Changes of GTP binding proteins, not neurofilament-associated proteins, in the brain of the neurofilament-deficient quail, "Quiver".
A neurofilament (NF)-deficient mutant of the Japanese quail was named "Quiver", as it showed generalized quivering as a clinical sign. NF consists of three major subunits; low, middle and high. We previously reported that the noradrenaline and 5-hydroxytryptamine content in the neostriatum of the Quiver's brain was different from that in the normal quail, although disappearance of the three NF proteins occurred in all areas of the Quiver's brain. Thus, NF-related proteins may show considerable changes in the specific sites of Quiver's brain. In this study, an examination was made of the changes in NF-related proteins in the Quiver, by immunoblotting analysis. The amounts of cyclin-dependent kinase 5 (cdk5), which phosphorylates NF proteins, and tau which is a substrate of cdk5, in the neostriatum of the Quiver, were essentially the same as those in the normal quail, although NF proteins could not be detected in the Quiver. The amount of alpha-tubulin in the Quiver's brain was similar to that in the normal quail. Next, we investigated the changes of GTP binding (G) proteins in the Quiver's brain, because cytoskeletal components such as tubulin and F-actin bind with G proteins. [32P]ADP-ribosylation of G proteins (Gs by cholera toxin and Gi/G0 by pertussis toxin) in the neostriatum of the Quiver increased significantly, although alpha subunits of G proteins showed no change by immunoblotting analysis. The ratios of the trimer form in G proteins thus appear to increase more in the NF-deficient Quiver brain than in the brain of the normal quail. The G proteins-mediated adenylate cyclase activities were the same in the brain of both the Quiver and the normal quail. Possible interactions between NFs and G proteins are discussed.
Hasegawa
H
H
Department of Pharmacology, Hokkaido University, Sapporo, Japan.
Murayama
T
T
Takahashi
A
A
Itakura
C
C
Nomura
Y
Y
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D037361:Adenylate Cyclase Toxin; D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D001923:Brain Chemistry / Q000187:drug effects / Q000502:physiology*; D002772:Cholera Toxin / Q000494:pharmacology; D003370:Coturnix; D019204:GTP-Binding Proteins / Q000378:metabolism*; D015151:Immunoblotting; D009154:Mutation; D009422:Nervous System Diseases / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism*; D016900:Neurofilament Proteins / Q000172:deficiency* / Q000378:metabolism*; D037342:Pertussis Toxin; D011784:Quail / Q000378:metabolism*; D010566:Virulence Factors, Bordetella / Q000494:pharmacology
D037361:Adenylate Cyclase Toxin; D016900:Neurofilament Proteins; D010566:Virulence Factors, Bordetella; D000246:Adenosine Diphosphate Ribose; D002772:Cholera Toxin; D037342:Pertussis Toxin; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases