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Sequence similarity of calreticulin with a Ca2(+)-binding protein that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60 cells

Simmerman, H. K.
Jones, L. R.
Campbell, K. P.
Published in Biochemical Journal. 1990, vol. 270, no. 2, p. 545-548
Abstract HL-60 cells possess a 60 kDa Ca2(+)-binding protein that is contained in a discrete subcellular compartment, referred to as calciosomes. Subcellular fractionation studies have suggested that, in HL-60 cells, this intracellular compartment is an Ins(1,4,5)P3-sensitive Ca2+ store. In order to investigate the structural relationship of the 60 kDa Ca2(+)-binding protein of HL-60 cells to other Ca2(+)-binding proteins, we have purified the protein by ammonium sulphate extraction, acid precipitation, and DEAE-cellulose and phenyl-Sepharose column chromatography. The N-terminal sequence of the protein shows 93% identity with rabbit muscle calreticulin, a recently cloned sarcoplasmic reticulum Ca2(+)-binding protein. No amino acid sequence similarity with calsequestrin was found, although the purified protein cross-reacted with anti-calsequestrin antibodies. The calreticulin-related protein of HL-60 cells might play a role as an intravesicular Ca2(+)-binding protein of an Ins(1,4,5)P3-sensitive Ca2+ store.
Keywords Amino Acid SequenceAnimalsCalcium/ metabolismCalcium-Binding Proteins/ isolation & purificationCalreticulinCalsequestrinCell FractionationChromatographyHumansImmunoblottingInositol 1,4,5-Trisphosphate/ pharmacologyLeukemia, Promyelocytic, AcuteMolecular Sequence DataMolecular WeightMuscles/analysisMyocardium/analysisOrganelles/ analysisRabbitsSequence Homology, Nucleic AcidTumor Cells, Cultured
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PMID: 2400400
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