FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2000584059> ?p ?o ?g. }

• W2000584059 endingPage "2290" @default.
• W2000584059 startingPage "2285" @default.
• W2000584059 abstract "Inositol 3,4,5,6-tetrakisphosphate is a novel intracellular signal that regulates calcium-dependent chloride conductance (Xie, W., Kaetzel, M. A., Bruzik, K. S., Dedman, J. R., Shears, S. B., and Nelson, D. J. (1996) J. Biol. Chem. 271, 14092-14097). The molecular mechanisms that regulate the cellular levels of this signal are not characterized. To pursue this problem we have now studied the 1-kinase that deactivates inositol 3,4,5,6-tetrakisphosphate. The enzyme was purified from rat liver 1600-fold with a 1% yield. The native molecular mass was determined to be 46 kDa by gel filtration. The Km values for inositol 3,4,5,6-tetrakisphosphate and ATP were 0.3 and 10.6 μM, respectively. The kinase was unaffected by either protein kinase A or protein kinase C. Increases in Ca2+ concentration from 0.1 to 1-2 μM inhibited activity by 10-20%. Most importantly, inositol 1,3,4-trisphosphate was shown to be a potent (Ki = 0.2 μM), specific, and competitive inhibitor of the 1-kinase. Our new kinetic data show that typical receptor-dependent adjustments in cellular levels of inositol 1,3,4-trisphosphate provide a mechanism by which the concentration of inositol 3,4,5,6-tetrakisphosphate is dependent on changes in phospholipase C activity. These conclusions also provide a new perspective to our understanding of the physiological importance of the pathway of inositol phosphate turnover initiated by the inositol 1,4,5-trisphosphate 3-kinase. Inositol 3,4,5,6-tetrakisphosphate is a novel intracellular signal that regulates calcium-dependent chloride conductance (Xie, W., Kaetzel, M. A., Bruzik, K. S., Dedman, J. R., Shears, S. B., and Nelson, D. J. (1996) J. Biol. Chem. 271, 14092-14097). The molecular mechanisms that regulate the cellular levels of this signal are not characterized. To pursue this problem we have now studied the 1-kinase that deactivates inositol 3,4,5,6-tetrakisphosphate. The enzyme was purified from rat liver 1600-fold with a 1% yield. The native molecular mass was determined to be 46 kDa by gel filtration. The Km values for inositol 3,4,5,6-tetrakisphosphate and ATP were 0.3 and 10.6 μM, respectively. The kinase was unaffected by either protein kinase A or protein kinase C. Increases in Ca2+ concentration from 0.1 to 1-2 μM inhibited activity by 10-20%. Most importantly, inositol 1,3,4-trisphosphate was shown to be a potent (Ki = 0.2 μM), specific, and competitive inhibitor of the 1-kinase. Our new kinetic data show that typical receptor-dependent adjustments in cellular levels of inositol 1,3,4-trisphosphate provide a mechanism by which the concentration of inositol 3,4,5,6-tetrakisphosphate is dependent on changes in phospholipase C activity. These conclusions also provide a new perspective to our understanding of the physiological importance of the pathway of inositol phosphate turnover initiated by the inositol 1,4,5-trisphosphate 3-kinase." @default.
• W2000584059 created "2016-06-24" @default.
• W2000584059 creator A5001378726 @default.
• W2000584059 creator A5033630229 @default.
• W2000584059 creator A5075243784 @default.
• W2000584059 date "1997-01-01" @default.
• W2000584059 modified "2023-10-15" @default.
• W2000584059 title "Properties of the Inositol 3,4,5,6-Tetrakisphosphate 1-Kinase Purified from Rat Liver" @default.
• W2000584059 cites W132866068 @default.
• W2000584059 cites W1484360204 @default.
• W2000584059 cites W1546431662 @default.
• W2000584059 cites W1558610458 @default.
• W2000584059 cites W1789455264 @default.
• W2000584059 cites W181110245 @default.
• W2000584059 cites W1954233493 @default.
• W2000584059 cites W1980166477 @default.
• W2000584059 cites W1997908015 @default.
• W2000584059 cites W2009480110 @default.
• W2000584059 cites W2010455912 @default.
• W2000584059 cites W2012729430 @default.
• W2000584059 cites W2018225424 @default.
• W2000584059 cites W2032072813 @default.
• W2000584059 cites W2045390680 @default.
• W2000584059 cites W2060852213 @default.
• W2000584059 cites W2086348707 @default.
• W2000584059 cites W2134786188 @default.
• W2000584059 cites W2177771047 @default.
• W2000584059 cites W2305508472 @default.
• W2000584059 cites W2429164993 @default.
• W2000584059 doi "https://doi.org/10.1074/jbc.272.4.2285" @default.
• W2000584059 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8999935" @default.
• W2000584059 hasPublicationYear "1997" @default.
• W2000584059 type Work @default.
• W2000584059 sameAs 2000584059 @default.
• W2000584059 citedByCount "26" @default.
• W2000584059 countsByYear W20005840592013 @default.
• W2000584059 countsByYear W20005840592019 @default.
• W2000584059 countsByYear W20005840592023 @default.
• W2000584059 crossrefType "journal-article" @default.
• W2000584059 hasAuthorship W2000584059A5001378726 @default.
• W2000584059 hasAuthorship W2000584059A5033630229 @default.
• W2000584059 hasAuthorship W2000584059A5075243784 @default.
• W2000584059 hasBestOaLocation W20005840591 @default.
• W2000584059 hasConcept C163235415 @default.
• W2000584059 hasConcept C170493617 @default.
• W2000584059 hasConcept C181199279 @default.
• W2000584059 hasConcept C184235292 @default.
• W2000584059 hasConcept C185592680 @default.
• W2000584059 hasConcept C2777427919 @default.
• W2000584059 hasConcept C2778597717 @default.
• W2000584059 hasConcept C2778618036 @default.
• W2000584059 hasConcept C55493867 @default.
• W2000584059 hasConcept C79879829 @default.
• W2000584059 hasConcept C86803240 @default.
• W2000584059 hasConceptScore W2000584059C163235415 @default.
• W2000584059 hasConceptScore W2000584059C170493617 @default.
• W2000584059 hasConceptScore W2000584059C181199279 @default.
• W2000584059 hasConceptScore W2000584059C184235292 @default.
• W2000584059 hasConceptScore W2000584059C185592680 @default.
• W2000584059 hasConceptScore W2000584059C2777427919 @default.
• W2000584059 hasConceptScore W2000584059C2778597717 @default.
• W2000584059 hasConceptScore W2000584059C2778618036 @default.
• W2000584059 hasConceptScore W2000584059C55493867 @default.
• W2000584059 hasConceptScore W2000584059C79879829 @default.
• W2000584059 hasConceptScore W2000584059C86803240 @default.
• W2000584059 hasIssue "4" @default.
• W2000584059 hasLocation W20005840591 @default.
• W2000584059 hasOpenAccess W2000584059 @default.
• W2000584059 hasPrimaryLocation W20005840591 @default.
• W2000584059 hasRelatedWork W1543925548 @default.
• W2000584059 hasRelatedWork W165533631 @default.
• W2000584059 hasRelatedWork W1851047213 @default.
• W2000584059 hasRelatedWork W1970652449 @default.
• W2000584059 hasRelatedWork W1997093700 @default.
• W2000584059 hasRelatedWork W2014367760 @default.
• W2000584059 hasRelatedWork W2023767739 @default.
• W2000584059 hasRelatedWork W2045378168 @default.
• W2000584059 hasRelatedWork W2071737785 @default.
• W2000584059 hasRelatedWork W2091079287 @default.
• W2000584059 hasVolume "272" @default.
• W2000584059 isParatext "false" @default.
• W2000584059 isRetracted "false" @default.
• W2000584059 magId "2000584059" @default.
• W2000584059 workType "article" @default.