FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1489399260> ?p ?o ?g. }

• W1489399260 endingPage "31830" @default.
• W1489399260 startingPage "31822" @default.
• W1489399260 abstract "Bradykinin (BK), a potent vasoactive nonapeptide formed by proteolytic cleavage of kininogen, mediates its activity by binding to specific cell surface receptors. Delivery of BK to these receptors is limited by cell-bound and plasma kininases that degrade BK to inactive fragments. Binding of its parent compound, kininogen, to specific endothelial cell receptors may provide an environment in which the degradation of BK by kininases is restricted. The determinants that mediate kininogen binding to endothelial cells have not been fully elucidated. The present studies suggest that part of BK and the amino-terminal amino acids of kininogens' common light chain constitute part of this recognition sequence. Human umbilical vein endothelial cells (HUVEC) in culture at 37 degrees C express 2-3-fold more binding sites for biotinylated high molecular weight kininogen (biotin-HK) containing BK than for biotin-HK from which BK has been liberated by plasma kallikrein. Binding of BK-free biotin-HK was not restored by preincubating HUVEC with BK, arguing against the possibility that BK released from biotin-HK stimulated expression of additional HK receptors. The extent of biotin-HK binding to HUVEC at 37 degrees C directly correlated with the amount of BK retained within the protein. Four lines of evidence suggest that part of BK and the amino terminus of the light chain of kininogens are part of the sequence recognized by the endothelial cell kininogen receptor. First, monoclonal antibodies to the carboxyl terminus of BK (MBK3) and the common light chains of the kininogens (HKL6, HKL8) inhibited biotin-HK binding to HUVEC. Second, a synthetic, dimeric bradykinin receptor antagonist blocked biotin-HK (IC50 = 9 microM) binding to HUVEC as did two synthetic tissue kallikrein inhibitors modeled after the carboxyl-terminal sequence of BK. Third, synthetic peptides containing the carboxyl-terminal portion of BK and the amino terminus of kininogens' common light chain, MKRPPGFSPFRSSRIG and GFSPFRSSRIG, blocked binding of biotin-HK (IC50 = 2-3 mM), whereas an overlapping peptide, SPFRSSRIGEIKEETT, at 5 mM and a scrambled peptide, FSGPKRSPIMGRPSFR, did not. Fourth, biotinylated GMKRPPGFSPFRSSRIG specifically bound to HUVEC, and its binding was blocked by HK. Since the presence of the nonapeptide BK in HK contributes to maximal binding of HK to HUVEC, there is a novel type of BK receptor in which part of the nonapeptide is recognized within the context of its parent molecule.(ABSTRACT TRUNCATED AT 400 WORDS)" @default.
• W1489399260 created "2016-06-24" @default.
• W1489399260 creator A5066630966 @default.
• W1489399260 creator A5072898800 @default.
• W1489399260 creator A5073501391 @default.
• W1489399260 creator A5077478635 @default.
• W1489399260 date "1994-12-01" @default.
• W1489399260 modified "2023-10-18" @default.
• W1489399260 title "The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain." @default.
• W1489399260 cites W1493873711 @default.
• W1489399260 cites W1499670582 @default.
• W1489399260 cites W1504002777 @default.
• W1489399260 cites W1518292773 @default.
• W1489399260 cites W1522151606 @default.
• W1489399260 cites W1554136003 @default.
• W1489399260 cites W1560626372 @default.
• W1489399260 cites W1584725601 @default.
• W1489399260 cites W1588136625 @default.
• W1489399260 cites W1604352043 @default.
• W1489399260 cites W1978094951 @default.
• W1489399260 cites W1989026791 @default.
• W1489399260 cites W1992076353 @default.
• W1489399260 cites W1994610964 @default.
• W1489399260 cites W2007737411 @default.
• W1489399260 cites W2013813492 @default.
• W1489399260 cites W2044038692 @default.
• W1489399260 cites W2050852845 @default.
• W1489399260 cites W2065583843 @default.
• W1489399260 cites W2078877062 @default.
• W1489399260 cites W2085587120 @default.
• W1489399260 cites W2157603347 @default.
• W1489399260 cites W2288317275 @default.
• W1489399260 cites W2293438303 @default.
• W1489399260 cites W2337219537 @default.
• W1489399260 cites W2411125548 @default.
• W1489399260 cites W2411238771 @default.
• W1489399260 cites W2464029665 @default.
• W1489399260 cites W4293247451 @default.
• W1489399260 cites W79103623 @default.
• W1489399260 doi "https://doi.org/10.1016/s0021-9258(18)31769-1" @default.
• W1489399260 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7989355" @default.
• W1489399260 hasPublicationYear "1994" @default.
• W1489399260 type Work @default.
• W1489399260 sameAs 1489399260 @default.
• W1489399260 citedByCount "48" @default.
• W1489399260 countsByYear W14893992602016 @default.
• W1489399260 countsByYear W14893992602017 @default.
• W1489399260 countsByYear W14893992602023 @default.
• W1489399260 crossrefType "journal-article" @default.
• W1489399260 hasAuthorship W1489399260A5066630966 @default.
• W1489399260 hasAuthorship W1489399260A5072898800 @default.
• W1489399260 hasAuthorship W1489399260A5073501391 @default.
• W1489399260 hasAuthorship W1489399260A5077478635 @default.
• W1489399260 hasBestOaLocation W14893992601 @default.
• W1489399260 hasConcept C104317684 @default.
• W1489399260 hasConcept C134306372 @default.
• W1489399260 hasConcept C14053116 @default.
• W1489399260 hasConcept C1491633281 @default.
• W1489399260 hasConcept C159654299 @default.
• W1489399260 hasConcept C167625842 @default.
• W1489399260 hasConcept C170493617 @default.
• W1489399260 hasConcept C185592680 @default.
• W1489399260 hasConcept C2779591629 @default.
• W1489399260 hasConcept C33923547 @default.
• W1489399260 hasConcept C36394416 @default.
• W1489399260 hasConcept C36503486 @default.
• W1489399260 hasConcept C515207424 @default.
• W1489399260 hasConcept C54355233 @default.
• W1489399260 hasConcept C55493867 @default.
• W1489399260 hasConcept C57711820 @default.
• W1489399260 hasConcept C86803240 @default.
• W1489399260 hasConcept C95444343 @default.
• W1489399260 hasConceptScore W1489399260C104317684 @default.
• W1489399260 hasConceptScore W1489399260C134306372 @default.
• W1489399260 hasConceptScore W1489399260C14053116 @default.
• W1489399260 hasConceptScore W1489399260C1491633281 @default.
• W1489399260 hasConceptScore W1489399260C159654299 @default.
• W1489399260 hasConceptScore W1489399260C167625842 @default.
• W1489399260 hasConceptScore W1489399260C170493617 @default.
• W1489399260 hasConceptScore W1489399260C185592680 @default.
• W1489399260 hasConceptScore W1489399260C2779591629 @default.
• W1489399260 hasConceptScore W1489399260C33923547 @default.
• W1489399260 hasConceptScore W1489399260C36394416 @default.
• W1489399260 hasConceptScore W1489399260C36503486 @default.
• W1489399260 hasConceptScore W1489399260C515207424 @default.
• W1489399260 hasConceptScore W1489399260C54355233 @default.
• W1489399260 hasConceptScore W1489399260C55493867 @default.
• W1489399260 hasConceptScore W1489399260C57711820 @default.
• W1489399260 hasConceptScore W1489399260C86803240 @default.
• W1489399260 hasConceptScore W1489399260C95444343 @default.
• W1489399260 hasIssue "50" @default.
• W1489399260 hasLocation W14893992601 @default.
• W1489399260 hasOpenAccess W1489399260 @default.
• W1489399260 hasPrimaryLocation W14893992601 @default.
• W1489399260 hasRelatedWork W1991233227 @default.
• W1489399260 hasRelatedWork W1994858472 @default.
• W1489399260 hasRelatedWork W2063199722 @default.
• W1489399260 hasRelatedWork W2078660393 @default.

• next