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

K. H. Krause, H. K.B. Simmerman, L. R. Jones, K. P. Campbell

Research output: Contribution to journalArticle

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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.

Original languageEnglish (US)
Pages (from-to)545-548
Number of pages4
JournalBiochemical Journal
Volume270
Issue number2
DOIs
StatePublished - Jan 1 1990

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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