The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell

G. Walker, W. G.L. Kerrick, L. Y.W. Bourguignon

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)496-500
Number of pages5
JournalJournal of Biological Chemistry
Volume264
Issue number1
StatePublished - 1989

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell'. Together they form a unique fingerprint.

Cite this