Tyrosine hydroxylase, tryptophan hydroxylase, and the biopterin cofactor in the brains from patients with Alzheimer's disease

1989 ◽  
Vol 1 (1-2) ◽  
pp. 21-21 ◽  
Author(s):  
T. Nagatsu ◽  
R. Iizuka
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tyrosine Hydroxylase ◽  
Tryptophan Hydroxylase

Allelic variation at the A218C tryptophan hydroxylase polymorphism influences agitation and aggression in Alzheimer's disease

2004 ◽  
Vol 363 (3) ◽  
pp. 199-202 ◽  
Author(s):  
David Craig ◽  
Dominic J. Hart ◽  
Robin Carson ◽  
Stephen P. McIlroy ◽  
A.Peter Passmore
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tryptophan Hydroxylase ◽  
Allelic Variation

scholarly journals Circulating Antibodies to IDO/THO Pathway Metabolites in Alzheimer's Disease

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
S. Duleu ◽  
A. Mangas ◽  
F. Sevin ◽  
B. Veyret ◽  
A. Bessede ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Chronic Diseases ◽  
Quinolinic Acid ◽  
Kynurenic Acid ◽  
Tryptophan Hydroxylase ◽  
Elisa Method ◽  
Tryptophan Metabolites ◽  
Circulating Antibodies ◽  
Tryptophan Derivatives

In Alzheimer's disease, indoleamine 2,3-dioxygenase and tryptophan hydroxylase are known to induce an overproduction of neurotoxic compounds, such as quinolinic acid and 3-hydroxykynurenine from the former, and 5-hydroxytryptophol and 5-methoxytryptophol from the latter. Other compounds, such as kynurenic acid, serotonin, and melatonin are produced via the same pathways. An improved ELISA method identified circulating antibodies directed against these compounds, linked to proteins, as previously described for other chronic diseases. This describes how only the A isotype of circulating immunoglobulins recognized a pattern of conjugated tryptophan metabolites in the sera of Alzheimer patients. These data indirectly confirmed the involvement of tryptophan derivatives in the pathogenic processes of Alzheimer's disease. Further studies are required to evaluate the relevance of these antibody patterns in monitoring this disease.

The Combined Effects of Amyloidosis and Serotonin Deficiency by Tryptophan Hydroxylase-2 Knockout Impacts Viability of the APP/PS1 Mouse Model of Alzheimer’s Disease

2021 ◽  
pp. 1-18
Author(s):  
Christian Ulrich von Linstow ◽  
Jonas Waider ◽  
Marianne Skov-Skov Bergh ◽  
Marco Anzalone ◽  
Cecilie Madsen ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tryptophan Hydroxylase ◽  
Presenilin 1 ◽  
Mrna Levels ◽  
Combined Effects ◽  
Tryptophan Hydroxylase 2 ◽  
Model Of Alzheimer’S Disease ◽  
Serotonin Deficiency ◽  
Targeted Inactivation

Background: A decline of brain serotonin (5-HT) is held responsible for the changes in mood that can be observed in Alzheimer’s disease (AD). However, 5-HT’ergic signaling is also suggested to reduce the production of pathogenic amyloid-4β (Aβ). Objective: To investigate the effect of targeted inactivation of tryptophan hydroxylase-2 (Tph2), which is essential for neuronal 5-HT synthesis, on amyloidosis in amyloid precursor protein (APP)swe/presenilin 1 (PS1) ΔE9 transgenic mice. Methods: Triple-transgenic (3xTg) APP/PS1 mice with partial (+/-) or complete Tph2 knockout (–/–) were allowed to survive until 6 months old with APP/PS1, Tph2–/–, and wildtype mice. Survival and weight were recorded. Levels of Aβ 42/40/38, soluble APPα (sAβPPα) and sAβPPβ, and cytokines were analyzed by mesoscale, neurotransmitters by mass spectrometry, and gene expression by quantitative PCR. Tph2, microglia, and Aβ were visualized histologically. Results: Tph2 inactivation in APP/PS1 mice significantly reduced viability, without impacting soluble and insoluble Aβ 42 and Aβ 40 in neocortex and hippocampus, and with only mild changes of soluble Aβ 42/Aβ 40. However, sAβPPα and sAβPPβ in hippocampus and Aβ 38 and Aβ 40 in cerebrospinal fluid were reduced. 3xTg–/–mice were devoid of Tph2 immunopositive fibers and 5-HT. Cytokines were unaffected by genotype, as were neocortical TNF, HTR2a and HTR2b mRNA levels in Tph2–/– mice. Microglia clustered around Aβ plaques regardless of genotype. Conclusion: The results suggest that Tph2 inactivation influences AβPP processing, at least in the hippocampus, although levels of Aβ are unchanged. The reduced viability of 3xTg–/–mice could indicate that 5-HT protects against the seizures that can impact the viability of APP/PS1 mice.

No Association between Tryptophan Hydroxylase Gene Polymorphism and Alzheimer’s Disease

2001 ◽  
Vol 43 (1) ◽  
pp. 1-4 ◽  
Author(s):  
Ying-Chieh Wang ◽  
Shih-Jen Tsai ◽  
Tsung-Yun Liu ◽  
Hsiu-Chih Liu ◽  
Chen-Jee Hong
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Gene Polymorphism ◽  
Tryptophan Hydroxylase ◽  
Hydroxylase Gene

Tyrosine hydroxylase and norepinephrine transporter mRNA expression in the locus coeruleus in Alzheimer’s disease

2000 ◽  
Vol 84 (1-2) ◽  
pp. 135-140 ◽  
Author(s):  
Patricia Szot ◽  
James B Leverenz ◽  
Elaine R Peskind ◽  
Elizabeth Kiyasu ◽  
Kirsten Rohde ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tyrosine Hydroxylase ◽  
Locus Coeruleus ◽  
Mrna Expression ◽  
Norepinephrine Transporter

P4-062 Alleleic variation at the A218C tryptophan hydroxylase polymorphism influences agitation and aggression in Alzheimer's disease

2004 ◽  
Vol 25 ◽  
pp. S491
Author(s):  
David Craig ◽  
Dominic J. Hart ◽  
Robin Carson ◽  
Stephen P. McIlroy ◽  
Peter Passmore
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tryptophan Hydroxylase
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