Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart

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Abstract

  • 1.

    1. Matrix-immobilized calcyclin as affinity ligand in chromatography led to purification of three protein bands at 68, 36 and 35 kDa from bovine heart that required Ca2+ for binding.

  • 2.

    2. Polyacrylamide-immobilized phosphatidylserine separated this fraction into a phospholipid-binding part (68 kDa, 35 kDa), also attaching to phospholipid vesicles even in the presence of calcyclin, and a flow-through part, constituting approx 30% of the total fraction (36 kDa).

  • 3.

    3. Enzyme assays and electrophoretic mobility showed an at least close relationship of the 36 kDa band to glyceraldehyde-3-phosphate dehydrogenase. Interaction between enzyme and calcyclin in a solid-phase assay was inhibited by sialoglycoproteins and depended strongly on the integrity of carboxyl and hydrophobic groups of the enzyme. The interaction between the two proteins had a Kd value of 110 nM.

  • 4.

    4. Application of annexin-specific antibodies revealed an immunological relationship of the 35 and 68 kDa calcyclin-binding proteins to members of the annexin family, namely to annexin II (35 kDa) and annexin VI (68 kDa). The N-terminal amino acid sequence of a cleavage peptide of the 68 kDa protein was identical to a sequence stretch in human annexin VI, corroborating this evidence.

References (43)

  • H. Tokumitsu et al.

    Molecular cloning of rabbit CAP-50, a calcyclin-associated annexin protein

    Biochem. biophys. Res. Commun.

    (1992)
  • C.A. Towle et al.

    Identification of a novel mammalian annexin

    J. biol. Chem.

    (1992)
  • S.F. Velick

    Glyceraldehyde-3-phosphate dehydrogenase from muscle

    Meth. Enzym.

    (1955)
  • F.-Y. Zeng et al.

    Carbohydrate-binding specificity of calcyclin and its expression in human tissues and leukemic cells

    Archs Biochem. Biophys.

    (1991)
  • F.-Y. Zeng et al.

    Purification and properties of a fucoidan-binding protein from human placenta and its identification as immunoglobulin G

    Int. J. Biochem.

    (1992)
  • T. Becker et al.

    Protein protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p 11

    EMBO Jl

    (1990)
  • R.D. Burgoyne et al.

    Phospholipid-binding proteins in calcium-dependent exocytosis

    Biochem. Soc. Trans.

    (1992)
  • B. Calabretta et al.

    Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein

    J. biol. Chem.

    (1986)
  • C.E. Creutz

    The annexins and exocytosis

    Science

    (1992)
  • M.R. Crompton et al.

    Primary structure of the human, membrane-associated Ca2+-binding protein p68: a novel member of a protein family

    EMBO Jl

    (1988)
  • D. Engelkamp et al.

    S-lOOa, CAPL and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart

    Biochemistry

    (1992)
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