Association of ligand-receptor complexes with actin filaments in human neutrophils: a possible regulatory role for a G-protein - PubMed (original) (raw)

Association of ligand-receptor complexes with actin filaments in human neutrophils: a possible regulatory role for a G-protein

E Särndahl et al. J Cell Biol. 1989 Dec.

Abstract

Most ligand-receptor interactions result in an immediate generation of various second messengers and a subsequent association of the ligand-receptor complex to the cytoskeleton. Depending on the receptor involved, this linkage to the cytoskeleton has been suggested to play a role in the termination of second messenger generation and/or the endocytic process whereby the ligand-receptor complex is internalized. We have studied how the binding of chemotactic peptide-receptor complexes to the cytoskeleton of human neutrophils is accomplished. As much as 76% of the tritiated formylmethionyl-leucyl-phenylalanine (fMet-Leu-[3H]Phe) specifically bound to intact cells, obtained by a 30-s stimulation with 20 nM fMet-Leu-[3H]Phe, still remained after Triton X-100 extraction. Preincubating intact cells with dihydrocytochalasin B (dhCB) or washing the cytoskeletal preparation with a high concentration of potassium, reduced the binding of ligand-receptor complexes to the cytoskeleton by 46% or more. Inhibition of fMet-Leu-Phe-induced generation of second messengers by ADP-ribosylating the alpha-subunit of the receptor-coupled G-protein with pertussis toxin, did not reduce the binding of ligand-receptor complexes to the cytoskeleton. However, using guanosine-5'-O-(2-thiodiphosphate) (GDP beta S) to prevent the dissociation of the fMet-Leu-Phe-associated G-protein within electrically permeabilized cells, led to a pronounced reduction (62%) of the binding between ligand-receptor complexes and the cytoskeleton. In summary, in human neutrophils the rapid association between chemotactic peptide-receptor complexes and the cytoskeleton is dependent on filamentous actin. This association is most likely regulated by the activation and dissociation of the fMet-Leu-Phe-associated G-protein.

PubMed Disclaimer

Cited by

Down-regulation of receptor antigen in leukotriene B4-induced chemotactic deactivation of human polymorphonuclear leucocytes.
Boggs JM, Koo CH, Goetzl EJ. Boggs JM, et al. Immunology. 1991 Jun;73(2):212-6. Immunology. 1991. PMID: 1649125 Free PMC article.
Tumor cell adhesion to the extracellular matrix and signal transduction mechanisms implicated in tumor cell motility, invasion and metastasis.
Lester BR, McCarthy JB. Lester BR, et al. Cancer Metastasis Rev. 1992 Mar;11(1):31-44. doi: 10.1007/BF00047601. Cancer Metastasis Rev. 1992. PMID: 1511495 Review.
The cytoskeleton and its importance as a mediator of inflammation.
Rogers KR, Morris CJ, Blake DR. Rogers KR, et al. Ann Rheum Dis. 1992 Apr;51(4):565-71. doi: 10.1136/ard.51.4.565. Ann Rheum Dis. 1992. PMID: 1586265 Free PMC article. Review. No abstract available.
Activation of phospholipase D is an early event in integrin-mediated signalling leading to phagocytosis in human neutrophils.
Serrander L, Fällman M, Stendahl O. Serrander L, et al. Inflammation. 1996 Aug;20(4):439-50. doi: 10.1007/BF01486745. Inflammation. 1996. PMID: 8872506
Glycoprotein IIb-IIIa and the translocation of Rap2B to the platelet cytoskeleton.
Torti M, Ramaschi G, Sinigaglia F, Lapetina EG, Balduini C. Torti M, et al. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4239-43. doi: 10.1073/pnas.91.10.4239. Proc Natl Acad Sci U S A. 1994. PMID: 8183895 Free PMC article.

References

1. J Biol Chem. 1979 Oct 10;254(19):9829-34 - PubMed
1. J Cell Biol. 1987 Sep;105(3):1395-404 - PubMed
1. J Cell Biol. 1987 Oct;105(4):1473-8 - PubMed
1. J Histochem Cytochem. 1987 Dec;35(12):1381-8 - PubMed
1. J Cell Biol. 1987 Dec;105(6 Pt 2):2959-71 - PubMed

Association of ligand-receptor complexes with actin filaments in human neutrophils: a possible regulatory role for a G-protein - PubMed (original) (raw)