies [8][9][10]. The murine ATGL-protein consists of 486 amino acids, whereas the corresponding human form is a 506-amino acid protein.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, it has been suggested that ATGL acts as an additional ratelimiting lipase, at least for lipolysis in mouse fat cells [9]. However, the functional importance of this novel lipase in human adipocytes remains to be established.…”

Section: Introductionmentioning

confidence: 99%

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Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity

et al. 2006

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Aims/hypothesis: The recent identification of murine adipose triglyceride lipase (ATGL, now known as patatin-like phospholipase domain containing 2 [PNPLA2]), gene product of Pnpla2, has questioned the unique role of hormone sensitive lipase (HSL, now known as LIPE), gene product of Lipe, in fat cell lipolysis. Here, we investigated human ATGL and HSL adipose tissue gene expression and in vitro lipase activity. Subjects, materials and methods: Levels of mRNA in adipose tissue from healthy obese and non-obese subjects were measured and lipase activity and adipocyte lipolytic capacity determined. HSL and ATGL cDNAs were transfected into Cos-7 cells and the relative tri-and diglyceride hydrolase activities were measured. Results: Obesity was associated with a decreased subcutaneous and increased omental adipose tissue level of HSL mRNA. Subcutaneous HSL mRNA content was normalised upon weight reduction. In contrast, ATGL mRNA levels were unaffected by obesity and weight reduction. A high adipose tissue lipase activity was associated with increased maximal lipolysis and increased HSL, but not with ATGL mRNA levels. The in vitro triglyceride hydrolase activity of HSL was markedly higher than that of ATGL and contrary to HSL, ATGL was devoid of diglyceride hydrolase activity. The use of a selective HSL-inhibitor resulted in complete inhibition of HSL-mediated tri-and diglyceride hydrolase activity. The pH profile of human white adipose tissue triolein hydrolase activity was identical to that of HSL but differed from the ATGL profile. Conclusions/interpretation: HSL, but not ATGL gene expression shows a regulation according to obesity status and is associated with increased adipose tissue lipase activity. Moreover, HSL has a higher capacity than ATGL to hydrolyse triglycerides in vitro.

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Section: Discussionmentioning

confidence: 95%

Section: Hsl and Atgl Gene Expression In Obesitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity

et al. 2006

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“…3,6 PNPLA2 is the rate-limiting lipolytic enzyme and catalyzes the initial step in triglyceride hydrolysis. 1,7,8 Most individuals with PNPLA2 mutations show atypical CDS-like symptoms, with myopathy and involvement of other organs but without ichthyosis. 1,3,6,9 Until now, 19 patients with PNPLA2 mutations have been reported.…”

mentioning

confidence: 99%

Novel PNPLA2 gene mutations in Chinese Han patients causing neutral lipid storage disease with myopathy

Lin

Wen

et al. 2012

J Hum Genet

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Neutral lipid storage disease with myopathy (NLSDM) referred to those neutral lipid storage disease (NLSD) patients with myopathy but without ichthyosis. Recently, NLSDM has been attributed to mutations in the PNPLA2 gene. Until now, 19 patients with PNPLA2 mutations have been reported. In the present study, we describe the clinical and genetic findings in three Chinese patients with NLSDM. Sequence analysis of PNPLA2 gene was performed. In our patients we identified four novel mutations in the PNPLA2 gene including two splicing mutations. The identification and study of mutations found in PNPLA2 is also particularly important to define the clinical spectrum and genotype-phenotype correlations of the PNPLA2 gene.

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A Novel Mutation in PNPLA2 Leading to Neutral Lipid Storage Disease With Myopathy

Ash¹

2012

Arch Neurol

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Fat Mobilization in Adipose Tissue Is Promoted by Adipose Triglyceride Lipase

Cited by 1,766 publications

References 21 publications

Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity

Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity

Novel PNPLA2 gene mutations in Chinese Han patients causing neutral lipid storage disease with myopathy

A Novel Mutation in PNPLA2 Leading to Neutral Lipid Storage Disease With Myopathy

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