The effect of mild oxidants on glycolysis in human erythrocytes

Harrison, Marietta L.; Rathinavelu, Prema; Arese, Paolo; Geahlen, Robert L.; Low, Philip S.

doi:10.1042/bj2830622

Cited by 3 publications

(2 citation statements)

References 6 publications

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“…Protein tyrosine phosphorylation in the intact cell can also be promoted by a variety of agents, notably agents which affect the system via oxidative stress [5–16]. These include hydrogen peroxide (usually added to the cells together with the PTP inhibitor vanadate, or generated within the cell) [5, 8–13], the thiol oxidizing agent diamide [6–8], thiol alkylating agents [11, 13], nitric oxide [14, 15], as well as UV irradiation [13]. In some cases, the enhanced tyrosine phosphorylation was suggested to result from direct oxidation and activation of PTK [7, 10, 12].…”

Section: Introductionmentioning

confidence: 99%

Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3‐associated phosphotyrosine phosphatase

1997

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Section: Introductionmentioning

confidence: 99%

Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3‐associated phosphotyrosine phosphatase

1997

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“…Phosphorylation by syk 25 releases the enzymes, and glycolysis levels in the cell increase. 26 That is, tyrosine phosphorylation is a negative control mechanism in the case of band 3-glycolytic enzyme association. The levels of glycolytic intermediates can be varied 30-fold by altering the level of band 3-enzyme association through phosphorylation of band 3.…”

Section: P S I L O O P I N B a N D 3 -G L Y C O L Y T I C E N Z Y M Ementioning

confidence: 99%

NMR structure of phospho-tyrosine signaling complexes

et al. 1999

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A structural basis for activation and substrate specificity of src tyrosine kinases, and regulation of protein–protein association by tyrosine phosphorylation is described. Lyn, a src‐family tyrosine kinase, recognizes and phosphorylates the immunoreceptor tyrosine‐based activation motif, ITAM, a critical component in transmembrane signal transduction in hemopoietic cells. The structure of an ITAM peptide substrate bound to an active form of Lyn tyrosine kinase was determined by high‐resolution NMR, and a model of the complex was generated using the crystallographic structure of Lck, a closely related Src‐family kinase. The results provide a rationale for the conserved ITAM residues and specificity of Lyn, and suggest that substrate plays a role in stabilizing the kinase conformation optimal for catalysis. It is our hope that the Lck‐ITAM peptide model complex will be useful in aiding structure‐based drug design efforts that target substrate binding determinants in the design. Concerning the regulation of protein–protein association, we report on a complex between erythrocyte band 3 and two glycolytic enzymes, aldolase and glyceraldehyde‐3‐phosphate dehydrogenase. The formation of this complex is negatively regulated by tyrosine phosphorylation of band 3 by p72syk tyrosine kinase. In red blood cells, this association results in a decrease in glycolysis due to competitive inhibition of the glycolytic enzymes. The structure of band 3 recognized by the glycolytic enzymes was determined by solution NMR, and found to be a loop structure with tyrosine centrally positioned and excluded from intermolecular contact. This phosphorylation sensitive interaction, or PSI, loop may be the basis of a general mechanism for negative regulation through tyrosine phosphorylation. © 1999 John Wiley & Sons, Inc. Med Res Rev, 19, No. 4, 295–305, 1999.

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Some red blood cell phenomena for the curious

Hoffman¹

2004

Blood Cells, Molecules, and Diseases

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The effect of mild oxidants on glycolysis in human erythrocytes

Cited by 3 publications

References 6 publications

Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3‐associated phosphotyrosine phosphatase

Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3‐associated phosphotyrosine phosphatase

NMR structure of phospho-tyrosine signaling complexes

Some red blood cell phenomena for the curious

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