Both ankyrin and band 4.1 are required to restrict the rotational mobility of band 3 in the human erythrocyte membrane

Wyatt, Katrina; Cherry, Richard J.

doi:10.1016/0005-2736(92)90104-t

Cited by 18 publications

(19 citation statements)

References 17 publications

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“…In normal bone marrow myeloid precursors [3], cultured human myeloid cell lines [3, 4, 16, 19, 20, 22, 23], and our HEK expression system [10], some of the newly synthesized proMPO retains the pro-peptide and is constitutively secreted.…”

Section: Resultsmentioning

confidence: 99%

“…Although little is known about the function or fate of the pro-peptide of MPO, it does not serve as a sorting determinant that directs proMPO selectively to azurophilic granules [18, 19] and its deletion results in an arrest in processing [20]. Although most of the proMPO synthesized in the ER undergoes proteolytic processing and targeting to azurophilic granules, a substantial fraction is constitutively secreted by normal bone marrow granulocyte precursors [3] as well as by cultured human myeloid cell lines [3, 4, 16, 19–23] and heterologous lines expressing recombinant MPO [9, 10]. …”

Section: Introductionmentioning

confidence: 99%

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Proconvertase proteolytic processing of an enzymatically active myeloperoxidase precursor

McCormick¹,

Nelson²,

Nauseef³

2012

Archives of Biochemistry and Biophysics

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Optimal and efficient killing of ingested microbes by human neutrophils is mediated in large part by the action of hypochlorous acid produced by the myeloperoxidase-H2O2-chloride system in phagosomes. Myeloperoxidase gene transcription is limited to early myeloid precursors in the bone marrow, when myeloperoxidase is synthesized and stored in azurophilic granules for subsequent release from stimulated neutrophils. Promyeloperoxidase, the 90-kDa myeloperoxidase precursor synthesized in the endoplasmic reticulum (ER), contains a 125-amino acid pro-region whose function and fate during myeloperoxidase biosynthesis are unknown. Promyeloperoxidase has two fates during myeloperoxidase biosynthesis; the majority undergoes proteolytic processing to generate mature myeloperoxidase, while the remainder is constituvely secreted from the cells in bone marrow. We used a promyelocytic cell line that produces endogenous myelperoxidase as well as human embryonic kidney cells stably expressing normal and mutant forms of myeloperoxidase to examine proteolytic processing of promyeloperoxidase. We demonstrated that CMK-RVKR, an inhibitor of subtilisin-like proteinases, blocked cleavage of the pro-peptide of promyeloperoxidase in a post-ER compartment. Mutants with alanine substitution of basic residues in the predicted proteinase cleavage site failed to undergo maturation to normal myeloperoxidase subunits and were arrested at the promyeloperoxidase stage. Whereas specific mutants varied as to their stability, secreted promyeloperoxidase from the mutants retained the capacity to generate hypochlorous acid. Taken together, these studies demonstrate proconvertase-dependent cleavage of promyeloperoxidase as an essential step in normal proteolytic processing and granule targeting of myeloperoxidase. Furthermore, although mutations in the proteinase cleavage site reduced intracellular stability of the mutants, the integrity of the heme group was not compromised, as chlorinating activity was retained in the secreted promyeloperoxidase.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proconvertase proteolytic processing of an enzymatically active myeloperoxidase precursor

McCormick¹,

Nelson²,

Nauseef³

2012

Archives of Biochemistry and Biophysics

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“…The molecular interactions that control band 3 rotational diffusion appear to involve both band 3 self-association (aggregation) in the plane of the RBC membrane (36,41) and specific binding interactions between the cytoplasmic domain of band 3 and membrane skeletal proteins (4,5,37,67) These data suggest that control of band 3 lateral mobility depends on the absolute number of spectrin molecules in the membrane skeleton and not on the state of spectrin oligomerization. Thus, the spectrin dimer-dimer interaction is unlikely to be important for the regulation of band 3 lateral diffusion.…”

Section: Methodsmentioning

confidence: 91%

Differential control of band 3 lateral and rotational mobility in intact red cells.

Corbett¹,

Agre²,

Palek³

et al. 1994

J. Clin. Invest.

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Measurements of integral membrane protein lateral mobility and rotational mobility have been separately used to investigate dynamic protein-protein and protein-lipid interactions that underlie plasma membrane structure and function. In model bilayer membranes, the mobilities of reconstituted proteins depend on the size of the diffusing molecule and the viscosity of the lipid bilayer. There are no direct tests, however, of the relationship between mechanisms that control protein lateral mobility and rotational mobility in intact biological membranes. We have measured the lateral and rotational mobility of band 3 in spectrin-deficient red blood cells from patients with hereditary spherocytosis and hereditary pyropoikilocytosis. Our data suggest that band 3 lateral mobility is regulated by the spectrin content of the red cell membrane. In contrast, band 3 rotational mobility is unaffected by changes in spectrin content. Band 3 lateral mobility and rotational mobility must therefore be controlled by different molecular mechanisms. (J. Clin. Invest. 1994. 94:683-688.) Key words: erythrocyte membrane * hereditary spherocytosis -hereditary pyropoikilocytosis fluorescence photobleaching recovery polarized fluorescence depletion

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“…Cherry et al [33] observed that the removal of spectrin and actin from the erythrocyte membrane resulted in little or no enhancement of Band 3 rotational mobility, a finding that has been verified since [4,34]. Therefore, these cytoskeletal proteins do not restrict the rotation of Band 3.…”

Section: The Link Between the Cytoplasmic And The Membrane Domains Ismentioning

confidence: 94%

Band 3 protein: Structure, flexibility and function

Wang

1994

FEBS Letters

102

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The electroneutral exchange of chloride and bicarbonate across the human erythrocyte membrane is facilitated by Band 3, a 911 amino acid glycoprotein. The 43 kDa amino-terminal cytosolic domain binds the cytoskeleton, haemoglobin and glycolytic enzymes. The 52 kDa carboxylterminal membrane domain mediates anion transport. The protein is a functional dimer, in which the two subunits probably interact with one another by an allosteric mechanism. It is proposed that the link between the mobile cytoplasmic and the membrane-spanning domains of the protein is flexible, based on recent biochemical, biophysical and structural data. This explains the long-standing puzzle that attachment to the cytoskeletal spectrin and actin does not appear to restrict the rotational movement of the Band 3 protein in the erythrocyte membrane. In the Band 3 isoform from the Southeast Asian Ovalocytes (SAO) this link is altered, resulting a tighter attachment of the cytoskeleton to the plasma membrane and a more rigid red blood cell.

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Both ankyrin and band 4.1 are required to restrict the rotational mobility of band 3 in the human erythrocyte membrane

Cited by 18 publications

References 17 publications

Proconvertase proteolytic processing of an enzymatically active myeloperoxidase precursor

Proconvertase proteolytic processing of an enzymatically active myeloperoxidase precursor

Differential control of band 3 lateral and rotational mobility in intact red cells.

Band 3 protein: Structure, flexibility and function

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