Linked Life Data

8026506

Source:http://linkedlifedata.com/resource/pubmed/id/8026506

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-8-11
pubmed:abstractText
In soluble and particulate extracts from muscle D-myo-inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and D-myo-inositol 1,3,4,5-tetrakisphosphate [Ins(1,3,4,5)P4] are metabolised stepwise to inositol. Ins(1,4,5)P3 is rapidly dephosphorylated to D-myo-inositol 1,4-bisphosphate then to D-myo-inositol 4-phosphate and finally inositol. In soluble extracts Ins(1,3,4,5)P4 is dephosphorylated to D-myo-inositol 1,3,4-trisphosphate then sequentially to D-myo-inositol 3,4-bisphosphate, D-myo-inositol 3-phosphate and inositol, while in particulate extracts D-myo-inositol 1,3-bisphosphate is the predominant inositol bisphosphate formed. Dephosphorylation of these inositol polyphosphates is Mg2+ dependent and inhibited by D-2,3-bisphosphoglyceric acid. Ins(1,4,5)P3 is also phosphorylated to form Ins(1,3,4,5)P4 in soluble extracts by Ins(1,4,5)P3 3-kinase. Ins(1,4,5)P3 3-kinase activity is Mg2+ and ATP dependent and is stimulated by Ca2+ and calmodulin. Particulate (sarcotubular) inositol polyphosphate 5-phosphatase (5-phosphatase) is found in membranes which are intimately involved in excitation-contraction coupling and the generation of the primary Ca2+ signal of muscle cells. Particulate 5-phosphatase had the highest specific activity in the transverse-tubule membrane, when compared to the terminal cisternae and longitudinal-tubule membranes of the sarcoplasmic reticulum. Particulate Ins(1,3,4,5)P4-3-phosphatase activity was also detected after fractionation of solubilised sarcotubular membranes by DEAE-Sephacel. Particulate 5-phosphatase activity was purified 25,600-fold to a specific activity of 25.6 mumol Ins(1,4,5)P3 hydrolysed.min-1.mg protein-1, after DEAE-Sephacel and novel affinity chromatography using D-2,3-bisphosphoglycerate/agarose and Sepharose-4B-immobilised Ins(1,4,5)P3-analog matrices. Purified particulate 5-phosphatase had apparent Km of 46.3 microM and 1.9 microM and Vmax of 115 and 0.046 mumol substrate hydrolysed.min-1.mg protein-1, for Ins(1,4,5)P3 and Ins(1,3,4,5)P4, respectively. In contrast, purified soluble type I 5-phosphatase had apparent Km of 8.9 microM and 1.1 microM and Vmax of 3.55 and 0.13 mumol substrate hydrolysed.min-1.mg protein-1, for Ins(1,4,5P3 and Ins(1,3,4,5)P4, respectively. As in other cells, muscle 5-phosphatases have a lower affinity, but a higher capacity to metabolise Ins(1,4,5)P3 than Ins(1,3,4,5)P4. Soluble type I 5-phosphatase may have a functional role in the metabolism of both inositol polyphosphates, while particulate 5-phosphatase may primarily metabolise Ins(1,4,5)P3. Purified Ins(1,4,5)P3 3-kinase had an apparent Km of 0.42 microM and a Vmax of 4.12 nmol Ins(1,4,5)P3 phosphorylated.min-1.mg protein-1. The profile of inositol polyphosphate metabolism in muscle is similar to that reported in other tissues.(ABSTRACT TRUNCATED AT 400 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
222
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
955-64
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The metabolism of D-myo-inositol 1,4,5-trisphosphate and D-myo-inositol 1,3,4,5-tetrakisphosphate by porcine skeletal muscle.
pubmed:affiliation
Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't