Kalcitoninski receptor

Kalcitoninski receptor
Kalcitoninski receptor
Identifikatori
Simboli	CALCR; CRT; CT-R; CTR1
Vanjski ID	OMIM: 114131 MGI: 101950 HomoloGene: 1320 IUPHAR: CT GeneCards: CALCR Gene
Ontologija gena
Molekularna funkcija	• receptorska akctivnost; • aktivnosti kalcitoninskog receptora; • proteinsko vezivanje;
Celularna komponenta	• ćelijska membrana; • integralno sa ćelijskom membranom; • integralno sa membranom;
Biološki proces	• signalni put adenilat ciklazom aktiviranog G-protein spregnutor receptora; • aktivacija adenilat ciklaze; • aktivacija fosfolipaze C;
Pregled RNK izražavanja
	podaci
Ortolozi
Vrsta	Čovek
Entrez	799
Ensembl	ENSG00000004948
UniProt	P30988
RefSeq (mRNA)	NM_001164737.1
RefSeq (protein)	NP_001158209.1
Lokacija (UCSC)	Chr 7:; 93.05 - 93.2 Mb
PubMed pretraga	[1]

Kalcitoninski receptor (CT) je G protein spregnuti receptor za koji se vezuje peptidni hormon kalcitonin. On učestvuje u održavanju kalcijumske homeostaze^[1], posebno u pogledu formiranja kostiju i metabolizma.^[2]^[3]^[4]

CT deluje putem aktivacije G-proteina G_s i G_q često nađenih na osteoklastima, na ćelijama u bubregu, i na ćelijama u brojnim regionima mozga.^[5]. On takođe može da utiče na jajnike i testise.

Funkcija CT receptora je posredovana interakcijom sa modifikujućim protenima receptorske aktivnosti, čime se formiraju multimerni amilinski receptori AMY₁ (CT + RAMP1), AMY₂ (CT + RAMP2), i AMY₃ (CT+ RAMP3).^[6]

Interakcije

Kalcitoninski receptor formira interakcije sa apolipoproteinom B^[7]^[8] i LRP1.^[9]

Reference

^ Purdue BW, Tilakaratne N, Sexton PM (2002). „Molecular pharmacology of the calcitonin receptor”. Recept. Channels. 8 (3–4): 243—55. PMID 12529940. doi:10.1080/10606820213681.
^ Chambers TJ, Magnus CJ (1982). „Calcitonin alters behaviour of isolated osteoclasts”. J. Pathol. 136 (1): 27—39. PMID 7057295. doi:10.1002/path.1711360104.
^ Dacquin R, Davey RA, Laplace C, Levasseur R, Morris HA, Goldring SR, Gebre-Medhin S, Galson DL, Zajac JD, Karsenty G (2004). „Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo”. J. Cell Biol. 164 (4): 509—514. PMC 2171986  . PMID 14970190. doi:10.1083/jcb.200312135.
^ Davey RA, Turner A, McManus JF, Chiu WS, Tjahyono F, Moore AJ, Atkins GJ, Anderson PH, Ma C, Glatt V, Maclean HE, Vincent C, Bouxsein M, Morris HA, Findlay DM, Zajac JD (2008). „Calcitonin Receptor Plays a Physiological Role to Protect Against Hypercalcemia in Mice”. J Bone Miner Res. 23 (8): 1182—1193. PMC 2680171  . PMID 18348688. doi:10.1359/jbmr.080310.
^ „senselab”. Архивирано из оригинала 28. 02. 2009. г. Приступљено 02. 08. 2012.
^ „Calcitonin Receptors: Introduction”. IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Архивирано из оригинала 03. 03. 2016. г.
^ Zhang, Jianying; Herscovitz Haya (2003). „Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B”. J. Biol. Chem. United States. 278 (9): 7459—68. ISSN 0021-9258. PMID 12397072. doi:10.1074/jbc.M207976200.
^ Linnik, K M; Herscovitz H (1998). „Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state”. J. Biol. Chem. UNITED STATES. 273 (33): 21368—73. ISSN 0021-9258. PMID 9694898. doi:10.1074/jbc.273.33.21368.
^ Orr, Anthony Wayne; Pedraza Claudio E; et al. (2003). „Low density lipoprotein receptor–related protein is a calreticulin coreceptor that signals focal adhesion disassembly”. J. Cell Biol. United States. 161 (6): 1179—89. ISSN 0021-9525. PMC 2172996  . PMID 12821648. doi:10.1083/jcb.200302069.

Literatura

Pondel M (2001). „Calcitonin and calcitonin receptors: bone and beyond”. International journal of experimental pathology. 81 (6): 405—22. PMID 11298188. doi:10.1046/j.1365-2613.2000.00176.x.
Gorn AH; Lin HY; Yamin M; et al. (1992). „Cloning, characterization, and expression of a human calcitonin receptor from an ovarian carcinoma cell line”. J. Clin. Invest. 90 (5): 1726—35. PMC 443230  . PMID 1331173. doi:10.1172/JCI116046.
Albrandt K; Brady EM; Moore CX; et al. (1995). „Molecular cloning and functional expression of a third isoform of the human calcitonin receptor and partial characterization of the calcitonin receptor gene”. Endocrinology. 136 (12): 5377—84. PMID 7588285. doi:10.1210/en.136.12.5377.
Egerton M; Needham M; Evans S; et al. (1995). „Identification of multiple human calcitonin receptor isoforms: heterologous expression and pharmacological characterization”. J. Mol. Endocrinol. 14 (2): 179—89. PMID 7619207. doi:10.1677/jme.0.0140179.
Nussenzveig DR, Mathew S, Gershengorn MC (1995). „Alternative splicing of a 48-nucleotide exon generates two isoforms of the human calcitonin receptor”. Endocrinology. 136 (5): 2047—51. PMID 7720653. doi:10.1210/en.136.5.2047.
Nakamura M; Hashimoto T; Nakajima T; et al. (1995). „A new type of human calcitonin receptor isoform generated by alternative splicing”. Biochem. Biophys. Res. Commun. 209 (2): 744—51. PMID 7733946. doi:10.1006/bbrc.1995.1562.
Pérez Jurado LA, Li X, Francke U (1995). „The human calcitonin receptor gene (CALCR) at 7q21.3 is outside the deletion associated with the Williams syndrome”. Cytogenet. Cell Genet. 70 (3–4): 246—9. PMID 7789182. doi:10.1159/000134044.
Nussenzveig DR, Thaw CN, Gershengorn MC (1994). „Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes”. J. Biol. Chem. 269 (45): 28123—9. PMID 7961748.
Kuestner RE; Elrod RD; Grant FJ; et al. (1994). „Cloning and characterization of an abundant subtype of the human calcitonin receptor”. Mol. Pharmacol. 46 (2): 246—55. PMID 8078488.
Frendo JL; Pichaud F; Mourroux RD; et al. (1994). „An isoform of the human calcitonin receptor is expressed in TT cells and in medullary carcinoma of the thyroid”. FEBS Lett. 342 (2): 214—6. PMID 8143880. doi:10.1016/0014-5793(94)80503-2.
Masi L; Becherini L; Gennari L; et al. (1998). „Allelic variants of human calcitonin receptor: distribution and association with bone mass in postmenopausal Italian women”. Biochem. Biophys. Res. Commun. 245 (2): 622—6. PMID 9571205. doi:10.1006/bbrc.1998.8445.
Taboulet J; Frenkian M; Frendo JL; et al. (1999). „Calcitonin receptor polymorphism is associated with a decreased fracture risk in post-menopausal women”. Hum. Mol. Genet. 7 (13): 2129—33. PMID 9817931. doi:10.1093/hmg/7.13.2129.
Christopoulos G; Perry KJ; Morfis M; et al. (1999). „Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product”. Mol. Pharmacol. 56 (1): 235—42. PMID 10385705.
Nishikawa T, Ishikawa H, Yamamoto S, Koshihara Y (2000). „A novel calcitonin receptor gene in human osteoclasts from normal bone marrow”. FEBS Lett. 458 (3): 409—14. PMID 10570950. doi:10.1016/S0014-5793(99)01176-X.
Beaudreuil J; Taboulet J; Orcel P; et al. (2000). „Calcitonin receptor mRNA in mononuclear leucocytes from postmenopausal women: decrease during osteoporosis and link to bone markers with specific isoform involvement”. Bone. 27 (1): 161—8. PMID 10865224. doi:10.1016/S8756-3282(00)00305-7.
Wada S; Yasuda S; Nagai T; et al. (2001). „Regulation of calcitonin receptor by glucocorticoid in human osteoclast-like cells prepared in vitro using receptor activator of nuclear factor-kappaB ligand and macrophage colony-stimulating factor”. Endocrinology. 142 (4): 1471—8. PMID 11250927. doi:10.1210/en.142.4.1471.
Ogden CA; deCathelineau A; Hoffmann PR; et al. (2001). „C1q and Mannose Binding Lectin Engagement of Cell Surface Calreticulin and Cd91 Initiates Macropinocytosis and Uptake of Apoptotic Cells”. J. Exp. Med. 194 (6): 781—95. PMC 2195958  . PMID 11560994. doi:10.1084/jem.194.6.781.
Nosaka Y; Tachi Y; Shimpuku H; et al. (2002). „Association of calcitonin receptor gene polymorphism with early marginal bone loss around endosseous implants”. The International journal of oral & maxillofacial implants. 17 (1): 38—43. PMID 11858573.
Strausberg RL; Feingold EA; Grouse LH; et al. (2003). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899—903. PMC 139241  . PMID 12477932. doi:10.1073/pnas.242603899.

Spoljašnje veze

„Calcitonin Receptors”. IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
Calcitonin+receptors на US National Library of Medicine Medical Subject Headings (MeSH)

[pmid12529940-1] Purdue BW, Tilakaratne N, Sexton PM (2002). „Molecular pharmacology of the calcitonin receptor”. Recept. Channels. 8 (3–4): 243—55. PMID 12529940. doi:10.1080/10606820213681.

[pmid7057295-2] Chambers TJ, Magnus CJ (1982). „Calcitonin alters behaviour of isolated osteoclasts”. J. Pathol. 136 (1): 27—39. PMID 7057295. doi:10.1002/path.1711360104.

[pmid14970190-3] Dacquin R, Davey RA, Laplace C, Levasseur R, Morris HA, Goldring SR, Gebre-Medhin S, Galson DL, Zajac JD, Karsenty G (2004). „Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo”. J. Cell Biol. 164 (4): 509—514. PMC 2171986  . PMID 14970190. doi:10.1083/jcb.200312135.

[pmid18348688-4] Davey RA, Turner A, McManus JF, Chiu WS, Tjahyono F, Moore AJ, Atkins GJ, Anderson PH, Ma C, Glatt V, Maclean HE, Vincent C, Bouxsein M, Morris HA, Findlay DM, Zajac JD (2008). „Calcitonin Receptor Plays a Physiological Role to Protect Against Hypercalcemia in Mice”. J Bone Miner Res. 23 (8): 1182—1193. PMC 2680171  . PMID 18348688. doi:10.1359/jbmr.080310.

[5] „senselab”. Архивирано из оригинала 28. 02. 2009. г. Приступљено 02. 08. 2012.

[IUPHAR-DB-6] „Calcitonin Receptors: Introduction”. IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Архивирано из оригинала 03. 03. 2016. г.

[pmid12397072-7] Zhang, Jianying; Herscovitz Haya (2003). „Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B”. J. Biol. Chem. United States. 278 (9): 7459—68. ISSN 0021-9258. PMID 12397072. doi:10.1074/jbc.M207976200.

[pmid9694898-8] Linnik, K M; Herscovitz H (1998). „Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state”. J. Biol. Chem. UNITED STATES. 273 (33): 21368—73. ISSN 0021-9258. PMID 9694898. doi:10.1074/jbc.273.33.21368.

[pmid12821648-9] Orr, Anthony Wayne; Pedraza Claudio E; et al. (2003). „Low density lipoprotein receptor–related protein is a calreticulin coreceptor that signals focal adhesion disassembly”. J. Cell Biol. United States. 161 (6): 1179—89. ISSN 0021-9525. PMC 2172996  . PMID 12821648. doi:10.1083/jcb.200302069.

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