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Article: Interactions of bismuth with human lactoferrin and recognition of the Bi III - Lactoferrin complex by intestinal cells

TitleInteractions of bismuth with human lactoferrin and recognition of the Bi III - Lactoferrin complex by intestinal cells
Authors
Issue Date2001
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 2001, v. 40 n. 44, p. 13281-13287 How to Cite?
AbstractSeveral bismuth compounds are currently used as antiulcer drugs, but the mechanism of action still remains unclear. The antimicrobial activity of Bi III complexes toward Gram-negative bacteria is reported to be dependent on the iron uptake system [Domenico, P., et al. (1996) J. Antimicrob. Chemother. 38, 1031-1040]. Electronic absorption and 13C NMR spectroscopic data show that Bi III binds to human lactoferrin at the specific Fe III sites along with either carbonate or oxalate as the synergistic anion. The uptake of Bi III by apo-hLF was rapid [minutes in 10 mM Hepes buffer and 5 mM bicarbonate (pH 7.4)], and almost equal in both lobes. The presence of ATP facilitates the release of Bi III from the Bi 2-hLF complex when the pH is lowered. The Bi 2-hLF complex blocked the uptake of the radiolabeled 59Fe-hLF complex into rat IEC-6 cells. Surprisingly, apo-hLF (but not apotransferrin) was almost as effective in blocking 59Fe uptake as bismuth-loaded lactoferrin. These results suggest that Bi III-loaded hLF might be recognized by the lactoferrin receptor and be taken up into cells.
Persistent Identifierhttp://hdl.handle.net/10722/167698
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Len_US
dc.contributor.authorKa Yee Szetoen_US
dc.contributor.authorWai Biu Wongen_US
dc.contributor.authorTat Tuck Lohen_US
dc.contributor.authorSadler, PJen_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2012-10-08T03:10:11Z-
dc.date.available2012-10-08T03:10:11Z-
dc.date.issued2001en_US
dc.identifier.citationBiochemistry, 2001, v. 40 n. 44, p. 13281-13287en_US
dc.identifier.issn0006-2960en_US
dc.identifier.urihttp://hdl.handle.net/10722/167698-
dc.description.abstractSeveral bismuth compounds are currently used as antiulcer drugs, but the mechanism of action still remains unclear. The antimicrobial activity of Bi III complexes toward Gram-negative bacteria is reported to be dependent on the iron uptake system [Domenico, P., et al. (1996) J. Antimicrob. Chemother. 38, 1031-1040]. Electronic absorption and 13C NMR spectroscopic data show that Bi III binds to human lactoferrin at the specific Fe III sites along with either carbonate or oxalate as the synergistic anion. The uptake of Bi III by apo-hLF was rapid [minutes in 10 mM Hepes buffer and 5 mM bicarbonate (pH 7.4)], and almost equal in both lobes. The presence of ATP facilitates the release of Bi III from the Bi 2-hLF complex when the pH is lowered. The Bi 2-hLF complex blocked the uptake of the radiolabeled 59Fe-hLF complex into rat IEC-6 cells. Surprisingly, apo-hLF (but not apotransferrin) was almost as effective in blocking 59Fe uptake as bismuth-loaded lactoferrin. These results suggest that Bi III-loaded hLF might be recognized by the lactoferrin receptor and be taken up into cells.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_US
dc.relation.ispartofBiochemistryen_US
dc.subject.meshAdenosine Triphosphate - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshBismuth - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshEnzyme Stabilityen_US
dc.subject.meshGram-Negative Bacteriaen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshIntestinal Absorptionen_US
dc.subject.meshIntestinal Mucosa - Metabolismen_US
dc.subject.meshIron - Chemistryen_US
dc.subject.meshLactoferrin - Metabolismen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshRatsen_US
dc.subject.meshSpectrophotometry, Atomicen_US
dc.subject.meshSpectrophotometry, Ultravioleten_US
dc.titleInteractions of bismuth with human lactoferrin and recognition of the Bi III - Lactoferrin complex by intestinal cellsen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/bi010579ten_US
dc.identifier.pmid11683638-
dc.identifier.scopuseid_2-s2.0-0035818422en_US
dc.identifier.hkuros76450-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035818422&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume40en_US
dc.identifier.issue44en_US
dc.identifier.spage13281en_US
dc.identifier.epage13287en_US
dc.identifier.isiWOS:000172057100019-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhang, L=15039869400en_US
dc.identifier.scopusauthoridKa Yee Szeto=7006866001en_US
dc.identifier.scopusauthoridWai Biu Wong=37162593000en_US
dc.identifier.scopusauthoridTat Tuck Loh=37161806200en_US
dc.identifier.scopusauthoridSadler, PJ=7103024488en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US

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