Membrane-bound phosphotyrosyl-protein phosphatase activity in human erythrocytes. Dephosphorylation of membrane band 3 protein

Clari, Giulio; Brunati, Anna Maria; Moret, V.

doi:10.1016/0006-291x(87)90314-7

Cited by 25 publications

(20 citation statements)

References 16 publications

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“…by guest www.bloodjournal.org From lane 1). We have previously detected PTP activities in both cytosolic and membrane fractions of human erythrocytes 28,29 and found that erythrocyte cytosol, subjected to diethylaminoethylcellulose chromatography followed by Ultragel AcA44 gel filtration (Amersham Pharmacia Biotech, Little Chalfont, United Kingdom), gave rise to 2 elution peaks displaying PTP activity. 28 Preliminary experiments in the present study demonstrated that the first peak of the AcA44 column both immunoreacted with anti-SHP-2 antibody and displayed phosphatase activity toward in vitro 32 P-Y-phosphorylated band 3 (data not shown).…”

Section: Shp-2 Binds To and Dephosphorylates Band 3 277mentioning

confidence: 99%

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Bordin

Brunati²,

Donella‐Deana³

et al. 2002

Blood

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Section: Shp-2 Binds To and Dephosphorylates Band 3 277mentioning

confidence: 99%

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Bordin

Brunati²,

Donella‐Deana³

et al. 2002

Blood

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Section: Detection Of a Type 1b Protein-tyrosine Phosphatase Associatmentioning

confidence: 99%

“…Because erythrocytes are known to be a rich source of these phosphatases (20,21), we assayed extracts of skate erythrocytes for protein-tyrosine phosphatases. Among the proteintyrosine phosphatases, a type 1B has been reported to be closely associated with band 3 in human red blood cells (20). To determine whether a similar association occurs in skate red cells, skate band 3 was immunoprecipitated, and protein-tyrosine phosphatases were detected by probing Western blots of co-immunoprecipitated proteins.…”

Section: Detection Of a Type 1b Protein-tyrosine Phosphatase Associatmentioning

confidence: 99%

Volume Expansion Stimulates p72 and p56 in Skate Erythrocytes

Musch

Hubert

Goldstein

1999

Journal of Biological Chemistry

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Hypotonic volume expansion of skate erythrocytes rapidly stimulates the tyrosine phosphorylation of band 3, the membrane protein thought to mediate the osmotically sensitive taurine efflux. Skate erythrocytes possess numerous tyrosine kinases including p59fyn, p56lyn, pp60 src , and p72 syk , demonstrated by immune complex assays measuring autocatalytic kinase activity. Inclusion of the cytoplasmic domain of band 3 in this assay showed that only Syk and Lyn can directly phosphorylate the cytoplasmic domain of band 3. Upon cell volume expansion, Syk activity was increased as assessed by three different assays (immune complex assay measuring autophosphorylation, assay of the level of phosphotyrosine of the immunoprecipitated kinase, and assay of level of 32 P in the kinase immunoprecipitated from cells prelabeled with 32 PO 4 and then volume-expanded). The tyrosine kinase Lyn was also stimulated by volume expansion, most notably when analyzed by the latter two methods. Volume expansion stimulated a large increase in the ability of Syk to phosphorylate band 3 at times that coincide with the stimulation of taurine flux. The stilbene piceatannol inhibited Syk preferentially over Lyn and other tyrosine kinases and inhibited volume-stimulated taurine efflux in a concentration-dependent manner similar to that for the inhibition of Syk. Two major phosphorylation peaks were detected in tryptic digests of cdb3 separated by reverse phase HPLC. Edman degradation demonstrated a phosphotyrosine in a YXXL motif. In conclusion, p72 syk appears to be a strong candidate as a pivotal signal-transducing step in the volume-activated taurine efflux in skate red cells. The level of band-3 phosphorylation may be regulated, in addition, by a protein-tyrosine phosphatase of the 1B variety.

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“…Human red cells contain several PTPs, cytosolic acid PTP and membrane-associated neutral PTP. 17,18 A neutral PTP, related to PTP1B, was found to be associated with and to dephosphorylate band 3 and to be inhibited by vanadate, diamide, and thiol-alkylating agents. 19,20 The possibility that PTK activity could be regulated by PTP came from studies with PTP inhibitors, such as H 2 O 2 and other oxidants.…”

mentioning

confidence: 99%

Deoxygenation of sickle cells stimulates Syk tyrosine kinase and inhibits a membrane tyrosine phosphatase

Merciris

Hardy‐Dessources

Giraud

2001

Blood

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Polymerization of hemoglobin S in sickle red cells, in deoxygenated conditions, is associated with K loss and cellular dehydration. It was previously reported that deoxygenation of sickle cells increases protein tyrosine kinase (PTK) activity and band 3 tyrosine phosphorylation and that PTK inhibitors reduce cell dehydration. Here, the study investigates which PTKs are involved and the mechanism of their activation. Deoxygenation of sickle cells induced a 2-fold increase in Syk activity, measured by autophosphorylation in immune complex assays, but had no effect on Lyn. Syk was not stimulated by deoxy-genation of normal red cells, and stimulation was partly reversible on reoxygen-ation of sickle cells. Syk activation was independent of the increase in intracellu-lar Ca and Mg 2 associated with deoxy-genation. Lectins that promote glyco-phorin or band 3 aggregation did not activate Syk. In parallel to Syk stimulation , deoxygenation of sickle cells, but not of normal red cells, decreased the activity of both membrane-associated protein tyrosine phosphatase (PTPs) and membrane protein thiol content. In vitro pretreatment of Syk immune complexes with membrane PTP inhibited Syk auto-phosphorylation. It is suggested that Syk activation in vivo could be mediated by PTP inhibition, itself resulting from thiol oxidation, as PTPs are known to be inhibited by oxidants. Altogether these data indicate that Syk could be involved in the mechanisms leading to sickle cell dehydration. (Blood. 2001;98:3121-3127)

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Membrane-bound phosphotyrosyl-protein phosphatase activity in human erythrocytes. Dephosphorylation of membrane band 3 protein

Cited by 25 publications

References 16 publications

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Volume Expansion Stimulates p72 and p56 in Skate Erythrocytes

Deoxygenation of sickle cells stimulates Syk tyrosine kinase and inhibits a membrane tyrosine phosphatase

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