Biochemical and Biophysical Research Communications
Volume 198, Issue 1, 15 January 1994, Pages 52-59
Regular ArticleRegulation of Alternative Pathway Complement Activation by Glycosaminoglycans: Specificity of the Polyanion Binding Site on Factor H
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Cited by (116)
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2016, ImmunobiologyCitation Excerpt :Removal of C8 and C9 carbons from Sia with NaIO4 treatment renders sheep erythrocytes susceptible to lysis by the alternative pathway (Fearon, 1978) Certain other polyanions such as highly sulfated heparin, heparain sulfate, dermatan sulfate, chondroitin sulfate A and carrageenan (types III and IV) also enhance the affinity of FH for surface-bound C3b and promote complement inhibition (Carreno et al., 1989; Kazatchkine et al., 1979; Meri and Pangburn, 1990, 1994). Kajander et al. proposed a model in which FH domains 19 and 20 interacted with C3 fragments and cell surface polyanions, respectively (Kajander et al., 2011).
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