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Membrane immunoglobulin: Anti-immunoglobulin interactions mediate the phosphorylation of actin associated proteins in the B-lymphocyte

Authors
Journal
Life Sciences
0024-3205
Publisher
Elsevier
Publication Date
Volume
42
Issue
5
Identifiers
DOI: 10.1016/0024-3205(88)90089-6
Disciplines
  • Biology

Abstract

Abstract The binding of membrane immunoglobulin (mIg) by anti-Ig anti-bodies is known to initiate a mitogenic signal in B lymphocytes. Because in many instances growth control appears to be correlated with phosphokinase activity, as well as with alterations in cytoskeletal architecture, we asked the question whether anti-bodies binding to mIg would also lead to the specific phosphorylation of lymphocyte actin-associated proteins. Utilizing a myosin affinity technique, we directly examined phosphoproteins that were associated with actin in the chicken B cell. We found that in a few instances the level of phosphorylation was indeed modulated by mIg:anti-Ig interactions. These actin-binding phosphoproteins may be important control elements in the lymphocyte cytoskeleton.

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