View source for BIOSIS / 2004:279615

AN   
     2004:279615  BIOSIS
DN   
     PREV200400277461
TI   
     Hormone-sensitive lipase - New roles for an old enzyme. 
AU   
     Yeaman, Stephen J. [Reprint Author]
CS   
     Sch MedSch Cell & Mol Biosci, Univ Newcastle Upon Tyne, Newcastle Upon
     Tyne, Tyne & Wear, NE2 4HH, England
     s.j.yeaman@ncl.ac.uk
SO   
     Biochemical Journal, (April 1 2004) Vol. 379, No. Part 1, pp. 11-22.
     print. 
     ISSN: 0264-6021. 
DT   
     Article
     General Review; (Literature Review)
LA   
     English
ED   
     Entered STN: 9 Jun 2004
     Last Updated on STN: 9 Jun 2004
AB   
     Although described initially as an intracellular adipocyte-specific
     triacylglycerol lipase. it is now clear that HSL (hormone-sensitive
     lipase) is expressed in Multiple tissues and plays a number of roles in
     lipid metabolism. including that of a neutral cholesteryl ester hydrolase.
     The major isoform is a single polypeptide with a moleclar mass of approx.
     84 kDa and which comprises three major domains: a catalytic domain. a
     regulatory domain encoding several phosphorylation sites and an N-terminal
     domain involved in protein-protein and protein-lipid interactions.  The
     activity of HSL is regulated acutely by several mechanisms, including
     reversible phosphorylation by a number of different protein kinases,
     translocation to different sites within the cell and interaction with a
     number of proteins, some of which may serve to direct the inhibitory
     products of HSL away from the protein.  It is also apparent from work
     with HSL null mice that more than one enzyme species may be classified
     as a hormone-sensitive lipase.  The possible presence of HSL in
     macrophages remains controversial, and the role of the protein in
     pancreatic beta-cells has yet to be fully elucidated.  Altered expression
     of HSL in different cell types may be associated with a number of
     pathological states, including obesity, atherosclerosis and Type II
     diabetes.
CC   
     Cytology - General   02502
     Cytology - Animal   02506
     Biochemistry studies - Sterols and steroids   10067
     Enzymes - General and comparative studies: coenzymes   10802
     Metabolism - General metabolism and metabolic pathways   13002
     Blood - Blood and lymph studies   15002
     Blood - Blood cell studies   15004
     Endocrine - General   17002
     Immunology - General and methods   34502
IT   
     Major Concepts
        Cell Biology; Endocrine System (Chemical Coordination and Homeostasis);
        Enzymology (Biochemistry and Molecular Biophysics); Metabolism
IT   
     Parts, Structures, & Systems of Organisms
        beta-cell: endocrine system; macrophage: blood and lymphatics, immune
        system
IT   
     Chemicals & Biochemicals
        cholesterol: metabolism; hormone-sensitive lipase; perilipin;
        protein kinase [EC 2.7.1.37]
IT   
     Miscellaneous Descriptors
        lipolysis; phosphorylation; protein-lipid interactions; protein-protein
        interactions
ORGN 
     Classifier
        Muridae   86375
     Super Taxa
        Rodentia; Mammalia; Vertebrata; Chordata; Animalia
     Organism Name
        mouse (common)
     Taxa Notes
        Animals, Chordates, Mammals, Nonhuman Vertebrates, Nonhuman Mammals,
        Rodents, Vertebrates
RN   
     57-88-5 (cholesterol)
     9001-62-1 (hormone-sensitive lipase)
     9026-43-1Q (protein kinase)
     80449-02-1Q (protein kinase)
     134549-83-0Q (protein kinase)
     372092-80-3Q (protein kinase)
     9026-43-1 (protein kinase)
     9026-43-1Q (EC 2.7.1.37)
     80449-02-1Q (EC 2.7.1.37)
     134549-83-0Q (EC 2.7.1.37)
     372092-80-3Q (EC 2.7.1.37)
     9026-43-1 (EC 2.7.1.37)