Phenylalanine hydroxylase contributes to serotonin synthesis in mice

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Phenylalanine hydroxylase contributes to serotonin synthesis in mice. / Mordhorst , Alexander ; Dhandapani , Priyavathi ; Matthes , Susann ; Mosienko , Valentina; Rothe , Michael ; Todiras , Mihail ; Self , Julie ; Schunck , Wolf-Hagen ; Schütz , Anja ; Bader, Michael; Alenina, Natalia .

In: FASEB Journal, Vol. 35, No. 6, e21648, 06.2021.

Research output: Contribution to journal › Article › peer-review

Harvard

Mordhorst , A, Dhandapani , P, Matthes , S, Mosienko , V, Rothe , M, Todiras , M, Self , J, Schunck , W-H, Schütz , A, Bader, M & Alenina, N 2021, 'Phenylalanine hydroxylase contributes to serotonin synthesis in mice', FASEB Journal, vol. 35, no. 6, e21648. https://doi.org/10.1096/fj.202100366R

APA

Mordhorst , A., Dhandapani , P., Matthes , S., Mosienko , V., Rothe , M., Todiras , M., Self , J., Schunck , W-H., Schütz , A., Bader, M., & Alenina, N. (2021). Phenylalanine hydroxylase contributes to serotonin synthesis in mice. FASEB Journal, 35(6), [e21648]. https://doi.org/10.1096/fj.202100366R

Vancouver

Mordhorst A, Dhandapani P, Matthes S, Mosienko V, Rothe M, Todiras M et al. Phenylalanine hydroxylase contributes to serotonin synthesis in mice. FASEB Journal. 2021 Jun;35(6). e21648. https://doi.org/10.1096/fj.202100366R

Author

Mordhorst , Alexander ; Dhandapani , Priyavathi ; Matthes , Susann ; Mosienko , Valentina ; Rothe , Michael ; Todiras , Mihail ; Self , Julie ; Schunck , Wolf-Hagen ; Schütz , Anja ; Bader, Michael ; Alenina, Natalia . / Phenylalanine hydroxylase contributes to serotonin synthesis in mice. In: FASEB Journal. 2021 ; Vol. 35, No. 6.

BibTeX

@article{a5d06d1583834a1dbbed50c261ac7e6c,

title = "Phenylalanine hydroxylase contributes to serotonin synthesis in mice",

abstract = "Serotonin is an important signaling molecule in the periphery and in the brain. The hydroxylation of tryptophan is the first and rate-limiting step of its synthesis. In most vertebrates, two enzymes have been described to catalyze this step, tryptophan hydroxylase (TPH) 1 and 2, with expression localized to peripheral and neuronal cells, respectively. However, animals lacking both TPH isoforms still exhibit about 10% of normal serotonin levels in the blood demanding an additional source of the monoamine. In this study, we provide evidence by the gain and loss of function approaches in in vitro and in vivo systems, including stable-isotope tracing in mice, that phenylalanine hydroxylase (PAH) is a third TPH in mammals. PAH contributes to serotonin levels in the blood, and may be important as a local source of serotonin in organs in which no other TPHs are expressed, such as liver and kidney.",

keywords = "phenylalanine hydroxylase, serotonin, tryptophan hydroxylase",

author = "Alexander Mordhorst and Priyavathi Dhandapani and Susann Matthes and Valentina Mosienko and Michael Rothe and Mihail Todiras and Julie Self and Wolf-Hagen Schunck and Anja Sch{\"u}tz and Michael Bader and Natalia Alenina",

note = "Publisher Copyright: {\textcopyright} 2021 The Authors. The FASEB Journal published by Wiley Periodicals LLC on behalf of Federation of American Societies for Experimental Biology.",

year = "2021",

month = jun,

doi = "10.1096/fj.202100366R",

language = "English",

volume = "35",

journal = "FASEB Journal",

issn = "0892-6638",

publisher = "FASEB",

number = "6",

}

RIS

TY - JOUR

T1 - Phenylalanine hydroxylase contributes to serotonin synthesis in mice

AU - Mordhorst , Alexander

AU - Dhandapani , Priyavathi

AU - Matthes , Susann

AU - Mosienko , Valentina

AU - Rothe , Michael

AU - Todiras , Mihail

AU - Self , Julie

AU - Schunck , Wolf-Hagen

AU - Schütz , Anja

AU - Bader, Michael

AU - Alenina, Natalia

PY - 2021/6

Y1 - 2021/6

N2 - Serotonin is an important signaling molecule in the periphery and in the brain. The hydroxylation of tryptophan is the first and rate-limiting step of its synthesis. In most vertebrates, two enzymes have been described to catalyze this step, tryptophan hydroxylase (TPH) 1 and 2, with expression localized to peripheral and neuronal cells, respectively. However, animals lacking both TPH isoforms still exhibit about 10% of normal serotonin levels in the blood demanding an additional source of the monoamine. In this study, we provide evidence by the gain and loss of function approaches in in vitro and in vivo systems, including stable-isotope tracing in mice, that phenylalanine hydroxylase (PAH) is a third TPH in mammals. PAH contributes to serotonin levels in the blood, and may be important as a local source of serotonin in organs in which no other TPHs are expressed, such as liver and kidney.

AB - Serotonin is an important signaling molecule in the periphery and in the brain. The hydroxylation of tryptophan is the first and rate-limiting step of its synthesis. In most vertebrates, two enzymes have been described to catalyze this step, tryptophan hydroxylase (TPH) 1 and 2, with expression localized to peripheral and neuronal cells, respectively. However, animals lacking both TPH isoforms still exhibit about 10% of normal serotonin levels in the blood demanding an additional source of the monoamine. In this study, we provide evidence by the gain and loss of function approaches in in vitro and in vivo systems, including stable-isotope tracing in mice, that phenylalanine hydroxylase (PAH) is a third TPH in mammals. PAH contributes to serotonin levels in the blood, and may be important as a local source of serotonin in organs in which no other TPHs are expressed, such as liver and kidney.

KW - phenylalanine hydroxylase

KW - serotonin

KW - tryptophan hydroxylase

UR - https://faseb.onlinelibrary.wiley.com/doi/full/10.1096/fj.202100366R

UR - http://www.scopus.com/inward/record.url?scp=85106348039&partnerID=8YFLogxK

U2 - 10.1096/fj.202100366R

DO - 10.1096/fj.202100366R

M3 - Article

VL - 35

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 6

M1 - e21648

ER -

ID: 88877779