Matches in SemOpenAlex for { <https://semopenalex.org/work/W2010214150> ?p ?o ?g. }
- W2010214150 endingPage "5830" @default.
- W2010214150 startingPage "5820" @default.
- W2010214150 abstract "The reductant dependence of iron mobilization from isolated rabbit reticulocyte endosomes containing diferric transferrin is reported. The kinetic effects of acidification by a H(+)-ATPase are eliminated by incubating the endosomes at pH 6.0 in the presence of 15 microM FCCP to acidify the intravesicular milieu and to dissociate 59Fe(III) from transferrin. In the absence of reductants, iron is not released from the vesicles, and iron leakage is negligible. The second-order dependence of rate constants and amounts of 59Fe mobilized from endosomes using ascorbate, ferrocyanide, or NADH are consistent with reversible mechanisms. The estimated apparent first-order rate constant for mobilization by ascorbate is (2.7 +/- 0.4) x 10(-3) s-1 in contrast to (3.2 +/- 0.1) x 10(-4) s-1 for NADH and (3.5 +/- 0.6) x 10(-4) s-1 for ferrocyanide. These results support models where multiple reactions are involved in complex processes leading to iron transfer and membrane translocation. A type II NADH dehydrogenase (diaphorase) is present on the endosome outer membrane. The kinetics of extravesicular ferricyanide reduction indicate a bimolecular-bimolecular steady-state mechanism with substrate inhibition. Ferricyanide inhibition of 59Fe mobilization is not detected. Significant differences between mobilization and ferricyanide reduction kinetics indicate that the diaphorase is not involved in 59Fe(III) reduction. Sequential additions of NADH followed by ascorbate or vice versa indicate a minimum of two sites of 59Fe(III) residence; one site available to reducing equivalents from ascorbate and a different site available to NADH. Sequential additions using ferrocyanide and the other reductants suggest interactions among sites available for reduction. Inhibition of ascorbate-mediated mobilization by DCCD and enhancement of ferrocyanide and NADH-mediated mobilization suggest a role for a moiety with characteristics of a proton pore similar to that of the H(+)-ATPase. These data provide significant constraints on models of iron reduction, translocation, and mobilization by endocytic vesicles." @default.
- W2010214150 created "2016-06-24" @default.
- W2010214150 creator A5008660028 @default.
- W2010214150 creator A5011854092 @default.
- W2010214150 creator A5038238152 @default.
- W2010214150 creator A5049100373 @default.
- W2010214150 creator A5052082041 @default.
- W2010214150 creator A5055119159 @default.
- W2010214150 creator A5087293704 @default.
- W2010214150 date "1992-06-30" @default.
- W2010214150 modified "2023-09-25" @default.
- W2010214150 title "Kinetic characterization of reductant dependent processes of iron mobilization from endocytic vesicles" @default.
- W2010214150 cites W1500500707 @default.
- W2010214150 cites W1500658881 @default.
- W2010214150 cites W1567706221 @default.
- W2010214150 cites W1590684642 @default.
- W2010214150 cites W1599567494 @default.
- W2010214150 cites W1606741128 @default.
- W2010214150 cites W1606989763 @default.
- W2010214150 cites W1647656396 @default.
- W2010214150 cites W1966759550 @default.
- W2010214150 cites W1999491269 @default.
- W2010214150 cites W2005766024 @default.
- W2010214150 cites W2024557451 @default.
- W2010214150 cites W2041400247 @default.
- W2010214150 cites W2068548237 @default.
- W2010214150 cites W2094523631 @default.
- W2010214150 cites W2148416836 @default.
- W2010214150 cites W2409594353 @default.
- W2010214150 cites W2412176019 @default.
- W2010214150 cites W2412451383 @default.
- W2010214150 cites W2414371662 @default.
- W2010214150 cites W2417473218 @default.
- W2010214150 cites W4246090862 @default.
- W2010214150 doi "https://doi.org/10.1021/bi00140a018" @default.
- W2010214150 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1535218" @default.
- W2010214150 hasPublicationYear "1992" @default.
- W2010214150 type Work @default.
- W2010214150 sameAs 2010214150 @default.
- W2010214150 citedByCount "36" @default.
- W2010214150 countsByYear W20102141502012 @default.
- W2010214150 countsByYear W20102141502013 @default.
- W2010214150 countsByYear W20102141502014 @default.
- W2010214150 countsByYear W20102141502016 @default.
- W2010214150 crossrefType "journal-article" @default.
- W2010214150 hasAuthorship W2010214150A5008660028 @default.
- W2010214150 hasAuthorship W2010214150A5011854092 @default.
- W2010214150 hasAuthorship W2010214150A5038238152 @default.
- W2010214150 hasAuthorship W2010214150A5049100373 @default.
- W2010214150 hasAuthorship W2010214150A5052082041 @default.
- W2010214150 hasAuthorship W2010214150A5055119159 @default.
- W2010214150 hasAuthorship W2010214150A5087293704 @default.
- W2010214150 hasConcept C102747710 @default.
- W2010214150 hasConcept C121332964 @default.
- W2010214150 hasConcept C12554922 @default.
- W2010214150 hasConcept C130316041 @default.
- W2010214150 hasConcept C147789679 @default.
- W2010214150 hasConcept C148898269 @default.
- W2010214150 hasConcept C17525397 @default.
- W2010214150 hasConcept C179104552 @default.
- W2010214150 hasConcept C185592680 @default.
- W2010214150 hasConcept C2776043530 @default.
- W2010214150 hasConcept C2777411777 @default.
- W2010214150 hasConcept C41625074 @default.
- W2010214150 hasConcept C55493867 @default.
- W2010214150 hasConcept C62520636 @default.
- W2010214150 hasConcept C75473681 @default.
- W2010214150 hasConcept C79879829 @default.
- W2010214150 hasConcept C86803240 @default.
- W2010214150 hasConcept C93391505 @default.
- W2010214150 hasConceptScore W2010214150C102747710 @default.
- W2010214150 hasConceptScore W2010214150C121332964 @default.
- W2010214150 hasConceptScore W2010214150C12554922 @default.
- W2010214150 hasConceptScore W2010214150C130316041 @default.
- W2010214150 hasConceptScore W2010214150C147789679 @default.
- W2010214150 hasConceptScore W2010214150C148898269 @default.
- W2010214150 hasConceptScore W2010214150C17525397 @default.
- W2010214150 hasConceptScore W2010214150C179104552 @default.
- W2010214150 hasConceptScore W2010214150C185592680 @default.
- W2010214150 hasConceptScore W2010214150C2776043530 @default.
- W2010214150 hasConceptScore W2010214150C2777411777 @default.
- W2010214150 hasConceptScore W2010214150C41625074 @default.
- W2010214150 hasConceptScore W2010214150C55493867 @default.
- W2010214150 hasConceptScore W2010214150C62520636 @default.
- W2010214150 hasConceptScore W2010214150C75473681 @default.
- W2010214150 hasConceptScore W2010214150C79879829 @default.
- W2010214150 hasConceptScore W2010214150C86803240 @default.
- W2010214150 hasConceptScore W2010214150C93391505 @default.
- W2010214150 hasIssue "25" @default.
- W2010214150 hasLocation W20102141501 @default.
- W2010214150 hasLocation W20102141502 @default.
- W2010214150 hasOpenAccess W2010214150 @default.
- W2010214150 hasPrimaryLocation W20102141501 @default.
- W2010214150 hasRelatedWork W153750752 @default.
- W2010214150 hasRelatedWork W1979200566 @default.
- W2010214150 hasRelatedWork W2011715586 @default.
- W2010214150 hasRelatedWork W2024744166 @default.
- W2010214150 hasRelatedWork W2032790643 @default.