Hormone-sensitive lipase ( @entity1384 )-L is a key enzyme in the mobilization of @entity1718 from @entity412 stores in adipocytes. A shorter variant of @entity1384 ( @entity1384 ) was detected in @entity1 . This one is generated through in-frame skipping of exon 6 during the processing of @entity1384 mRNA and results in a protein devoid of lipase activity. The role of @entity1384 is unknown. The aims of this study were to identify both @entity1384 variants in adipose tissue biopsies and to determine if the presence of @entity1384 is correlated to the lipolytic capacity of adipocytes. The study was performed in @entity1 abdominal subcutaneous adipocytes from two groups of seven @entity28 subjects. In the group of subjects with both @entity1384 proteins (L+S) group, two immunoreactive bands (80 and 88 kDa) were detected, whereas only the 88-kDa protein was detected in the group with only the wild-type @entity1384 -protein (L group). In the L+S group, the @entity1384 activity was 20% lower (P < 0.05) and the (S/S(+)) @entity1384 mRNA ratio was twofold higher than in the L group (P < 0.05). The maximally lipolytic capacities measured from isolated adipocytes incubated with @entity1063 or other lipolytic agents were 40% lower in the L+S group (P < 0.05). These results suggest that the presence of the truncated @entity1384 protein is associated with an impaired adipocyte lipolysis.

The presence of a catalytically inactive form of hormone-sensitive lipase is associated with decreased lipolysis in abdominal subcutaneous adipose tissue of XXXX subjects.

@entity1 :: ('9606', 'Species') :: ['humans', 'human'] @entity28 :: ('MESH:D009765', 'Disease') :: ['obese'] @entity412 :: ('CHEBI:17855', 'Chemical') :: ['triglyceride'] @entity1063 :: ('MESH:D009638', 'Chemical') :: ['norepinephrine'] @entity1384 :: ('3991', 'Gene') :: ['HSL', 'HSL-S'] @entity1718 :: ('MESH:D005227', 'Chemical') :: ['fatty acids']
@entity28 :: (MESH:D009765,Disease) :: ['obese']
