The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell |
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Authors: | G Walker W G Kerrick L Y Bourguignon |
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Institution: | Department of Anatomy and Cell Biology, University of Miami, Florida 33101. |
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Abstract: | Several complementary techniques, including immunocytochemical and immunobiochemical analyses, two-dimensional gel electrophoresis, and peptide mapping, were used in this study to examine the involvement of caldesmon in lymphocyte receptor capping. We have found a lymphoma 140-kDa polypeptide that is structurally similar to muscle caldesmon, suggesting that this polypeptide may be a lymphoma caldesmon. When lymphoma 140-kDa polypeptide is extracted from permeabilized cells using 25 mM MgCl2, capping is inhibited. Adding the 140-kDa protein or gizzard caldesmon back to the extracted cells restores their ability to cap. These findings suggest that actin-linked regulatory proteins such as caldesmon may be critically important to actomyosin-mediated contraction which, in turn, is responsible for collecting receptors into cap structures. |
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