Involvement of an Inhibitory G-Protein in the Signal Transduction Pathway of Maturation-Inducing Hormone (17α,20β-dihydroxy-4-pregnen-3-one) Action in Rainbow Trout (Oncorhynchus mykiss) Oocytes

1994 ◽  
Vol 166 (2) ◽  
pp. 615-622 ◽  
Author(s):  
Michiyasu Yoshikuni ◽  
Yoshitaka Nagahama
Keyword(s):  
Signal Transduction ◽  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
G Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Inhibitory G Protein

scholarly journals A G-protein alpha subunit from asexual Candida albicans functions in the mating signal transduction pathway of Saccharomyces cerevisiae and is regulated by the a1-alpha 2 repressor.

1992 ◽  
Vol 12 (5) ◽  
pp. 1977-1985 ◽  
Author(s):  
C Sadhu ◽  
D Hoekstra ◽  
M J McEachern ◽  
S I Reed ◽  
J B Hicks
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Candida Albicans ◽  
G Protein ◽  
Signal Transduction Pathway ◽  
Alpha Subunit ◽  
Transduction Pathway ◽  
G Protein Alpha Subunit ◽  
Protein Alpha Subunit ◽  
Null Mutants

We have isolated a gene, designated CAG1, from Candida albicans by using the G-protein alpha-subunit clone SCG1 of Saccharomyces cerevisiae as a probe. Amino acid sequence comparison revealed that CAG1 is more homologous to SCG1 than to any other G protein reported so far. Homology between CAG1 and SCG1 not only includes the conserved guanine nucleotide binding domains but also spans the normally variable regions which are thought to be involved in interaction with the components of the specific signal transduction pathway. Furthermore, CAG1 contains a central domain, previously found only in SCG1. cag1 null mutants of C. albicans created by gene disruption produced no readily detectable phenotype. The C. albicans CAG1 gene complemented both the growth and mating defects of S. cerevisiae scg1 null mutants when carried on either a low- or high-copy-number plasmid. In diploid C. albicans, the CAG1 transcript was readily detectable in mycelial and yeast cells of both the white and opaque forms. However, the CAG1-specific transcript in S. cerevisiae transformants containing the C. albicans CAG1 gene was observed only in haploid cells. This transcription pattern matches that of SCG1 in S. cerevisiae and is caused by a1-alpha 2 mediated repression in diploid cells. That is, CAG1 behaves as a haploid-specific gene in S. cerevisiae, subject to control by the a1-alpha 2 mating-type regulation pathway. We infer from these results that C. albicans may have a signal transduction system analogous to that controlling mating type in S. cerevisiae or possibly even a sexual pathway that has so far remained undetected.

A new putative G-protein coupled receptor gene associated with the immune system of rainbow trout (Oncorhynchus mykiss)

2003 ◽  
Vol 15 (2) ◽  
pp. 117-127 ◽  
Author(s):  
Ikunari Kiryu ◽  
Bernd Köllner ◽  
Akashi Kuroda ◽  
Mitsuru Ototake ◽  
Johannes Martinus Dijkstra
Keyword(s):  
Immune System ◽  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
G Protein ◽  
Receptor Gene ◽  
G Protein Coupled Receptor ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
G Protein Coupled

NO inhibits signal transduction pathway for ATP release from erythrocytes via its action on heterotrimeric G protein Gi

2004 ◽  
Vol 287 (2) ◽  
pp. H748-H754 ◽  
Author(s):  
Jeffrey J. Olearczyk ◽  
Alan H. Stephenson ◽  
Andrew J. Lonigro ◽  
Randy S. Sprague
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
Atp Release ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Heterotrimeric G Protein

Heterotrimeric G protein Giis involved in a signal transduction pathway for ATP release from erythrocytes

2004 ◽  
Vol 286 (3) ◽  
pp. H940-H945 ◽  
Author(s):  
Jeffrey J. Olearczyk ◽  
Alan H. Stephenson ◽  
Andrew J. Lonigro ◽  
Randy S. Sprague
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
G Proteins ◽  
Pertussis Toxin ◽  
Atp Release ◽  
Signal Transduction Pathway ◽  
Protein G ◽  
Transduction Pathway ◽  
Heterotrimeric G Proteins ◽  
Heterotrimeric G Protein

Erythrocytes are reported to release ATP in response to mechanical deformation and decreased oxygen tension. Previously we proposed that receptor-mediated activation of the heterotrimeric G protein Gsresulted in ATP release from erythrocytes. Here we investigate the hypothesis that activation of heterotrimeric G proteins of the Gisubtype are also involved in a signal transduction pathway for ATP release from rabbit erythrocytes. Heterotrimeric G proteins Gαi1, Gαi2, and Gαi3but not Gαowere identified in rabbit and human erythrocyte membranes. Pretreatment of rabbit erythrocytes with pertussis toxin (100 ng/ml, 2 h), which uncouples Gi/ofrom their effector proteins, inhibited deformation-induced ATP release. Incubation of rabbit and human erythrocytes with mastoparan (Mas, 10 μM) or Mas-7 (1 μM), which are compounds that directly activate Giproteins, resulted in ATP release. However, rabbit erythrocytes did not release ATP when incubated with Mas-17 (10 μM), which is an inactive Mas analog. In separate experiments, Mas (10 μM) but not Mas-17 (10 μM) increased intracellular concentrations of cAMP when incubated with rabbit erythrocytes. Importantly, Mas-induced ATP release from rabbit erythrocytes was inhibited after treatment with pertussis toxin (100 ng/ml, 2 h). These data are consistent with the hypothesis that the heterotrimeric G protein Giis a component of a signal transduction pathway for ATP release from erythrocytes.

Sign in / Sign up

Export Citation Format

Share Document