Linked Life Data

11123945

Source:http://linkedlifedata.com/resource/pubmed/id/11123945

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
2001-1-8
pubmed:abstractText
The copines are a novel group of Ca(2+)-dependent, phospholipid-binding proteins first isolated from Paramecium tetraurelia [Creutz, C. E., et al. (1998) J. Biol. Chem. 273, 1393-1402] and found in a wide range of organisms, from plants to humans. They have a Ca(2+) and phospholipid-binding domain consisting of two C2 domains and a core domain in the C-terminal portion that is homologous to the A domain found in certain integrins. We provide here the first description of the properties and distribution of a native mammalian copine, copine I. This protein is expressed in all major adult rat organs as demonstrated by probing Western blots of rat organ homogenates with anticopine antibodies. The highest levels of copine are found in the spleen. A protocol for purifying copine to homogeneity from bovine spleen is described. Purified native copine is a 58 kDa monomer that exhibits Ca(2+) self-association to form higher-order multimers, and Ca(2+)-dependent, phospholipid binding activity with preference for negatively charged phospholipids over neutral phospholipids and selectivity for Ca(2+) over Mg(2+). Half-maximal association with vesicles enriched in phosphatidylserine occurs at Ca(2+) concentrations between 1 and 10 microM. Copine I exhibits Mn(2+) binding activity that is strongly competed by Mg(2+) and partially competed by Ca(2+), suggesting that the copine I A domain may be a functional MIDAS metal binding site similar to that found in integrins [Lee, J. O., et al. (1995) Cell 80, 631-638]. Roles for copine in binding membranes and target proteins or small molecules are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16163-75
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11123945-Adenosine Triphosphate, pubmed-meshheading:11123945-Amino Acid Sequence, pubmed-meshheading:11123945-Animals, pubmed-meshheading:11123945-Brain, pubmed-meshheading:11123945-Calcium, pubmed-meshheading:11123945-Carrier Proteins, pubmed-meshheading:11123945-Cations, Divalent, pubmed-meshheading:11123945-Cattle, pubmed-meshheading:11123945-Female, pubmed-meshheading:11123945-Humans, pubmed-meshheading:11123945-Integrins, pubmed-meshheading:11123945-Liposomes, pubmed-meshheading:11123945-Liver, pubmed-meshheading:11123945-Male, pubmed-meshheading:11123945-Metals, pubmed-meshheading:11123945-Molecular Sequence Data, pubmed-meshheading:11123945-Organ Specificity, pubmed-meshheading:11123945-Phospholipids, pubmed-meshheading:11123945-Protein Binding, pubmed-meshheading:11123945-Rats, pubmed-meshheading:11123945-Rats, Wistar, pubmed-meshheading:11123945-Spleen
pubmed:year
2000
pubmed:articleTitle
Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein.
pubmed:affiliation
Department of Pharmacology, University of Virginia, Charlottesville, Virginia 22908, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't