Linked Life Data

15087282

Source:http://linkedlifedata.com/resource/pubmed/id/15087282

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-7-23
pubmed:abstractText
Several vital functions/physical characteristics of erythrocytes (including glycolysis, the pentose phosphate pathway, ion fluxes, and cellular deformability) display dependence on the state of hemoglobin oxygenation. The molecular mechanism proposed involves an interaction between deoxyhemoglobin and the cytoplasmic domain of the anion-exchange protein, band 3 (cdB3). Given that band 3 also binds to membrane proteins 4.1 and 4.2, several kinases, hemichromes, and integral membrane proteins, and at least three glycolytic enzymes, it has been suggested that the cdB3-deoxyhemoglobin interaction might modulate the pathways mediated by these associated proteins in an O(2)-dependent manner. We have investigated this mechanism by synthesizing 10-mer peptides corresponding to the NH(2)-terminal fragments of various vertebrate cdB3s, determining their effects on the oxygenation reactions of hemoglobins from the same and different species and examining binding of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase to the erythrocytic membrane of mouse erythrocytes. The cdB3 interaction is strongly dependent on pH and the number of negative and positive charges of the peptide and at the effector binding site, respectively. It lowers the O(2) association equilibrium constant of the deoxygenated (Tense) state of the hemoglobin and is inhibited by magnesium ions, which neutralize cdB3's charge and by 2,3-diphosphoglycerate, which competes for the cdB3-binding site. The interaction is stronger in humans (whose erythrocytes derive energy predominantly from glycolysis and exhibit higher buffering capacity) than in birds and ectothermic vertebrates (whose erythrocytes metabolize aerobically and are poorly buffered) and is insignificant in fish, suggesting that its role in the regulation of red cell glycolysis increased with phylogenetic development in vertebrates.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0363-6119
pubmed:author
pubmed:issnType
Print
pubmed:volume
287
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
R454-64
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15087282-2,3-Diphosphoglycerate, pubmed-meshheading:15087282-Amino Acid Sequence, pubmed-meshheading:15087282-Animals, pubmed-meshheading:15087282-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:15087282-Buffers, pubmed-meshheading:15087282-Chickens, pubmed-meshheading:15087282-Erythrocytes, pubmed-meshheading:15087282-Fishes, pubmed-meshheading:15087282-Glyceraldehyde-3-Phosphate Dehydrogenases, pubmed-meshheading:15087282-Glycolysis, pubmed-meshheading:15087282-Hemoglobins, pubmed-meshheading:15087282-Humans, pubmed-meshheading:15087282-Hydrogen-Ion Concentration, pubmed-meshheading:15087282-Magnesium, pubmed-meshheading:15087282-Molecular Sequence Data, pubmed-meshheading:15087282-Oxyhemoglobins, pubmed-meshheading:15087282-Phosphoric Acid Esters, pubmed-meshheading:15087282-Protein Structure, Tertiary, pubmed-meshheading:15087282-Vertebrates
pubmed:year
2004
pubmed:articleTitle
Modulation of red cell glycolysis: interactions between vertebrate hemoglobins and cytoplasmic domains of band 3 red cell membrane proteins.
pubmed:affiliation
Zoophysiology Department, Institute of Biological Sciences, University of Aarhus, DK 8000 Aarhus, Denmark; . roy.weber@biology.au.dk
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't