A reappraisal of the binding of cytosolic enzymes to erythrocyte membranes

Maretzki, D; Reimann, Bettina; Rapoport, S.

doi:10.1016/0968-0004(89)90128-x

Cited by 56 publications

(19 citation statements)

References 37 publications

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“…The criticisms of Maretzki et al [18] rely mainly on the fact that glycolytic enzymes bind poorly to the red cell membrane except under hypotonic conditions or hypotonic hemolysis. This ignores a series of other experiments using a variety of techniques which indicate binding of glycolytic enzymes to the red cell membrane (see [6] for review).…”

Section: Glycolysismentioning

confidence: 99%

Enzyme‐enzyme interactions and their metabolic role

1990

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There are continuing reports on the existence ofcomplcxes of sequential metabolic enzymes. New techniques for their detection have been described and include afinity electrophorcsis and the use of :mti-idlotypic antIbodIes. Channeling of substrates has been reported for several systems as well as direct substrate transfer through dynamic enzyme associations.Kinetic parameters of metabolic control of organized sjsterns hale been formulated and tested in several systems. These recent results arc expanding our understanding of metabolic proccsws and their control.

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Section: Glycolysismentioning

confidence: 99%

Enzyme‐enzyme interactions and their metabolic role

1990

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“…Indeed, the GE binding sequence at the NH 2 terminus of band 3 is one of the least conserved regions of the polypeptide (13)(14)(15). Third, despite significant differences in GAPDH retention in hypotonically prepared membranes, all mammalian RBCs exhibit similar glycolytic rates (16), suggesting that any differences seen in membrane association have no functional consequence. Fourth, more recent studies employing a modified version of the aforementioned rapid filtration technique report no evidence for membrane binding of GEs when proper adjustment for the kinetics of hemolysis is made (10).…”

mentioning

confidence: 99%

“…Fourth, more recent studies employing a modified version of the aforementioned rapid filtration technique report no evidence for membrane binding of GEs when proper adjustment for the kinetics of hemolysis is made (10). And finally, mathematical modeling of glycolytic fluxes in human RBCs does not require consideration of any inhibitory band 3-enzyme complexes to achieve a good fit with the experimental data (16). In fact, the catalytic capacity of GAPDH in human RBCs is so high that inhibition of Ͼ90% of the enzyme through association with band 3 would not be expected to affect the glycolytic flux (16).…”

mentioning

confidence: 99%

“…And finally, mathematical modeling of glycolytic fluxes in human RBCs does not require consideration of any inhibitory band 3-enzyme complexes to achieve a good fit with the experimental data (16). In fact, the catalytic capacity of GAPDH in human RBCs is so high that inhibition of Ͼ90% of the enzyme through association with band 3 would not be expected to affect the glycolytic flux (16). Thus, given the absence of compelling experimental evidence for a band 3 interaction in vivo and the lack of a strong theoretical argument for its existence, the concept of a membrane-localized compartment of GEs has been dismissed by its opponents as an experimental artifact (16,17).…”

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confidence: 99%

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Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane

Campanella

Chu

Low

2005

Proc. Natl. Acad. Sci. U.S.A.

356

327

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To characterize the location of glycolytic enzymes (GEs) in intact human erythrocytes, freshly drawn blood was fixed and stained with Abs to GAPDH, aldolase, phosphofructokinase (PFK), pyruvate kinase (PK), lactate dehydrogenase (LDH), carbonic anhydrase II, Hb, and band 3 (AE1). Confocal microscopy revealed that in cells where band 3 displays its expected membrane staining and Hb is evenly distributed across the cytoplasm, GEs are largely limited to the membrane. Biochemical studies confirmed that the membrane binding sites for GAPDH, aldolase, and PFK reside on band 3, but related analyses demonstrate that sites for PK and LDH do not. Four lines of evidence demonstrate that the GEs are at least partially assembled into multimeric complexes near the NH2 terminus of band 3. First, a mAb to residues 1-12 of band 3 displaces all of the above GEs from the membrane, including LDH and PK, which do not bind band 3. Second, tyrosine phosphorylation of the NH2 terminus of band 3 (Y8 and Y21) reversibly releases all of the GEs from the membrane, including LDH and PK. Third, deoxygenation of RBCs dislodges all GEs from the membrane, consistent with the established ability of deoxyHb but not oxyHb to bind the NH2 terminus of band 3. Fourth, a large increase in the accessibility of enzyme epitopes is observed upon dissociation of GEs from the membrane. We conclude, therefore, that GEs are organized into complexes on the membrane whose assembly is regulated by oxygenation and phosphorylation.GAPDH ͉ band 3 ͉ AE1 ͉ metabolon ͉ compartmentalization

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“…Ova'di (28) has confirmed the direct channeling of substrates among aldolase, TPI, and glyceraldehyde-3-phosphate dehydrogenase in erythrocytes when the protein concentration was held high. The relevance of glycolytic enzyme interactions with band 3 has been repeatedly questioned (29,30). However, the most recent data of Low et at (31) …”

Section: Discussionmentioning

confidence: 98%

Erythrocyte lipids in triose-phosphate isomerase deficiency.

Hollán

Dey

Szollár

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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Marked hypoalphalipoproteinemia was found together with relatively low serum cholesterol, triacylglycerol, and LDL levels in a triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 53.1.1)-deficient Hungarian family, especially in the two compound-heterozygote brothers. Apart from a slight increase in palmitic and stearic acids together with a slight decrease in oleic and linoleic acids, no other changes were found in the fatty acid composition of the erythrocyte phospholipids. Anisotropy measurements with n-(9-anthroyloxy)stearic and -palmitic acid fluorophores revealed increased motional freedom of the fatty acid chains in the external lipid layers of the intact erythrocytes from all members of the TPI-deficient family as compared with normal agematched controls. This asymmetric increase in membrane fluidity was found to be significantly higher in the propositus than in his compound-heterozygote brother without any neurological disorders. The change in membrane fluidity may result fromas-yet-unresolved aspects of the lipid composition of the plasma membrane. Our findings that the differences between the TPIdeficient individuals and normal controls and the differences between the two compound-heterozygote brothers were all absent in the phospholipid extracts of the same erythrocytes favor the assumption that the increased motional freedom of the fatty acid chains in the external surface of the bilayer is caused by the binding of the mutant TPI molecule to the N-terminal sequence of band 3 protein.

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A reappraisal of the binding of cytosolic enzymes to erythrocyte membranes

Cited by 56 publications

References 37 publications

Enzyme‐enzyme interactions and their metabolic role

Enzyme‐enzyme interactions and their metabolic role

Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane

Erythrocyte lipids in triose-phosphate isomerase deficiency.

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