The emerging role of promiscuous 7TM receptors as chemosensors for food intake

Research output: Chapter in Book/Report/Conference proceedingBook chapterResearch

Standard

The emerging role of promiscuous 7TM receptors as chemosensors for food intake. / Wellendorph, Petrine; Johansen, Lars Dan; Bräuner-Osborne, Hans.

Incretins and insulin secretion. ed. / Gerald Litwack. Vol. 84 Amsterdam : Elsevier Editora, 2010. p. 151-184 (Vitamins & hormones, Vol. 84).

Research output: Chapter in Book/Report/Conference proceedingBook chapterResearch

Harvard

Wellendorph, P, Johansen, LD & Bräuner-Osborne, H 2010, The emerging role of promiscuous 7TM receptors as chemosensors for food intake. in G Litwack (ed.), Incretins and insulin secretion. vol. 84, Elsevier Editora, Amsterdam, Vitamins & hormones, vol. 84, pp. 151-184. https://doi.org/10.1016/B978-0-12-381517-0.00005-9

APA

Wellendorph, P., Johansen, L. D., & Bräuner-Osborne, H. (2010). The emerging role of promiscuous 7TM receptors as chemosensors for food intake. In G. Litwack (Ed.), Incretins and insulin secretion (Vol. 84, pp. 151-184). Amsterdam: Elsevier Editora. Vitamins & hormones, Vol.. 84 https://doi.org/10.1016/B978-0-12-381517-0.00005-9

Vancouver

Wellendorph P, Johansen LD, Bräuner-Osborne H. The emerging role of promiscuous 7TM receptors as chemosensors for food intake. In Litwack G, editor, Incretins and insulin secretion. Vol. 84. Amsterdam: Elsevier Editora. 2010. p. 151-184. (Vitamins & hormones, Vol. 84). https://doi.org/10.1016/B978-0-12-381517-0.00005-9

Author

Wellendorph, Petrine ; Johansen, Lars Dan ; Bräuner-Osborne, Hans. / The emerging role of promiscuous 7TM receptors as chemosensors for food intake. Incretins and insulin secretion. editor / Gerald Litwack. Vol. 84 Amsterdam : Elsevier Editora, 2010. pp. 151-184 (Vitamins & hormones, Vol. 84).

Bibtex

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title = "The emerging role of promiscuous 7TM receptors as chemosensors for food intake",
abstract = "In recent years, several highly promiscuous seven transmembrane (7TM) receptors have been cloned and characterized of which many are activated broadly by amino acids, proteolytic degradation products, carbohydrates, or free fatty acids (FFAs) and are expressed in taste tissue, the gastrointestinal (GI) tract, endocrine glands, adipose tissue, and/or kidney. This has led to the hypothesis that these receptors may act as sensors of food intake modulating, for example, release of incretin hormones from the gut, insulin/glucagon from the pancreas, and leptin from adipose tissue. In the present review, we describe the molecular mechanisms of nutrient-sensing of the calcium-sensing receptor (CaR), the G protein-coupled receptor family C, group 6, subtype A (GPRC6A), and the taste1 receptor T1R1/T1R3-sensing L-a-amino acids; the carbohydrate-sensing T1R2/T1R3 receptor; the proteolytic degradation product sensor GPR93 (also termed GPR92); and the FFA sensing receptors FFA1, FFA2, FFA3, GPR84, and GPR120. Due to their omnipresent nature, the natural ligands have had limited usability in pharmacological/physiological studies which has hampered the elucidation of the physiological function and therapeutic prospect of their receptors. However, an increasing number of subtype-selective ligands and/or receptor knockout mice are being developed which at least for some of the receptors have validated them as promising drug targets in, for example, type II diabetes.",
keywords = "The Faculty of Pharmaceutical Sciences",
author = "Petrine Wellendorph and Johansen, {Lars Dan} and Hans Br{\"a}uner-Osborne",
note = "Copyright {\circledC} 2010 Elsevier Inc. All rights reserved.",
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language = "English",
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RIS

TY - CHAP

T1 - The emerging role of promiscuous 7TM receptors as chemosensors for food intake

AU - Wellendorph, Petrine

AU - Johansen, Lars Dan

AU - Bräuner-Osborne, Hans

N1 - Copyright © 2010 Elsevier Inc. All rights reserved.

PY - 2010/1/1

Y1 - 2010/1/1

N2 - In recent years, several highly promiscuous seven transmembrane (7TM) receptors have been cloned and characterized of which many are activated broadly by amino acids, proteolytic degradation products, carbohydrates, or free fatty acids (FFAs) and are expressed in taste tissue, the gastrointestinal (GI) tract, endocrine glands, adipose tissue, and/or kidney. This has led to the hypothesis that these receptors may act as sensors of food intake modulating, for example, release of incretin hormones from the gut, insulin/glucagon from the pancreas, and leptin from adipose tissue. In the present review, we describe the molecular mechanisms of nutrient-sensing of the calcium-sensing receptor (CaR), the G protein-coupled receptor family C, group 6, subtype A (GPRC6A), and the taste1 receptor T1R1/T1R3-sensing L-a-amino acids; the carbohydrate-sensing T1R2/T1R3 receptor; the proteolytic degradation product sensor GPR93 (also termed GPR92); and the FFA sensing receptors FFA1, FFA2, FFA3, GPR84, and GPR120. Due to their omnipresent nature, the natural ligands have had limited usability in pharmacological/physiological studies which has hampered the elucidation of the physiological function and therapeutic prospect of their receptors. However, an increasing number of subtype-selective ligands and/or receptor knockout mice are being developed which at least for some of the receptors have validated them as promising drug targets in, for example, type II diabetes.

AB - In recent years, several highly promiscuous seven transmembrane (7TM) receptors have been cloned and characterized of which many are activated broadly by amino acids, proteolytic degradation products, carbohydrates, or free fatty acids (FFAs) and are expressed in taste tissue, the gastrointestinal (GI) tract, endocrine glands, adipose tissue, and/or kidney. This has led to the hypothesis that these receptors may act as sensors of food intake modulating, for example, release of incretin hormones from the gut, insulin/glucagon from the pancreas, and leptin from adipose tissue. In the present review, we describe the molecular mechanisms of nutrient-sensing of the calcium-sensing receptor (CaR), the G protein-coupled receptor family C, group 6, subtype A (GPRC6A), and the taste1 receptor T1R1/T1R3-sensing L-a-amino acids; the carbohydrate-sensing T1R2/T1R3 receptor; the proteolytic degradation product sensor GPR93 (also termed GPR92); and the FFA sensing receptors FFA1, FFA2, FFA3, GPR84, and GPR120. Due to their omnipresent nature, the natural ligands have had limited usability in pharmacological/physiological studies which has hampered the elucidation of the physiological function and therapeutic prospect of their receptors. However, an increasing number of subtype-selective ligands and/or receptor knockout mice are being developed which at least for some of the receptors have validated them as promising drug targets in, for example, type II diabetes.

KW - The Faculty of Pharmaceutical Sciences

U2 - 10.1016/B978-0-12-381517-0.00005-9

DO - 10.1016/B978-0-12-381517-0.00005-9

M3 - Book chapter

SN - 978-0-12-381517-0

VL - 84

SP - 151

EP - 184

BT - Incretins and insulin secretion

A2 - Litwack, Gerald

PB - Elsevier Editora

CY - Amsterdam

ER -

ID: 32167812