Enhanced tyrosine phosphorylation in B lymphocytes upon complexing of membrane immunoglobulin

Andre E. Nel; Gary E. Landreth; Pascal J. Goldschmidt-Clermont; H. Edward Tung; Robert M. Galbraith

doi:10.1016/0006-291X(84)91362-7

Enhanced tyrosine phosphorylation in B lymphocytes upon complexing of membrane immunoglobulin

Andre E. Nel, Gary E. Landreth, Pascal J. Goldschmidt-Clermont, H. Edward Tung, Robert M. Galbraith

Medicine

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

14 Scopus citations

Abstract

Activation of normal human perioheral blood B-enriched lymphocytes with antiserum reacting with membrane immunoglobulin was associated with increased phosphorylation of ceilular proteins, particularly in the Triton-insoluble cytoskelutal fraction. At least two proteins (56K and 60K) were labeled predominantly at tyrosine residues. These findings may indicate another specialized membrane structure which upon specific ligand binding stimulates tyrosine phosphorylation in association with cellular proliferation.

Original language	English (US)
Pages (from-to)	859-866
Number of pages	8
Journal	Biochemical and biophysical research communications
Volume	125
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(84)91362-7
State	Published - Dec 28 1984

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Enhanced tyrosine phosphorylation in B lymphocytes upon complexing of membrane immunoglobulin",

abstract = "Activation of normal human perioheral blood B-enriched lymphocytes with antiserum reacting with membrane immunoglobulin was associated with increased phosphorylation of ceilular proteins, particularly in the Triton-insoluble cytoskelutal fraction. At least two proteins (56K and 60K) were labeled predominantly at tyrosine residues. These findings may indicate another specialized membrane structure which upon specific ligand binding stimulates tyrosine phosphorylation in association with cellular proliferation.",

author = "Nel, {Andre E.} and Landreth, {Gary E.} and Goldschmidt-Clermont, {Pascal J.} and Tung, {H. Edward} and Galbraith, {Robert M.}",

note = "Funding Information: Publioatioll Immunology Cirrol ina. Grant BNS SC Institutronal Kesearc:h supported University Number 000 and MIcrobiology, Research supported 81-10452, Labcatal Award CR17. Career DeveIopment by a Clinical of South from the Depnrtmellr Mzdioal University in part by N1H Grant Laboratories, Paris, R.M.C. the reciprerlt Award and A.E.N. Postdoctoral from Carolina.",

year = "1984",

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doi = "10.1016/0006-291X(84)91362-7",

language = "English (US)",

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pages = "859--866",

journal = "Biochemical and Biophysical Research Communications",

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T1 - Enhanced tyrosine phosphorylation in B lymphocytes upon complexing of membrane immunoglobulin

AU - Nel, Andre E.

AU - Landreth, Gary E.

AU - Goldschmidt-Clermont, Pascal J.

AU - Tung, H. Edward

AU - Galbraith, Robert M.

N1 - Funding Information: Publioatioll Immunology Cirrol ina. Grant BNS SC Institutronal Kesearc:h supported University Number 000 and MIcrobiology, Research supported 81-10452, Labcatal Award CR17. Career DeveIopment by a Clinical of South from the Depnrtmellr Mzdioal University in part by N1H Grant Laboratories, Paris, R.M.C. the reciprerlt Award and A.E.N. Postdoctoral from Carolina.

PY - 1984/12/28

Y1 - 1984/12/28

N2 - Activation of normal human perioheral blood B-enriched lymphocytes with antiserum reacting with membrane immunoglobulin was associated with increased phosphorylation of ceilular proteins, particularly in the Triton-insoluble cytoskelutal fraction. At least two proteins (56K and 60K) were labeled predominantly at tyrosine residues. These findings may indicate another specialized membrane structure which upon specific ligand binding stimulates tyrosine phosphorylation in association with cellular proliferation.

AB - Activation of normal human perioheral blood B-enriched lymphocytes with antiserum reacting with membrane immunoglobulin was associated with increased phosphorylation of ceilular proteins, particularly in the Triton-insoluble cytoskelutal fraction. At least two proteins (56K and 60K) were labeled predominantly at tyrosine residues. These findings may indicate another specialized membrane structure which upon specific ligand binding stimulates tyrosine phosphorylation in association with cellular proliferation.

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