Interaction between actomyosin complexes and Fc receptors on human peripheral mononuclear blood cells

F. Uher, Ágnes Jancsó, M. Sándor, Katalin Pintér, E. N A Biró, J. Gergely

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The soluble FcRI shed from HPMBC following 4-37°C temperature shift interacts with AM, A-HMM and A-S1, respectively, but do not bind to A, M, HMM or S1. In contrast to the monovalent soluble FcRI the multivalent A-HMM-FcRI and A-S1-FcRI complexes agglutinate EA cells. Due to the interaction of soluble FcR with muscle proteins an alteration in the binding properties of the receptor was observed. FcRI in soluble form inhibits only the EA rosette formation of FcRI+ HPMBC in contrast to FcRI-A-HMM and FcRI-A-S1 complexes inhibiting the rosette formation of FcRI+ and FcRII+ cells as well. Based on these observations one can suppose that depending on their anchoring to cytoskeletal structures the FcRs possess one or two binding sites.

Original languageEnglish
Pages (from-to)213-217
Number of pages5
JournalImmunology Letters
Volume2
Issue number4
DOIs
Publication statusPublished - 1981

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Rosette Formation
Actomyosin
Fc Receptors
Blood Cells
Muscle Proteins
Binding Sites
Temperature

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

Cite this

Interaction between actomyosin complexes and Fc receptors on human peripheral mononuclear blood cells. / Uher, F.; Jancsó, Ágnes; Sándor, M.; Pintér, Katalin; Biró, E. N A; Gergely, J.

In: Immunology Letters, Vol. 2, No. 4, 1981, p. 213-217.

Research output: Contribution to journalArticle

Uher, F. ; Jancsó, Ágnes ; Sándor, M. ; Pintér, Katalin ; Biró, E. N A ; Gergely, J. / Interaction between actomyosin complexes and Fc receptors on human peripheral mononuclear blood cells. In: Immunology Letters. 1981 ; Vol. 2, No. 4. pp. 213-217.
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AU - Gergely, J.

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