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]

Kalcitoninski receptor
Identifikatori
Simboli CALCR; CRT; CT-R; CTR1
Vanjski ID OMIM114131 MGI101950 HomoloGene1320 IUPHAR: CT GeneCards: CALCR Gene
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 799 12311
Ensembl ENSG00000004948 ENSMUSG00000023964
UniProt P30988 Q3UUL9
RefSeq (mRNA) NM_001164737.1 NM_001042725.1
RefSeq (protein) NP_001158209.1 NP_001036190.1
Lokacija (UCSC) Chr 7:
93.05 - 93.2 Mb
Chr 6:
3.64 - 3.71 Mb
PubMed pretraga [1] [2]

CT deluje putem aktivacije G-proteina Gs i Gq 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

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

Reference

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  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. 
  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. 
  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. 
  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. 
  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. 
  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. 
  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. 
  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. 

Literatura

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Spoljašnje veze

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