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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
Journal article   Open access   Peer reviewed

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 Simmerman, L R Jones and K P Campbell
The Biochemical journal, Vol.270(2), pp.545-548
09/01/1990
DOI: 10.1042/bj2700545
PMCID: PMC1131758
PMID: 2400400
url
https://europepmc.org/articles/pmc1131758View
Published (Version of record) Open Access

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.
Chromatography Calsequestrin Amino Acid Sequence Rabbits Cell Fractionation Molecular Weight Calcium - metabolism Humans Molecular Sequence Data Immunoblotting Inositol 1,4,5-Trisphosphate - pharmacology Organelles - analysis Myocardium - analysis Sequence Homology, Nucleic Acid Calreticulin Animals Leukemia, Promyelocytic, Acute Calcium-Binding Proteins - isolation & purification Tumor Cells, Cultured Muscles - analysis

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