FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2013613294> ?p ?o ?g. }

• W2013613294 endingPage "9042" @default.
• W2013613294 startingPage "9037" @default.
• W2013613294 abstract "Cholecystokinin (CCK)-A and CCK-B receptors are highly homologous members of the seven transmembrane domain G-protein-coupled receptor superfamily. Genes of both receptors contain five exons and share a similar exon-intron organization. To determine the structural basis of CCK-A receptor (CCK-AR) functionally coupled to Gs, a series of chimeric mutants were constructed by replacing exons of human CCK-B receptor (CCK-BR), from the second to the fifth (last) exon, with human CCK-AR counterparts. Binding and signal transduction properties of wild-type and chimeric receptors were examined in stably transfected HEK-293 cells. Chimeric receptors that maintained high affinity binding to CCK exhibited dose-dependent increases in intracellular calcium mobilization similar to both wild-type receptors. However, only the wild-type CCK-AR and chimeric mutants containing the second exon of CCK-AR were able to mediate significantly greater increases in intracellular cAMP content and adenylyl cyclase activity compared with wild-type CCK-BR. A CCK-BR mutant was further constructed by replacing five amino acids, Gly-Leu-Ser-Arg-(Arg)-Leu, in the first intracellular loop with the corresponding five CCK-AR specific amino acids, Ile-Arg-Asn-Lys-(Arg)-Met. The resultant receptor maintained high affinity binding to both CCK and gastrin and dose-dependent calcium responses similar to wild-type CCK-BR. However, this first intracellular loop mutant also gained positive cAMP responses to both sulfated CCK-8 and gastrin-17 with EC50 values of 8.5 ± 1 nM and 23 ± 7 nM, respectively. These data suggest that the first intracellular loop of CCK-AR is essential for coupling to Gs and activation of adenylyl cyclase signal transduction cascade. Cholecystokinin (CCK)-A and CCK-B receptors are highly homologous members of the seven transmembrane domain G-protein-coupled receptor superfamily. Genes of both receptors contain five exons and share a similar exon-intron organization. To determine the structural basis of CCK-A receptor (CCK-AR) functionally coupled to Gs, a series of chimeric mutants were constructed by replacing exons of human CCK-B receptor (CCK-BR), from the second to the fifth (last) exon, with human CCK-AR counterparts. Binding and signal transduction properties of wild-type and chimeric receptors were examined in stably transfected HEK-293 cells. Chimeric receptors that maintained high affinity binding to CCK exhibited dose-dependent increases in intracellular calcium mobilization similar to both wild-type receptors. However, only the wild-type CCK-AR and chimeric mutants containing the second exon of CCK-AR were able to mediate significantly greater increases in intracellular cAMP content and adenylyl cyclase activity compared with wild-type CCK-BR. A CCK-BR mutant was further constructed by replacing five amino acids, Gly-Leu-Ser-Arg-(Arg)-Leu, in the first intracellular loop with the corresponding five CCK-AR specific amino acids, Ile-Arg-Asn-Lys-(Arg)-Met. The resultant receptor maintained high affinity binding to both CCK and gastrin and dose-dependent calcium responses similar to wild-type CCK-BR. However, this first intracellular loop mutant also gained positive cAMP responses to both sulfated CCK-8 and gastrin-17 with EC50 values of 8.5 ± 1 nM and 23 ± 7 nM, respectively. These data suggest that the first intracellular loop of CCK-AR is essential for coupling to Gs and activation of adenylyl cyclase signal transduction cascade." @default.
• W2013613294 created "2016-06-24" @default.
• W2013613294 creator A5012227349 @default.
• W2013613294 creator A5026131228 @default.
• W2013613294 creator A5037645081 @default.
• W2013613294 creator A5052788564 @default.
• W2013613294 creator A5056461765 @default.
• W2013613294 creator A5059296721 @default.
• W2013613294 creator A5076886453 @default.
• W2013613294 creator A5081937972 @default.
• W2013613294 creator A5091680206 @default.
• W2013613294 date "1997-04-01" @default.
• W2013613294 modified "2023-10-15" @default.
• W2013613294 title "First Intracellular Loop of the Human Cholecystokinin-A Receptor Is Essential for Cyclic AMP Signaling in Transfected HEK-293 Cells" @default.
• W2013613294 cites W1496104502 @default.
• W2013613294 cites W1526437569 @default.
• W2013613294 cites W1585471043 @default.
• W2013613294 cites W1589012184 @default.
• W2013613294 cites W1966380554 @default.
• W2013613294 cites W1966563991 @default.
• W2013613294 cites W1975316279 @default.
• W2013613294 cites W1979100850 @default.
• W2013613294 cites W1980106250 @default.
• W2013613294 cites W1982527304 @default.
• W2013613294 cites W1984415406 @default.
• W2013613294 cites W1990109135 @default.
• W2013613294 cites W1998591058 @default.
• W2013613294 cites W2003577584 @default.
• W2013613294 cites W2015179997 @default.
• W2013613294 cites W2017832365 @default.
• W2013613294 cites W2020154116 @default.
• W2013613294 cites W2024476894 @default.
• W2013613294 cites W2026777257 @default.
• W2013613294 cites W2035807640 @default.
• W2013613294 cites W2049224383 @default.
• W2013613294 cites W2053174683 @default.
• W2013613294 cites W2054009022 @default.
• W2013613294 cites W2068818952 @default.
• W2013613294 cites W207069409 @default.
• W2013613294 cites W2072022592 @default.
• W2013613294 cites W2073925618 @default.
• W2013613294 cites W2114213874 @default.
• W2013613294 cites W2136906322 @default.
• W2013613294 doi "https://doi.org/10.1074/jbc.272.14.9037" @default.
• W2013613294 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9083028" @default.
• W2013613294 hasPublicationYear "1997" @default.
• W2013613294 type Work @default.
• W2013613294 sameAs 2013613294 @default.
• W2013613294 citedByCount "58" @default.
• W2013613294 countsByYear W20136132942012 @default.
• W2013613294 countsByYear W20136132942013 @default.
• W2013613294 countsByYear W20136132942014 @default.
• W2013613294 countsByYear W20136132942015 @default.
• W2013613294 countsByYear W20136132942016 @default.
• W2013613294 countsByYear W20136132942018 @default.
• W2013613294 countsByYear W20136132942019 @default.
• W2013613294 countsByYear W20136132942021 @default.
• W2013613294 countsByYear W20136132942022 @default.
• W2013613294 countsByYear W20136132942023 @default.
• W2013613294 crossrefType "journal-article" @default.
• W2013613294 hasAuthorship W2013613294A5012227349 @default.
• W2013613294 hasAuthorship W2013613294A5026131228 @default.
• W2013613294 hasAuthorship W2013613294A5037645081 @default.
• W2013613294 hasAuthorship W2013613294A5052788564 @default.
• W2013613294 hasAuthorship W2013613294A5056461765 @default.
• W2013613294 hasAuthorship W2013613294A5059296721 @default.
• W2013613294 hasAuthorship W2013613294A5076886453 @default.
• W2013613294 hasAuthorship W2013613294A5081937972 @default.
• W2013613294 hasAuthorship W2013613294A5091680206 @default.
• W2013613294 hasBestOaLocation W20136132941 @default.
• W2013613294 hasConcept C104317684 @default.
• W2013613294 hasConcept C118892022 @default.
• W2013613294 hasConcept C135285700 @default.
• W2013613294 hasConcept C143065580 @default.
• W2013613294 hasConcept C153911025 @default.
• W2013613294 hasConcept C170493617 @default.
• W2013613294 hasConcept C174510640 @default.
• W2013613294 hasConcept C185592680 @default.
• W2013613294 hasConcept C207583985 @default.
• W2013613294 hasConcept C2777593968 @default.
• W2013613294 hasConcept C2779178603 @default.
• W2013613294 hasConcept C54009773 @default.
• W2013613294 hasConcept C55493867 @default.
• W2013613294 hasConcept C62478195 @default.
• W2013613294 hasConcept C79879829 @default.
• W2013613294 hasConcept C86803240 @default.
• W2013613294 hasConcept C95444343 @default.
• W2013613294 hasConceptScore W2013613294C104317684 @default.
• W2013613294 hasConceptScore W2013613294C118892022 @default.
• W2013613294 hasConceptScore W2013613294C135285700 @default.
• W2013613294 hasConceptScore W2013613294C143065580 @default.
• W2013613294 hasConceptScore W2013613294C153911025 @default.
• W2013613294 hasConceptScore W2013613294C170493617 @default.
• W2013613294 hasConceptScore W2013613294C174510640 @default.
• W2013613294 hasConceptScore W2013613294C185592680 @default.
• W2013613294 hasConceptScore W2013613294C207583985 @default.
• W2013613294 hasConceptScore W2013613294C2777593968 @default.
• W2013613294 hasConceptScore W2013613294C2779178603 @default.

• next