Biology:STC1
 Generic protein structure example |
Stanniocalcin-1 is a glycoprotein, a homologue of a hormone stanniocalcin, first discovered in bony fishes. In humans it is encoded by the STC1 gene.[1][2]
Function
This gene encodes a secreted, homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The only known molecular function of human Stanniocalcin-1 to date is a SUMO E3 ubiquitin ligase activity in the SUMOylation cycle. However, STC1 interacts with many proteins in the cytoplasm, mitochondria, endoplasmatic reticulum, and in dot-like fashion in the cell nucleus. The N-terminal region of STC1 is the function region which is responsible to establish the interaction with its partners, including SUMO1.[3] Low-resolution studies shows that STC1 is an anti-parallel homodimer in solution and the cysteine 202 is responsible for its dimerization. All the 5 disulfide bonds of human STC1 are conserved and have the same profile of fish STC.[4] The gene contains a 5' UTR rich in CAG trinucleotide repeats. The encoded protein contains 11 conserved cysteine residues and is phosphorylated by protein kinase C exclusively on its serine residues.
The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Overexpression of human stanniocalcin 1 in mice produces high serum phosphate levels, dwarfism, and increased metabolic rate. This gene has altered expression in hepatocellular, ovarian, and breast cancers,[2] and is a putative molecular biomarker of leukemic microenvironment.
References
- ↑ "Human stanniocalcin (STC): genomic structure, chromosomal localization, and the presence of CAG trinucleotide repeats". Genomics 47 (3): 393–8. Feb 1998. doi:10.1006/geno.1997.5120. PMID 9480753.
- ↑ 2.0 2.1 "Entrez Gene: STC1 stanniocalcin 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6781.
- ↑ "Human stanniocalcin-1 interacts with nuclear and cytoplasmic proteins and acts as a SUMO E3 ligase". Molecular BioSystems 7 (1): 180–93. Jan 2011. doi:10.1039/c0mb00088d. PMID 21042649.
- ↑ "Low-resolution structural studies of human Stanniocalcin-1". BMC Structural Biology 9: 57. Aug 27, 2009. doi:10.1186/1472-6807-9-57. PMID 19712479.
Further reading
- "Mammalian stanniocalcins and cancer". Endocrine-Related Cancer 10 (3): 359–73. Sep 2003. doi:10.1677/erc.0.0100359. PMID 14503913.
- "Differential display and cloning of messenger RNAs from human breast cancer versus mammary epithelial cells". Cancer Research 52 (24): 6966–8. Dec 1992. PMID 1458489.
- "A novel human cDNA highly homologous to the fish hormone stanniocalcin". Molecular and Cellular Endocrinology 112 (2): 241–7. Aug 1995. doi:10.1016/0303-7207(95)03601-3. PMID 7489828.
- "Immunological and biological evidence for a stanniocalcin-like hormone in human kidney". Proceedings of the National Academy of Sciences of the United States of America 92 (6): 1871–5. Mar 1995. doi:10.1073/pnas.92.6.1871. PMID 7892193. Bibcode: 1995PNAS...92.1871W.
- "Human stanniocalcin: a possible hormonal regulator of mineral metabolism". Proceedings of the National Academy of Sciences of the United States of America 93 (5): 1792–6. Mar 1996. doi:10.1073/pnas.93.5.1792. PMID 8700837. Bibcode: 1996PNAS...93.1792O.
- "High expression of stanniocalcin in differentiated brain neurons". The American Journal of Pathology 153 (2): 439–45. Aug 1998. doi:10.1016/S0002-9440(10)65587-3. PMID 9708804.
- "Comparative analysis of mammalian stanniocalcin genes". Endocrinology 139 (11): 4714–25. Nov 1998. doi:10.1210/en.139.11.4714. PMID 9794484.
- "Stanniocalcin: A molecular guard of neurons during cerebral ischemia". Proceedings of the National Academy of Sciences of the United States of America 97 (7): 3637–42. Mar 2000. doi:10.1073/pnas.070045897. PMID 10725397.
- "Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells". The Biochemical Journal 350 Pt 2 (2): 453–61. Sep 2000. doi:10.1042/0264-6021:3500453. PMID 10947959.
- "Overexpression of human stanniocalcin affects growth and reproduction in transgenic mice". Endocrinology 143 (3): 868–76. Mar 2002. doi:10.1210/endo.143.3.8671. PMID 11861508.
- "Characterization of mammalian stanniocalcin receptors. Mitochondrial targeting of ligand and receptor for regulation of cellular metabolism". The Journal of Biological Chemistry 277 (47): 45249–58. Nov 2002. doi:10.1074/jbc.M205954200. PMID 12223480.
- "Expression of stanniocalcin-1 in megakaryocytes and platelets". British Journal of Haematology 119 (2): 359–63. Nov 2002. doi:10.1046/j.1365-2141.2002.03916.x. PMID 12406069.
- "Stanniocalcin-1 is a naturally occurring L-channel inhibitor in cardiomyocytes: relevance to human heart failure". American Journal of Physiology. Heart and Circulatory Physiology 285 (1): H442–8. Jul 2003. doi:10.1152/ajpheart.01071.2002. PMID 12663264.
- "Stanniocalcin 1 is an autocrine modulator of endothelial angiogenic responses to hepatocyte growth factor". The Journal of Biological Chemistry 278 (48): 47654–9. Nov 2003. doi:10.1074/jbc.M301353200. PMID 14500721.
- "Co-localization of stanniocalcin-1 ligand and receptor in human breast carcinomas". Molecular and Cellular Endocrinology 213 (2): 167–72. Jan 2004. doi:10.1016/j.mce.2003.10.042. PMID 15062564.
- "Paracrine regulation of ovarian granulosa cell differentiation by stanniocalcin (STC) 1: mediation through specific STC1 receptors". Molecular Endocrinology 18 (8): 2085–96. Aug 2004. doi:10.1210/me.2004-0066. PMID 15131261.
- "Upregulated expression of stanniocalcin-1 during adipogenesis". Experimental Cell Research 296 (2): 256–64. Jun 2004. doi:10.1016/j.yexcr.2004.02.016. PMID 15149855.
 |
