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Calcium-independent phospholipase A(2): structure and function.

M V Winstead1, J Balsinde, E A Dennis

  • 1Department of Chemistry and Biochemistry, 0601, Revelle College and School of Medicine, University of California at San Diego, 92093-0601, USA.

Biochimica Et Biophysica Acta
|November 18, 2000
PubMed
Summary

Group VIA phospholipase A(2) (PLA(2)) is a calcium-independent enzyme involved in phospholipid remodeling. Further research is needed to fully understand the roles of newly identified Ca(2+)-independent PLA(2) enzymes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The classical calcium (Ca(2+))-independent phospholipase A(2) (PLA(2)) enzyme, now known as Group VIA PLA(2), was first purified from the P388D(1) macrophage-like cell line.
  • Multiple splice variants of Group VIA PLA(2) are expressed, with some potentially regulating the active enzyme's function.

Purpose of the Study:

  • To characterize the Group VIA PLA(2) enzyme, including its structure, function, and substrate specificity.
  • To explore the enzyme's role in phospholipid remodeling and other cellular processes.
  • To differentiate Group VIA PLA(2) from newly identified Ca(2+)-independent PLA(2) enzymes.

Main Methods:

  • Purification and characterization of Group VIA PLA(2) from P388D(1) cells.
  • Cloning of the corresponding cDNA and identification of splice variants.

Related Experiment Videos

  • Enzyme activity assays to determine substrate hydrolysis and lysophospholipase activity.

    • Main Results:

    • Group VIA PLA(2) possesses a consensus lipase motif (GTSTG) with a catalytic serine and has a molecular weight of 85-88 kDa.
    • The enzyme exists in an aggregated form and contains ankyrin repeats potentially involved in oligomerization.
    • Group VIA PLA(2) exhibits both phospholipase A(2) and lysophospholipase activities, mediating phospholipid remodeling.

    Conclusions:

    • Group VIA PLA(2) is a key enzyme in phospholipid remodeling with diverse substrate capabilities.
    • The existence of multiple splice variants suggests complex regulatory mechanisms.
    • Further investigation is required to elucidate the physiological functions of newly discovered Ca(2+)-independent PLA(2) enzymes and their distinctions from Group VIA PLA(2).