Phosphate metabolite regulation of spectrin interactions

Michael P. Sheetz; Joseph Casaly

doi:10.3109/00365518109097443

Phosphate metabolite regulation of spectrin interactions

Michael P. Sheetz
, Joseph Casaly

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

The deformability of the erythrocyte membrane is believed to depend upon component interactions in the spectrin, actin and band 4.1 complex. Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1. This dissociation by 2,3 DPG is highly pH dependent but does not involve divalent cations, 2,3 DPG hydrolysis or spectrin dephos-phorylation. In intact erythrocytes the concentrations of 2,3 DPG and the lipid, triphosphatidyl inositol, are sufficient to cause increased labilization in the spectrin, actin and band 4.1 network.

Original language	English (US)
Pages (from-to)	117-122
Number of pages	6
Journal	Scandinavian Journal of Clinical and Laboratory Investigation
Volume	41
Issue number	S156
DOIs	https://doi.org/10.3109/00365518109097443
State	Published - 1981
Externally published	Yes

Keywords

Erythrocyte membrane
Phosphorylation
Spectrin

ASJC Scopus subject areas

Clinical Biochemistry

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10.3109/00365518109097443

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title = "Phosphate metabolite regulation of spectrin interactions",

abstract = "The deformability of the erythrocyte membrane is believed to depend upon component interactions in the spectrin, actin and band 4.1 complex. Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1. This dissociation by 2,3 DPG is highly pH dependent but does not involve divalent cations, 2,3 DPG hydrolysis or spectrin dephos-phorylation. In intact erythrocytes the concentrations of 2,3 DPG and the lipid, triphosphatidyl inositol, are sufficient to cause increased labilization in the spectrin, actin and band 4.1 network.",

keywords = "Erythrocyte membrane, Phosphorylation, Spectrin",

author = "Sheetz, \{Michael P.\} and Joseph Casaly",

note = "Funding Information: We would like to thank P. Cosgrove and D. Koppel for their helpful comments on the manuscript. This research was supported in part by a grant from NIH (HL-23359).",

year = "1981",

doi = "10.3109/00365518109097443",

language = "English (US)",

volume = "41",

pages = "117--122",

journal = "Scandinavian Journal of Clinical and Laboratory Investigation",

issn = "0036-5513",

publisher = "Taylor and Francis Ltd.",

number = "S156",

}

TY - JOUR

T1 - Phosphate metabolite regulation of spectrin interactions

AU - Sheetz, Michael P.

AU - Casaly, Joseph

N1 - Funding Information: We would like to thank P. Cosgrove and D. Koppel for their helpful comments on the manuscript. This research was supported in part by a grant from NIH (HL-23359).

PY - 1981

Y1 - 1981

N2 - The deformability of the erythrocyte membrane is believed to depend upon component interactions in the spectrin, actin and band 4.1 complex. Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1. This dissociation by 2,3 DPG is highly pH dependent but does not involve divalent cations, 2,3 DPG hydrolysis or spectrin dephos-phorylation. In intact erythrocytes the concentrations of 2,3 DPG and the lipid, triphosphatidyl inositol, are sufficient to cause increased labilization in the spectrin, actin and band 4.1 network.

AB - The deformability of the erythrocyte membrane is believed to depend upon component interactions in the spectrin, actin and band 4.1 complex. Phosphate metabolites, such as 2,3-diphosphoglycerate (2,3 DPG) will dissociate spectrin from actin and band 4.1. This dissociation by 2,3 DPG is highly pH dependent but does not involve divalent cations, 2,3 DPG hydrolysis or spectrin dephos-phorylation. In intact erythrocytes the concentrations of 2,3 DPG and the lipid, triphosphatidyl inositol, are sufficient to cause increased labilization in the spectrin, actin and band 4.1 network.

KW - Erythrocyte membrane

KW - Phosphorylation

KW - Spectrin

UR - https://www.scopus.com/pages/publications/0019738508

UR - https://www.scopus.com/pages/publications/0019738508#tab=citedBy

U2 - 10.3109/00365518109097443

DO - 10.3109/00365518109097443

M3 - Article

C2 - 6948372

AN - SCOPUS:0019738508

SN - 0036-5513

VL - 41

SP - 117

EP - 122

JO - Scandinavian Journal of Clinical and Laboratory Investigation

JF - Scandinavian Journal of Clinical and Laboratory Investigation

IS - S156

ER -

Phosphate metabolite regulation of spectrin interactions

Abstract

Keywords

ASJC Scopus subject areas

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