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

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

Research output: Contribution to journalArticle

23 Citations (Scopus)

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
Pages (from-to)496-500
Number of pages5
JournalJournal of Biological Chemistry
Volume264
Issue number1
StatePublished - Jan 1 1989

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Receptor Aggregation
Calmodulin-Binding Proteins
T-Cell Lymphoma
Lymphoma
Peptides
Actomyosin
Magnesium Chloride
Peptide Mapping
Lymphocytes
Electrophoresis, Gel, Two-Dimensional
Electrophoresis
Muscle
Actins
Proteins
Gels
Muscles

ASJC Scopus subject areas

  • Biochemistry

Cite this

The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell. / Walker, G.; Kerrick, W. Glenn; Bourguignon, L. Y W.

In: Journal of Biological Chemistry, Vol. 264, No. 1, 01.01.1989, p. 496-500.

Research output: Contribution to journalArticle

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