FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2083376185> ?p ?o ?g. }

• W2083376185 endingPage "1334" @default.
• W2083376185 startingPage "1325" @default.
• W2083376185 abstract "The aim was to examine systematically the potencies of protein kinase C inhibitors as a function of the kinase activator. Protein kinase C is activated by at least four stimulators: calcium plus phosphatidylserine (Ca/PS), phorbol 12-myristate 13-acetate plus PS (PS/PMA), arachidonic acid plus calcium (Ca/AA) and the synthetic peptide activator PCK530-558. With histone or GS1-12 as substrates, protein kinase C was maximally activated by Ca/PS, or to maxima of 62%, 89% or 82% with PS/PMA, Ca/AA or PKC530-558, respectively. One group of inhibitors, including H-7 and staurosporine, were equipotent, regardless of the activator. All other inhibitors showed variable selectivity, dependent upon the activator. A second group of inhibitors, including sphingosine and lipophosphoglycan, were eight or 200 times more potent for inhibition of PS/PMA-stimulated activity (relative to Ca/PS) and a third group, including retinal and palmitoylcarnitine, were 14 or 262 times more potent towards Ca/PS-stimulated activity. A final group (rhodamine 6G) was nine times more potent when Ca/AA was the activator. Similar results were obtained using the endogenous substrates dephosphin or MARCKS in synaptosol. Phosphorylation of MARCKS was stimulated by PS/PMA or Ca/PS, while phosphorylation of dephosphin was stimulated only by Ca/PS. The phosphorylation of either by Ca/PS-activated kinase was nine times more potently inhibited by palmitoylcarnitine, while phosphorylation of MARCKS by PS/PMA-activated kinase was 10 times more potently inhibited by sphingosine. H-7 inhibited both at similar concentrations. A model encompasses these differences in potency if the inhibitors are divided into four groups (A-D) according to their competitive inhibition with the appropriate activator or at the active site. The non-selective inhibitors interact at the active sites of protein kinase C (group A). The compounds which preferentially inhibit PS/PMA-activated kinase (sphingosine and lipophosphoglycan) are competitive inhibitors of PMA and 1,2-diacylglycerol (group B), those selective for Ca/PS-activated kinase (palmitoylcarnitine and retinal) are competitive with PS (group C) and those selective for Ca-AA activation (rhodamine 6G) are likely to be competitive with fatty acid (group D). Therefore, the effectiveness of protein kinase C inhibitors is dependent upon the activator employed." @default.
• W2083376185 created "2016-06-24" @default.
• W2083376185 creator A5005523254 @default.
• W2083376185 date "1992-10-01" @default.
• W2083376185 modified "2023-10-14" @default.
• W2083376185 title "Potencies of protein kinase C inhibitors are dependent on the activators used to stimulate the enzyme" @default.
• W2083376185 cites W1485079524 @default.
• W2083376185 cites W1502793076 @default.
• W2083376185 cites W1508657545 @default.
• W2083376185 cites W1508860572 @default.
• W2083376185 cites W1522849075 @default.
• W2083376185 cites W1534834744 @default.
• W2083376185 cites W1550017207 @default.
• W2083376185 cites W1556549089 @default.
• W2083376185 cites W1564012501 @default.
• W2083376185 cites W1565640556 @default.
• W2083376185 cites W1568354597 @default.
• W2083376185 cites W1576200545 @default.
• W2083376185 cites W1589866689 @default.
• W2083376185 cites W1590089681 @default.
• W2083376185 cites W1594649157 @default.
• W2083376185 cites W1594758412 @default.
• W2083376185 cites W1602085473 @default.
• W2083376185 cites W1602098131 @default.
• W2083376185 cites W1605148153 @default.
• W2083376185 cites W1661120989 @default.
• W2083376185 cites W1964839077 @default.
• W2083376185 cites W1967741846 @default.
• W2083376185 cites W1973454785 @default.
• W2083376185 cites W1973625300 @default.
• W2083376185 cites W1974190630 @default.
• W2083376185 cites W1977672499 @default.
• W2083376185 cites W1977758375 @default.
• W2083376185 cites W1980854090 @default.
• W2083376185 cites W1991781635 @default.
• W2083376185 cites W1993282564 @default.
• W2083376185 cites W1995499596 @default.
• W2083376185 cites W1995916018 @default.
• W2083376185 cites W1996585868 @default.
• W2083376185 cites W1997709415 @default.
• W2083376185 cites W2001392129 @default.
• W2083376185 cites W2003114605 @default.
• W2083376185 cites W2007096194 @default.
• W2083376185 cites W2009373735 @default.
• W2083376185 cites W2009856702 @default.
• W2083376185 cites W2019464191 @default.
• W2083376185 cites W2023366456 @default.
• W2083376185 cites W2023447656 @default.
• W2083376185 cites W2023978323 @default.
• W2083376185 cites W2024208090 @default.
• W2083376185 cites W2025010851 @default.
• W2083376185 cites W2026617113 @default.
• W2083376185 cites W2026930564 @default.
• W2083376185 cites W2032993257 @default.
• W2083376185 cites W2044469415 @default.
• W2083376185 cites W2050338578 @default.
• W2083376185 cites W2051531396 @default.
• W2083376185 cites W2052028692 @default.
• W2083376185 cites W2052519739 @default.
• W2083376185 cites W2054800842 @default.
• W2083376185 cites W2059793417 @default.
• W2083376185 cites W2060622769 @default.
• W2083376185 cites W2064274949 @default.
• W2083376185 cites W2068669272 @default.
• W2083376185 cites W2068957364 @default.
• W2083376185 cites W2073265875 @default.
• W2083376185 cites W2078250644 @default.
• W2083376185 cites W2080690667 @default.
• W2083376185 cites W2084524998 @default.
• W2083376185 cites W2085547973 @default.
• W2083376185 cites W2088152528 @default.
• W2083376185 cites W2091673674 @default.
• W2083376185 cites W2121049876 @default.
• W2083376185 cites W2126698050 @default.
• W2083376185 cites W2153046617 @default.
• W2083376185 cites W2154124833 @default.
• W2083376185 cites W2251920431 @default.
• W2083376185 cites W84058586 @default.
• W2083376185 doi "https://doi.org/10.1016/0006-2952(92)90533-o" @default.
• W2083376185 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1417956" @default.
• W2083376185 hasPublicationYear "1992" @default.
• W2083376185 type Work @default.
• W2083376185 sameAs 2083376185 @default.
• W2083376185 citedByCount "21" @default.
• W2083376185 crossrefType "journal-article" @default.
• W2083376185 hasAuthorship W2083376185A5005523254 @default.
• W2083376185 hasConcept C11960822 @default.
• W2083376185 hasConcept C153911025 @default.
• W2083376185 hasConcept C170493617 @default.
• W2083376185 hasConcept C181199279 @default.
• W2083376185 hasConcept C184235292 @default.
• W2083376185 hasConcept C185592680 @default.
• W2083376185 hasConcept C195794163 @default.
• W2083376185 hasConcept C2778078955 @default.
• W2083376185 hasConcept C2778703144 @default.
• W2083376185 hasConcept C2779084600 @default.
• W2083376185 hasConcept C2780043322 @default.
• W2083376185 hasConcept C2780780085 @default.

• next