Biomaterial Database

[Regulation of energy metabolism by bone]. 2008

Hideaki Sowa

Columbia University, Genetics and Development.

In terms of feedback regulation in Endocrinology, one question was arisen from the evidences that energy metabolism regulates bone metabolism. "Does bone metabolism regulates energy metabolism?" To address this question, Dr. Gerard Karsenty and his colleagues studied energy metabolism in the mice lacking Osteocalcin, an osteoblast-specific gene. The mutant mice exhibited abnormal energy metabolism phenotypes, diabetes and obesity. Here I would like to remind you his previous and recent works so that we can discuss how to apply bone metabolism information to therapeutic strategy for metabolic syndrome.

UI	MeSH Term	Description	Entries
D009765	Obesity	A status with BODY WEIGHT that is grossly above the recommended standards, usually due to accumulation of excess FATS in the body. The standards may vary with age, sex, genetic or cultural background. In the BODY MASS INDEX, a BMI greater than 30.0 kg/m2 is considered obese, and a BMI greater than 40.0 kg/m2 is considered morbidly obese (MORBID OBESITY).
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D001842	Bone and Bones	A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principal cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.	Bone Tissue,Bone and Bone,Bone,Bones,Bones and Bone,Bones and Bone Tissue,Bony Apophyses,Bony Apophysis,Condyle,Apophyses, Bony,Apophysis, Bony,Bone Tissues,Condyles,Tissue, Bone,Tissues, Bone
D003920	Diabetes Mellitus	A heterogeneous group of disorders characterized by HYPERGLYCEMIA and GLUCOSE INTOLERANCE.
D004734	Energy Metabolism	The chemical reactions involved in the production and utilization of various forms of energy in cells.	Bioenergetics,Energy Expenditure,Bioenergetic,Energy Expenditures,Energy Metabolisms,Expenditure, Energy,Expenditures, Energy,Metabolism, Energy,Metabolisms, Energy
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
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
D015675	Osteocalcin	Vitamin K-dependent calcium-binding protein synthesized by OSTEOBLASTS and found primarily in BONES. Serum osteocalcin measurements provide a noninvasive specific marker of bone metabolism. The protein contains three residues of the amino acid gamma-carboxyglutamic acid (Gla), which, in the presence of CALCIUM, promotes binding to HYDROXYAPATITE and subsequent accumulation in BONE MATRIX.	Bone Gla Protein,Calcium-Binding Protein, Vitamin K-Dependent,Gla Protein, Bone,Vitamin K-Dependent Bone Protein,4-Carboxyglutamic Protein, Bone,Bone gamma-Carboxyglutamic Acid Protein,4 Carboxyglutamic Protein, Bone,Bone 4-Carboxyglutamic Protein,Bone gamma Carboxyglutamic Acid Protein,Calcium Binding Protein, Vitamin K Dependent,Protein, Bone 4-Carboxyglutamic,Protein, Bone Gla,Vitamin K Dependent Bone Protein
D051379	Mice	The common name for the genus Mus.	Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D054631	Receptor-Like Protein Tyrosine Phosphatases, Class 3	A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.	Protein Tyrosine Phosphatase, Receptor Type B,Protein Tyrosine Phosphatase, Receptor Type H,Protein Tyrosine Phosphatase, Receptor Type J,Protein Tyrosine Phosphatase, Receptor Type O,Protein Tyrosine Phosphatase, Receptor Type Q,Protein Tyrosine Phosphatase, Receptor Type V,DEP1 Phosphatase,Density-Enhanced Phosphatase 1,GLEPP1 Phosphatase,Glomerular Epithelial Protein 1,PTPRB Phosphatase,PTPRH Phosphatase,PTPRJ Phosphatase,PTPRO Phosphatase,PTPRQ Phosphatase,PTPRV Phosphatase,Protein Tyrosine Phosphatase Receptor omicron,Protein-Tyrosine Phosphatase eta,Receptor-Like Protein Tyrosine Phosphatases, Class III,SAP-1 Phosphatase,Stomach Cancer-Associated Protein-Tyrosine Phosphatase,VE-PTP Phosphatase,Vascular Endothelial Protein Tyrosine Phosphatase,Density Enhanced Phosphatase 1,Phosphatase eta, Protein-Tyrosine,Phosphatase, GLEPP1,Phosphatase, PTPRB,Phosphatase, PTPRH,Phosphatase, PTPRJ,Phosphatase, PTPRO,Phosphatase, PTPRQ,Phosphatase, PTPRV,Phosphatase, SAP-1,Protein Tyrosine Phosphatase eta,Receptor Like Protein Tyrosine Phosphatases, Class 3,Receptor Like Protein Tyrosine Phosphatases, Class III,SAP 1 Phosphatase,Stomach Cancer Associated Protein Tyrosine Phosphatase,VE PTP Phosphatase