Linked Life Data

8006039

Source:http://linkedlifedata.com/resource/pubmed/id/8006039

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1994-7-20
pubmed:databankReference
pubmed:abstractText
Agonist stimulation of cells results in phosphatidylinositol turnover and the generation of inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), which mobilizes intracellular calcium. The inositol-polyphosphate 5-phosphatase (5-phosphatase) enzymes hydrolyze Ins(1,4,5)P3 in a signal-terminating reaction. We have isolated a 2.7-kilobase (kb) composite cDNA, encoding the 43-kDa membrane-associated 5-phosphatase, by screening a human placental lambda gt11 library, using degenerate oligonucleotides. The 2.7-kb cDNA contains a 1.1-kb open reading frame, comprising 363 amino acids, which encodes a protein of a predicted molecular mass of 42 kDa. Amino acid sequence analysis demonstrates a number of potential sites for phosphorylation by protein kinase C and a CAAX motif in the COOH terminus, which may mediate membrane localization. The recombinant enzyme was expressed in COS-7 cells, resulting in a 50-fold increase in enzyme activity in the detergent-soluble membrane fraction of the cell (nanomole of Ins(1,4,5)P3 hydrolyzed per min/mg), but only a 2.5-fold increase in 5-phosphatase activity in the total cell homogenate. Sequence analysis demonstrated a 73-amino acid domain in the COOH terminus of the 43-kDa membrane-associated 5-phosphatase, which had 30% sequence identity and 67% similarity to a region in the 75-kDa 5-phosphatase and 34% identity and 70% similarity to a sequence in the protein that is encoded by the gene, defective in Lowe's oculocerebrorenal syndrome. As shown by RNA analysis the 43-kDa membrane-associated 5-phosphatase appears to be predominantly expressed in heart, brain, and skeletal muscle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17305-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8006039-Amino Acid Sequence, pubmed-meshheading:8006039-Base Sequence, pubmed-meshheading:8006039-Cell Membrane, pubmed-meshheading:8006039-Cloning, Molecular, pubmed-meshheading:8006039-DNA, Complementary, pubmed-meshheading:8006039-Gene Expression, pubmed-meshheading:8006039-Genes, pubmed-meshheading:8006039-Humans, pubmed-meshheading:8006039-Membrane Proteins, pubmed-meshheading:8006039-Molecular Sequence Data, pubmed-meshheading:8006039-Phosphoric Monoester Hydrolases, pubmed-meshheading:8006039-Proteins, pubmed-meshheading:8006039-RNA, Messenger, pubmed-meshheading:8006039-Recombinant Proteins, pubmed-meshheading:8006039-Restriction Mapping, pubmed-meshheading:8006039-Sequence Alignment, pubmed-meshheading:8006039-Sequence Homology, Amino Acid, pubmed-meshheading:8006039-Tissue Distribution
pubmed:year
1994
pubmed:articleTitle
Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase.
pubmed:affiliation
Department of Medicine, Box Hill Hospital, Monash Medical School, Victoria, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't