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)