U937 cell differentiation: G protein alterations and interaction with the chemotactic peptide receptor

1991 ◽  
Vol 19 (2) ◽  
pp. 98S-98S
Author(s):  
FIONA M. MITCHELL ◽  
GRAEME MILLIGAN
Keyword(s):  
Cell Differentiation ◽  
G Protein ◽  
U937 Cell ◽  
Chemotactic Peptide ◽  
Peptide Receptor ◽  
Protein Alterations

Reconstitution of recombinant N -formyl chemotactic peptide receptor with G protein

1993 ◽  
Vol 53 (4) ◽  
pp. 470-474 ◽  
Author(s):  
Ronda E. Schreiber ◽  
Eric R. Prossnitz ◽  
Richard D. Ye ◽  
Charles G. Cochrane ◽  
Algirdas J. Jesaitis ◽  
...  
Keyword(s):  
G Protein ◽  
Chemotactic Peptide ◽  
Peptide Receptor

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

1989 ◽  
Vol 109 (6) ◽  
pp. 2791-2799 ◽  
Author(s):  
E Särndahl ◽  
M Lindroth ◽  
T Bengtsson ◽  
M Fällman ◽  
J Gustavsson ◽  
...  
Keyword(s):  
G Protein ◽  
Second Messengers ◽  
Human Neutrophils ◽  
Receptor Complex ◽  
Chemotactic Peptide ◽  
Filamentous Actin ◽  
High Concentration ◽  
Intact Cells ◽  
Peptide Receptor ◽  
Receptor Complexes

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.

G Protein Alterations in Hypertension and Aging

Hypertension ◽  
1995 ◽  
Vol 26 (5) ◽  
pp. 725-732 ◽  
Author(s):  
R.D. Feldman ◽  
C.M. Tan ◽  
J. Chorazyczewski
Keyword(s):  
G Protein ◽  
Protein Alterations

Molecular Cloning and Chromosomal Localization of the MouseGpr37Gene Encoding an Orphan G-Protein-Coupled Peptide Receptor Expressed in Brain and Testis

Genomics ◽  
1998 ◽  
Vol 53 (3) ◽  
pp. 315-324 ◽  
Author(s):  
Daniela Marazziti ◽  
Angela Gallo ◽  
Elisabetta Golini ◽  
Rafaele Matteoni ◽  
Glauco P. Tocchini-Valentini,
Keyword(s):  
Molecular Cloning ◽  
G Protein ◽  
Chromosomal Localization ◽  
Peptide Receptor ◽  
G Protein Coupled
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