Development by environment interactions controlling tryptophan hydroxylase expression

Matthew W. Hale, Anantha Shekhar, Christopher A. Lowry

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Tryptophan hydroxylase is the rate-limiting enzyme in the biosynthesis of serotonin (5-hydroxytryptamine; 5-HT). Two isoforms of tryptophan hydroxylase, derived from different genes, tph1 and tph2, have been identified. The tph1 isoform is expressed in peripheral tissues, whereas tph2 is brain and neuron-specific. Recent studies suggest that tph2 expression and brain serotonin turnover are upregulated in depressed suicide patients, and drug-free depressed patients, respectively. Increased tph2 expression could result from genetic influences, early life developmental influences, adverse experience during adulthood, or interactions among these factors. Studies in rodents support the hypothesis that interactions between early life developmental influences and adverse experience during adulthood play an important role in determining tph2 expression. In this review, we highlight the evidence for the effects of adverse early life experience and stressful experience during adulthood on both tph1 and tph2 expression.

Original languageEnglish
Pages (from-to)219-226
Number of pages8
JournalJournal of Chemical Neuroanatomy
Volume41
Issue number4
DOIs
StatePublished - Jul 2011

Fingerprint

Tryptophan Hydroxylase
Serotonin
Protein Isoforms
Life Change Events
Brain
Suicide
Rodentia
Neurons
Enzymes
Pharmaceutical Preparations
Genes

Keywords

  • Dorsal raphe nucleus
  • Serotonin
  • Tph1
  • Tph2
  • Tryptophan hydroxylase

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience

Cite this

Development by environment interactions controlling tryptophan hydroxylase expression. / Hale, Matthew W.; Shekhar, Anantha; Lowry, Christopher A.

In: Journal of Chemical Neuroanatomy, Vol. 41, No. 4, 07.2011, p. 219-226.

Research output: Contribution to journalArticle

@article{3a39e5e43a334e14b96b5255dd829515,
title = "Development by environment interactions controlling tryptophan hydroxylase expression",
abstract = "Tryptophan hydroxylase is the rate-limiting enzyme in the biosynthesis of serotonin (5-hydroxytryptamine; 5-HT). Two isoforms of tryptophan hydroxylase, derived from different genes, tph1 and tph2, have been identified. The tph1 isoform is expressed in peripheral tissues, whereas tph2 is brain and neuron-specific. Recent studies suggest that tph2 expression and brain serotonin turnover are upregulated in depressed suicide patients, and drug-free depressed patients, respectively. Increased tph2 expression could result from genetic influences, early life developmental influences, adverse experience during adulthood, or interactions among these factors. Studies in rodents support the hypothesis that interactions between early life developmental influences and adverse experience during adulthood play an important role in determining tph2 expression. In this review, we highlight the evidence for the effects of adverse early life experience and stressful experience during adulthood on both tph1 and tph2 expression.",
keywords = "Dorsal raphe nucleus, Serotonin, Tph1, Tph2, Tryptophan hydroxylase",
author = "Hale, {Matthew W.} and Anantha Shekhar and Lowry, {Christopher A.}",
year = "2011",
month = "7",
doi = "10.1016/j.jchemneu.2011.05.002",
language = "English",
volume = "41",
pages = "219--226",
journal = "Journal of Chemical Neuroanatomy",
issn = "0891-0618",
publisher = "Elsevier",
number = "4",

}

TY - JOUR

T1 - Development by environment interactions controlling tryptophan hydroxylase expression

AU - Hale, Matthew W.

AU - Shekhar, Anantha

AU - Lowry, Christopher A.

PY - 2011/7

Y1 - 2011/7

N2 - Tryptophan hydroxylase is the rate-limiting enzyme in the biosynthesis of serotonin (5-hydroxytryptamine; 5-HT). Two isoforms of tryptophan hydroxylase, derived from different genes, tph1 and tph2, have been identified. The tph1 isoform is expressed in peripheral tissues, whereas tph2 is brain and neuron-specific. Recent studies suggest that tph2 expression and brain serotonin turnover are upregulated in depressed suicide patients, and drug-free depressed patients, respectively. Increased tph2 expression could result from genetic influences, early life developmental influences, adverse experience during adulthood, or interactions among these factors. Studies in rodents support the hypothesis that interactions between early life developmental influences and adverse experience during adulthood play an important role in determining tph2 expression. In this review, we highlight the evidence for the effects of adverse early life experience and stressful experience during adulthood on both tph1 and tph2 expression.

AB - Tryptophan hydroxylase is the rate-limiting enzyme in the biosynthesis of serotonin (5-hydroxytryptamine; 5-HT). Two isoforms of tryptophan hydroxylase, derived from different genes, tph1 and tph2, have been identified. The tph1 isoform is expressed in peripheral tissues, whereas tph2 is brain and neuron-specific. Recent studies suggest that tph2 expression and brain serotonin turnover are upregulated in depressed suicide patients, and drug-free depressed patients, respectively. Increased tph2 expression could result from genetic influences, early life developmental influences, adverse experience during adulthood, or interactions among these factors. Studies in rodents support the hypothesis that interactions between early life developmental influences and adverse experience during adulthood play an important role in determining tph2 expression. In this review, we highlight the evidence for the effects of adverse early life experience and stressful experience during adulthood on both tph1 and tph2 expression.

KW - Dorsal raphe nucleus

KW - Serotonin

KW - Tph1

KW - Tph2

KW - Tryptophan hydroxylase

UR - http://www.scopus.com/inward/record.url?scp=79960106666&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79960106666&partnerID=8YFLogxK

U2 - 10.1016/j.jchemneu.2011.05.002

DO - 10.1016/j.jchemneu.2011.05.002

M3 - Article

VL - 41

SP - 219

EP - 226

JO - Journal of Chemical Neuroanatomy

JF - Journal of Chemical Neuroanatomy

SN - 0891-0618

IS - 4

ER -