Biomaterial Database

Novel neuropeptides in the control of food intake: neuronostatin and nesfatin-1. 2013

Gina L C Yosten

Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, Saint Louis, Missouri, USA. gyosten@slu.edu

Food intake is a complex, multifaceted process that involves the integration of numerous nutritional signals and behavioral outputs. Dozens of centrally acting peptide hormones that contribute to the control of appetite and food intake have been identified. Two recently described peptide hormones, neuronostatin and nesfatin-1, both act in the brain to induce anorexia, albeit through potentially different mechanisms. In this chapter, the central circuits mediating the anorexigenic effect of these two hormones, their interaction with the central melanocortin and oxytocin systems, and the physiological relevance of these hormones in appetite control are described and an integrated model of hypothalamic control of energy intake is presented.

UI	MeSH Term	Description	Entries
D009419	Nerve Tissue Proteins		Proteins, Nerve Tissue,Tissue Proteins, Nerve
D001921	Brain	The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.	Encephalon
D002135	Calcium-Binding Proteins	Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.	Calcium Binding Protein,Calcium-Binding Protein,Calcium Binding Proteins,Binding Protein, Calcium,Binding Proteins, Calcium,Protein, Calcium Binding,Protein, Calcium-Binding
D004268	DNA-Binding Proteins	Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.	DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D004435	Eating	The consumption of edible substances.	Dietary Intake,Feed Intake,Food Intake,Macronutrient Intake,Micronutrient Intake,Nutrient Intake,Nutritional Intake,Ingestion,Dietary Intakes,Feed Intakes,Intake, Dietary,Intake, Feed,Intake, Food,Intake, Macronutrient,Intake, Micronutrient,Intake, Nutrient,Intake, Nutritional,Macronutrient Intakes,Micronutrient Intakes,Nutrient Intakes,Nutritional Intakes
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000080866	Nucleobindins	A DNA and calcium binding protein which plays a role in calcium homeostasis.	CALNUC protein,Nucleobindin,Nucleobindin-1 protein,CALNUC,Nucleobindin 1 protein,protein, CALNUC,protein, Nucleobindin-1
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D000855	Anorexia	The lack or loss of APPETITE accompanied by an aversion to food and the inability to eat. It is the defining characteristic of the disorder ANOREXIA NERVOSA.	Anorexias
D036361	Peptide Hormones	Hormones synthesized from amino acids. They are distinguished from INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS in that their actions are systemic.	Hormones, Peptide,Peptide Hormone,Polypeptide Hormone,Polypeptide Hormones,Hormone, Peptide,Hormone, Polypeptide,Hormones, Polypeptide