Matches in SemOpenAlex for { <https://semopenalex.org/work/W1938377819> ?p ?o ?g. }
Showing items 1 to 78 of
78
with 100 items per page.
- W1938377819 endingPage "408" @default.
- W1938377819 startingPage "403" @default.
- W1938377819 abstract "Abstract We examined the formation of the early classical complement (C) pathway enzymes on sheep (Es), guinea pig (Egp), and human (Eh) erythrocytes (E). Each species' E were sensitized with sufficient IgM or IgG anti-E Ab to establish equal numbers of C1-fixing sites on all E. After sensitization with 100 C1-fixing sites of Ab and excess C1, uptake of C4 was equivalent on all three cell types, judged by anti-C4 binding (for guinea pig C4) or by direct uptake of radiolabeled protein (for human C4). With equal numbers of cell-bound C1 and C4, however, there were marked differences in C2 convertase activity on Es, Egp, and Eh. Sheep EAC14 utilized C2 at least 20 times faster than Egp and Eh bearing the same number of C1 and C4 molecules. C3 cleavage was even further depressed on Egp and Eh, and was not changed by the substitution of oxyC2 for normal human C2. In whole guinea pig serum (GPS), 300 times more C1-fixing sites were required on Egp than on Es to achieve similar amounts of lysis; however, equivalent C3 uptake on Egp and Es was associated with equal extents of lysis, demonstrating that GPS lysis of these cells was regulated by early steps in classical pathway (CP) activation. Incubation of E bearing radiolabeled C4b with Factor I demonstrated that C4b on Egp was highly resistant to cleavage compared to the same protein bound to Es or Eh. Studies with partially purified C3 convertase decay-accelerating factors from Eh stroma demonstrated that these membrane proteins could not account for the observed surface regulation of CP activity because these proteins do not affect the rate of C2 cleavage by EAC14. We conclude that E surface molecules have an important role in modulation of CP activation. This surface-associated CP regulation occurs at the level of cell-bound C4b." @default.
- W1938377819 created "2016-06-24" @default.
- W1938377819 creator A5016603844 @default.
- W1938377819 creator A5035493694 @default.
- W1938377819 creator A5048214608 @default.
- W1938377819 creator A5056223703 @default.
- W1938377819 date "1983-07-01" @default.
- W1938377819 modified "2023-10-18" @default.
- W1938377819 title "Surface modulation of classical pathway activation: C2 and C3 convertase formation and regulation on sheep, guinea pig, and human erythrocytes." @default.
- W1938377819 doi "https://doi.org/10.4049/jimmunol.131.1.403" @default.
- W1938377819 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6602833" @default.
- W1938377819 hasPublicationYear "1983" @default.
- W1938377819 type Work @default.
- W1938377819 sameAs 1938377819 @default.
- W1938377819 citedByCount "10" @default.
- W1938377819 countsByYear W19383778192014 @default.
- W1938377819 crossrefType "journal-article" @default.
- W1938377819 hasAuthorship W1938377819A5016603844 @default.
- W1938377819 hasAuthorship W1938377819A5035493694 @default.
- W1938377819 hasAuthorship W1938377819A5048214608 @default.
- W1938377819 hasAuthorship W1938377819A5056223703 @default.
- W1938377819 hasBestOaLocation W19383778191 @default.
- W1938377819 hasConcept C111684460 @default.
- W1938377819 hasConcept C134018914 @default.
- W1938377819 hasConcept C151730666 @default.
- W1938377819 hasConcept C153911025 @default.
- W1938377819 hasConcept C159654299 @default.
- W1938377819 hasConcept C171279029 @default.
- W1938377819 hasConcept C175156509 @default.
- W1938377819 hasConcept C181199279 @default.
- W1938377819 hasConcept C185592680 @default.
- W1938377819 hasConcept C189446657 @default.
- W1938377819 hasConcept C203014093 @default.
- W1938377819 hasConcept C2778815084 @default.
- W1938377819 hasConcept C43369102 @default.
- W1938377819 hasConcept C55493867 @default.
- W1938377819 hasConcept C57409179 @default.
- W1938377819 hasConcept C86803240 @default.
- W1938377819 hasConcept C9478725 @default.
- W1938377819 hasConceptScore W1938377819C111684460 @default.
- W1938377819 hasConceptScore W1938377819C134018914 @default.
- W1938377819 hasConceptScore W1938377819C151730666 @default.
- W1938377819 hasConceptScore W1938377819C153911025 @default.
- W1938377819 hasConceptScore W1938377819C159654299 @default.
- W1938377819 hasConceptScore W1938377819C171279029 @default.
- W1938377819 hasConceptScore W1938377819C175156509 @default.
- W1938377819 hasConceptScore W1938377819C181199279 @default.
- W1938377819 hasConceptScore W1938377819C185592680 @default.
- W1938377819 hasConceptScore W1938377819C189446657 @default.
- W1938377819 hasConceptScore W1938377819C203014093 @default.
- W1938377819 hasConceptScore W1938377819C2778815084 @default.
- W1938377819 hasConceptScore W1938377819C43369102 @default.
- W1938377819 hasConceptScore W1938377819C55493867 @default.
- W1938377819 hasConceptScore W1938377819C57409179 @default.
- W1938377819 hasConceptScore W1938377819C86803240 @default.
- W1938377819 hasConceptScore W1938377819C9478725 @default.
- W1938377819 hasIssue "1" @default.
- W1938377819 hasLocation W19383778191 @default.
- W1938377819 hasLocation W19383778192 @default.
- W1938377819 hasOpenAccess W1938377819 @default.
- W1938377819 hasPrimaryLocation W19383778191 @default.
- W1938377819 hasRelatedWork W13594097 @default.
- W1938377819 hasRelatedWork W1677039908 @default.
- W1938377819 hasRelatedWork W1777690075 @default.
- W1938377819 hasRelatedWork W2013302811 @default.
- W1938377819 hasRelatedWork W2030382685 @default.
- W1938377819 hasRelatedWork W2045407001 @default.
- W1938377819 hasRelatedWork W2415562614 @default.
- W1938377819 hasRelatedWork W2462315822 @default.
- W1938377819 hasRelatedWork W4228996633 @default.
- W1938377819 hasRelatedWork W4313309189 @default.
- W1938377819 hasVolume "131" @default.
- W1938377819 isParatext "false" @default.
- W1938377819 isRetracted "false" @default.
- W1938377819 magId "1938377819" @default.
- W1938377819 workType "article" @default.