scholarly journals The structure of brain-specific rat aldolase C mRNA and the evolution of aldolase isozyme genes

1988 ◽  
Vol 171 (3) ◽  
pp. 471-478 ◽  
Author(s):  
Akiko KUKITA ◽  
Tsunehiro MUKAI ◽  
Takashi MIYATA ◽  
Katsuji HORI
Keyword(s):  
Aldolase C

Aldolase C/Zebrin II is Released to the Extracellular Space after Stroke and Inhibits the Network Activity of Cortical Neurons

2006 ◽  
Vol 31 (11) ◽  
pp. 1297-1303 ◽  
Author(s):  
Stephanie Linke ◽  
Philipp Goertz ◽  
Stephan L. Baader ◽  
Volkmar Gieselmann ◽  
Mario Siebler ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Extracellular Space ◽  
Network Activity ◽  
Aldolase C ◽  
Zebrin Ii

Purification of Aldolase C from Rat Brain and Hepatoma

1977 ◽  
Vol 77 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Antoinette HATZFELD ◽  
Jacques ELION ◽  
Francois MENNECIER ◽  
Fanny SCHAPIRA
Keyword(s):  
Rat Brain ◽  
Aldolase C

scholarly journals Bidirectional activity and orientation-dependent specificity of the rat aldolase C promoter in transgenic mice

FEBS Letters ◽  
2001 ◽  
Vol 499 (1-2) ◽  
pp. 143-146 ◽  
Author(s):  
Françoise Phan Dinh Tuy ◽  
Arlette Porteu ◽  
Axel Kahn ◽  
Henriette Skala
Keyword(s):  
Transgenic Mice ◽  
Aldolase C

On the ubiquity of aldolase C in ruminant tissues

1969 ◽  
Vol 178 (3) ◽  
pp. 623-625 ◽  
Author(s):  
R.J. Sheedy ◽  
C.J. Masters
Keyword(s):  
Aldolase C

scholarly journals Histidine to aspartate phosphotransferase activity of nm23 proteins: phosphorylation of aldolase C on Asp-319

2000 ◽  
Vol 346 (3) ◽  
pp. 623-630 ◽  
Author(s):  
Paul D. WAGNER ◽  
Ngoc-Diep VU
Keyword(s):  
Cell Motility ◽  
Bovine Brain ◽  
Transferase Activity ◽  
Atp Citrate Lyase ◽  
Histidine Residues ◽  
Aldolase C ◽  
Tumour Metastasis ◽  
Citrate Lyase ◽  
Equivalent Residue ◽  
Biochemical Mechanisms

nm23 genes have been implicated in the suppression of tumour metastasis and cell motility; however, the biochemical mechanisms for these suppressions are not known. We have previously described the transfer of phosphate from the catalytic histidine residues of nm23 proteins to an aspartic or a glutamic residue on one or more 43 kDa proteins in detergent extracts of bovine brain membranes. To gain a better understanding of this transferase activity, we partly purified this 43 kDa protein and identified aldolases A and C as the major 43 kDa proteins present in the preparation. Aldolase was purified from brain cytosol; its phosphorylation by rat liver nm23 proteins and by recombinant human nm23-H1 was examined. The site of phosphorylation was identified as Asp-319 on aldolase C. The equivalent residue on aldolase A, a glutamic residue, was not phosphorylated. Aldolase C was rapidly phosphorylated by wild-type nm23-H1 but was not phosphorylated, or was phosphorylated very slowly, by either nm23-H1P96S or nm23-H1S120G, mutants of nm23-H1 that do not suppress cell motility. This is the first identification of a protein that is phosphorylated on an aspartic residue by nm23 proteins. The sequence around Asp-319 of aldolase C has some similarities to those around the histidine residues on ATP-citrate lyase and succinic thiokinase that are phosphorylated by nm23 proteins.

scholarly journals New Proteins Found Interacting with Brain Metallothionein-3 Are Linked to Secretion

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Issam El Ghazi ◽  
Bruce L. Martin ◽  
Ian M. Armitage
Keyword(s):  
Immunoaffinity Chromatography ◽  
Glycolytic Metabolism ◽  
Interacting Protein ◽  
Aldolase C ◽  
Growth Inhibitory Factor ◽  
Protein Partners ◽  
Growth Inhibitory ◽  
Proposed Model ◽  
The Brain ◽  
Partner Proteins

Metallothionein 3 (MT-3), also known as growth inhibitory factor (GIF), exhibits a neuroinhibitory activity. Our lab and others have previously shown that this biological activity involves interacting protein partners in the brain. However, nothing specific is yet known about which of these interactions is responsible for the GIF activity. In this paper, we are reporting upon new proteins found interacting with MT-3 as determined through immunoaffinity chromatography and mass spectrometry. These new partner proteins—Exo84p, 14-3-3 Zeta,αandβEnolase, Aldolase C, Malate dehydrogenase, ATP synthase, and Pyruvate kinase—along with those previously identified have now been classified into three functional groups: transport and signaling, chaperoning and scaffolding, and glycolytic metabolism. When viewed together, these interactions support a proposed model for the regulation of the GIF activity of MT-3.

Monoclonal Anti-Human Aldolase C Antibodies That React to the Isozyme Group-Specific Sequences and Generally Conserved Sequences of Human Aldolase C

1996 ◽  
Vol 119 (2) ◽  
pp. 281-290
Author(s):  
R. Kaihara ◽  
S. Matsuhashi ◽  
T. Kusakabe ◽  
T. Kondo ◽  
A. Iwanaga ◽  
...  
Keyword(s):  
Conserved Sequences ◽  
Aldolase C ◽  
Specific Sequences

Antineuronal Antibodies in Obsessive-compulsive Disorder: Comparisons in Children with OCD-only, OCD + Chronic tics and OCD + PANDAS

2009 ◽  
Vol 24 (S1) ◽  
pp. 1-1 ◽  
Author(s):  
H. Singer ◽  
C. Gause ◽  
M. Grados
Keyword(s):  
Pyruvate Kinase ◽  
Obsessive Compulsive Disorder ◽  
Competitive Inhibition ◽  
Detection Methods ◽  
Cingulate Gyrus ◽  
Obsessive Compulsive ◽  
Western Immunoblotting ◽  
Antineuronal Antibodies ◽  
Compulsive Disorder ◽  
Aldolase C

We will present a comparison of serum antineuronal antibody profiles in children with OCD-only (n=13), PANDAS + OCD (n=20), CTD + OCD (n=23), and age-matched controls (n=29). Detection methods used to evaluate anti-brain antibodies included immunohistochemistry (striatum), ELISA (BA 9/10, BA 11, caudate, and cingulate gyrus), and Western immunoblotting (BA 9/10, BA 11, caudate, and cingulate gyrus).Immunublotting was further used to assess the presence and concentration of putative antigens identified in post-streptococcal patients, i.e., *- and *-enolase, aldolase C, pyruvate kinase M1 and tubulin. Anti-lysoganglioside GM1 activity was measured by competitive inhibition.

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