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1

Luo, Ching-Wei, Margareta D. Pisarska, and Aaron J. W. Hsueh. "Identification of a Stanniocalcin Paralog, Stanniocalcin-2, in Fish and the Paracrine Actions of Stanniocalcin-2 in the Mammalian Ovary." Endocrinology 146, no. 1 (January 1, 2005): 469–76. http://dx.doi.org/10.1210/en.2004-1197.

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2

Chang, A. C. M., and Roger R. Reddel. "Identification of a second stanniocalcin cDNA in mouse and human: Stanniocalcin 2." Molecular and Cellular Endocrinology 141, no. 1-2 (June 1998): 95–99. http://dx.doi.org/10.1016/s0303-7207(98)00097-5.

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3

Gagliardi, Anthony D., Evan Y. W. Kuo, Sanda Raulic, Graham F. Wagner, and Gabriel E. DiMattia. "Human stanniocalcin-2 exhibits potent growth-suppressive properties in transgenic mice independently of growth hormone and IGFs." American Journal of Physiology-Endocrinology and Metabolism 288, no. 1 (January 2005): E92—E105. http://dx.doi.org/10.1152/ajpendo.00268.2004.

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Stanniocalcin (STC)-2 was discovered by its primary amino acid sequence identity to the hormone STC-1. The function of STC-2 has not been examined; thus we generated two lines of transgenic mice overexpressing human (h)STC-2 to gain insight into its potential functions through identification of overt phenotypes. Analysis of mouse Stc2 gene expression indicates that, unlike Stc1, it is not highly expressed during development but exhibits overlapping expression with Stc1 in adult mice, with heart and skeletal muscle exhibiting highest steady-state levels of Stc2 mRNA. Constitutive overexpression of hSTC-2 resulted in pre- and postnatal growth restriction as early as embryonic day 12.5, progressing such that mature hSTC-2-transgenic mice are ∼45% smaller than wild-type littermates. hSTC-2 overexpression is sometimes lethal; we observed 26–34% neonatal morbidity without obvious dysmorphology. hSTC-2-induced growth retardation is associated with developmental delay, most notably cranial suture formation. Organ allometry studies show that hSTC-2-induced dwarfism is associated with testicular organomegaly and a significant reduction in skeletal muscle mass likely contributing to the dwarf phenotype. hSTC-2-transgenic mice are also hyperphagic, but this does not result in obesity. Serum Ca2+ and PO4 were unchanged in hSTC-2-transgenic mice, although STC-1 can regulate intra- and extracellular Ca2+ in mammals. Interestingly, severe growth retardation induced by hSTC-2 is not associated with a decrease in GH or IGF expression. Consequently, similar to STC-1, STC-2 can act as a potent growth inhibitor and reduce intramembranous and endochondral bone development and skeletal muscle growth, implying that these tissues are specific physiological targets of stanniocalcins.
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4

Steffensen, Lasse B., Cheryl A. Conover, Martin M. Bjørklund, Thomas Ledet, Jacob F. Bentzon, and Claus Oxvig. "Stanniocalcin-2 overexpression reduces atherosclerosis in hypercholesterolemic mice." Atherosclerosis 248 (May 2016): 36–43. http://dx.doi.org/10.1016/j.atherosclerosis.2016.02.026.

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5

Sarapio, Elaine, Samir K. De Souza, Jorge F. A. Model, Marcia Trapp, and Roselis S. M. Da Silva. "Stanniocalcin-1 and -2 effects on glucose and lipid metabolism in white adipose tissue from fed and fasted rats." Canadian Journal of Physiology and Pharmacology 97, no. 10 (October 2019): 916–23. http://dx.doi.org/10.1139/cjpp-2019-0023.

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Stanniocalcin-1 and -2 belong to a family of molecules that exhibit both paracrine and autocrine effects in mammalian cells. Human stanniocalcin-1 (hSTC-1) is expressed in a wide range of tissues, including white adipose tissue. In fed rats, hSTC-1 increases carbon flux from glucose to lipids in retroperitoneal white adipose tissue. Human stanniocalcin-2 (hSTC-2) is expressed in almost all tissues and regulates various biological processes. The aim of this work was to study the action of hSTC-1 and hSTC-2 in the lipid and glucose metabolism of epididymal white adipose tissue (eWAT) in rats in different nutritional states. This study shows for the first time an opposite effect of hSTC-1 and hSTC-2 on glyceride-glycerol generation from glucose in eWAT of fed rats. hSTC-1 stimulated the storage of triacylglycerol in eWAT in the postprandial period, increasing glucose uptake and glyceride-glycerol generation from 14C-glucose. hSTC-2 decreased triacylglycerol synthesis, reducing glyceride-glycerol generation from 14C-glucose, direct phosphorylation of glycerol, and fatty acid synthesis from 14C-glucose in eWAT of fed rats. However, both hormones increased glucose uptake in fed and fasting states. These findings provide evidence for a direct role of hSTC-1 and hSTC-2 in the regulation of lipid and glucose metabolism in eWAT of rats.
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6

Zhou, Juan, Yinghua Li, Lina Yang, Yougen Wu, Yunjiao Zhou, Yunqing Cui, Gong Yang, and Yang Hong. "Stanniocalcin 2 improved osteoblast differentiation via phosphorylation of ERK." Molecular Medicine Reports 14, no. 6 (November 16, 2016): 5653–59. http://dx.doi.org/10.3892/mmr.2016.5951.

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7

ZHANG, ZHEN-HAI, YA-GUANG WU, CHENG-KUN QIN, ZHONG-HOU RONG, ZHONG-XUE SU, and GUO-ZHE XIAN. "Stanniocalcin 2 expression predicts poor prognosis of hepatocellular carcinoma." Oncology Letters 8, no. 5 (September 10, 2014): 2160–64. http://dx.doi.org/10.3892/ol.2014.2520.

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8

Zhou, Han, Ying-Ying Li, Wei-Qiang Zhang, Dan Lin, Wei-Ming Zhang, and Wei-Da Dong. "Expression of Stanniocalcin-1 and Stanniocalcin-2 in Laryngeal Squamous Cell Carcinoma and Correlations with Clinical and Pathological Parameters." PLoS ONE 9, no. 4 (April 17, 2014): e95466. http://dx.doi.org/10.1371/journal.pone.0095466.

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9

Hu, Lixia, Yanyan Zha, Fanliang Kong, and Yueyin Pan. "Prognostic value of high stanniocalcin 2 expression in solid cancers." Medicine 98, no. 43 (October 2019): e17432. http://dx.doi.org/10.1097/md.0000000000017432.

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10

Meyer, Hellmuth-A., Angelika Tölle, Monika Jung, Florian R. Fritzsche, Bernard Haendler, Ilka Kristiansen, Ariana Gaspert, Manfred Johannsen, Klaus Jung, and Glen Kristiansen. "Identification of Stanniocalcin 2 as Prognostic Marker in Renal Cell Carcinoma." European Urology 55, no. 3 (March 2009): 669–78. http://dx.doi.org/10.1016/j.eururo.2008.04.001.

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11

Zeiger, W., D. Ito, C. Swetlik, M. Oh-hora, M. L. Villereal, and G. Thinakaran. "Stanniocalcin 2 Is a Negative Modulator of Store-Operated Calcium Entry." Molecular and Cellular Biology 31, no. 18 (July 11, 2011): 3710–22. http://dx.doi.org/10.1128/mcb.05140-11.

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12

Kim, Pyung-Hwan, Sang-Su Na, Bomnaerin Lee, Joo-Hyun Kim, and Je-Yoel Cho. "Stanniocalcin 2 enhances mesenchymal stem cell survival by suppressing oxidative stress." BMB Reports 48, no. 12 (December 31, 2015): 702–7. http://dx.doi.org/10.5483/bmbrep.2015.48.12.158.

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13

Jiang, Shu-ting, Hua-qiao Wang, Tie-cheng Yang, Dan-wen Wang, Li-jie Yang, Yi-qing Xi, Fan-zheng Kong, et al. "Expression of Stanniocalcin 2 in Breast Cancer and Its Clinical Significance." Current Medical Science 39, no. 6 (December 2019): 978–83. http://dx.doi.org/10.1007/s11596-019-2131-2.

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14

Mittapalli, Venugopal Rao, Felicitas Pröls, Ruijin Huang, Bodo Christ, and Martin Scaal. "Avian stanniocalcin-2 is expressed in developing striated muscle and joints." Anatomy and Embryology 211, no. 5 (May 23, 2006): 519–23. http://dx.doi.org/10.1007/s00429-006-0100-6.

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15

Wang, Yuxia, Ying Gao, Hairong Cheng, Guichun Yang, and Wenhua Tan. "Stanniocalcin 2 promotes cell proliferation and cisplatin resistance in cervical cancer." Biochemical and Biophysical Research Communications 466, no. 3 (October 2015): 362–68. http://dx.doi.org/10.1016/j.bbrc.2015.09.029.

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16

Flik, G., T. Labedz, J. A. Neelissen, R. G. Hanssen, S. E. Wendelaar Bonga, and P. K. Pang. "Rainbow trout corpuscles of Stannius: stanniocalcin synthesis in vitro." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 258, no. 5 (May 1, 1990): R1157—R1164. http://dx.doi.org/10.1152/ajpregu.1990.258.5.r1157.

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In fresh-water rainbow trout, Oncorhynchus mykiss (formerly called Salmo gairdneri), experimentally induced mild hypercalcemia results in release of immunoreactive stanniocalcin from the corpuscles of Stannius (CS) and stimulated synthetic and releasing activities of the glands as measured in vitro. Pulse-chase experiments showed that stanniocalcin (STC) is a 56-kDa glycoprotein, processed from a 64-kDa precursor, prostanniocalcin (PSTC). PSTC and STC are homodimeric molecules that are readily split into monomers in the presence of reducing agents such as 2-mercaptoethanol. The monomeric form of PSTC and STC contains an approximately 5- to 6-kDa glycomoiety. Neither this sugar residue nor the NH2-terminal amino acid sequences of PSTC or STC proved to contain antigenic sites for the antiserum used in this study. Two-dimensional gel electrophoresis indicated the presence of several isoforms of PSTC and STC molecules that may reflect different stages of maturation of the (pro)hormone.
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17

Xiao, Li-Juan, Jin-Xiang Yuan, Xin-Xin Song, Yin-Chuan Li, Zhao-Yuan Hu, and Yi-Xun Liu. "Expression and regulation of stanniocalcin 1 and 2 in rat uterus during embryo implantation and decidualization." Reproduction 131, no. 6 (June 2006): 1137–49. http://dx.doi.org/10.1530/rep.1.01100.

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Stanniocalcin-1 (STC-1) is a recently discovered polypeptide hormone, while stanniocalcin-2 (STC-2) is a subsequently identified homologue of stanniocalcin-1. Although previous studies have shown that both STC-1 and -2 are involved in various physiological processes, such as ion transport, reproduction and development, their expression in the uterus and roles in implantation and early pregnancy are unclear. Here we have investigated the expression and regulation of both STC-1 and STC-2 in rat uterus during early pregnancy under various physiological conditions. We show that only basal levels of STC-1 and STC-2 mRNA were detected in the uterus from day one (D1) to day five (D5) of pregnancy. STC-2 immunostaining was gradually increased in the glandular epithelium from day two (D2), with a peak occurring on D5. High levels of both STC-1 and STC-2 mRNA were observed in the stoma cells at the implantation site on day six (D6) of pregnancy, whereas their immunostaining signals were also significant in the luminal epithelium. Basal levels of both STC-1 and STC-2 mRNA and STC-1 immunostaining were detected in the uterus with delayed implantation. After the delayed implantation was terminated by estrogen treatment, both STC-1 and STC-2 mRNA signals were significantly induced in the stroma underlying the luminal epithelium at the implantation site, and STC-2 immunostaining was also observed in the luminal epithelium surrounding the implanting blastocyst. Embryo transfer experiments further confirmed that STC-1 and STC-2 expression at the implantation sites was induced by the implanting blastocyst. Both STC-1 mRNA and immunostaining were seen in the decidualized cells from day seven (D7) to day nine (D9) of pregnancy. STC-2 mRNA was also found in the whole decidua from D7 to D9 of pregnancy; STC-2 protein, however, was strictly localized to the primary deciduas on D7 and D8, with a weak expression in the whole deciduas on D9. Consistent with the normal pregnancy process, strong STC-1 and STC-2 mRNA signals were detected in the decidualized cells under artificial decidualization, whereas only basal levels of STC-1 mRNA and immunostaining were observed in the control horn. These data suggest, for the first time, that STC-1 together with STC-2 may play important roles in the processes of implantation and decidualization in the rat.
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18

Paciga, Mark, Kathi James, J. Ryan J. Gillespie, and Graham F. Wagner. "Evidence for cross-talk between stanniocalcins." Canadian Journal of Physiology and Pharmacology 83, no. 11 (November 1, 2005): 953–56. http://dx.doi.org/10.1139/y05-055.

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There are 2 forms of stanniocalcin (STC) produced by the STC-1 gene; a 50 kDa polypeptide known as STC50 and a recently discovered group of higher molecular weight variants that are collectively referred to as big STC. Both have different tissue patterns of expression and different intracellular targeting pathways. STC50 functions locally in tissues such as muscle, liver, and kidney and is targeted to mitochondria. Big STC, on the other hand, is made by the ovaries. It signals both locally on nearby corpus luteal cells and systemically. Interestingly, however, receptor binding assays employing STC50 as the tracer have shown that the smaller ligand can bind equally to tissue receptors targeted by either form of the hormone. This suggests there may be cross-talk between ligands. The present study provides credence to this notion by demonstrating how the 2 hormones can compete for tissue receptors normally targeted by 1 form of the hormone (big STC). The results also reveal how STC50 can completely block the inhibitory effects of big STC on luteal cell progesterone release when added simultaneously. The findings therefore add credence to the possibility that there may be circumstances during which the 2 ligands functionally antagonize each other's actions.Key words: stanniocalcin (STC), STC50, big STC, receptor, antagonism, progesterone release.
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19

Lin, Shaojun, Qiaojuan Guo, Jiangmei Wen, Chao Li, Jin Lin, Xiaofei Cui, Nianli Sang, and Jianji Pan. "Survival analyses correlate stanniocalcin 2 overexpression to poor prognosis of nasopharyngeal carcinomas." Journal of Experimental & Clinical Cancer Research 33, no. 1 (2014): 26. http://dx.doi.org/10.1186/1756-9966-33-26.

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20

Yokobori, Takehiko, Koshi Mimori, Hideshi Ishii, Masaaki Iwatsuki, Fumiaki Tanaka, Yukio Kamohara, Keisuke Ieta, et al. "Clinical Significance of Stanniocalcin 2 as a Prognostic Marker in Gastric Cancer." Annals of Surgical Oncology 17, no. 10 (April 27, 2010): 2601–7. http://dx.doi.org/10.1245/s10434-010-1086-0.

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21

JELLINEK, Derek A., Andy C. CHANG, Martin R. LARSEN, Xin WANG, Phillip J. ROBINSON, and Roger R. REDDEL. "Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells." Biochemical Journal 350, no. 2 (September 1, 2000): 453. http://dx.doi.org/10.1042/0264-6021:3500453.

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22

JELLINEK, Derek A., Andy C. CHANG, Martin R. LARSEN, Xin WANG, Phillip J. ROBINSON, and Roger R. REDDEL. "Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells." Biochemical Journal 350, no. 2 (August 23, 2000): 453–61. http://dx.doi.org/10.1042/bj3500453.

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Stanniocalcin 1 (STC1) and stanniocalcin 2 (STC2) are two recently identified mammalian peptide hormones. STC1 plays a role in calcium and phosphate homoeostasis, while the role of STC2 is unknown. We examined a human fibrosarcoma cell line, HT1080, that has high steady-state STC1 and STC2 mRNA levels, to determine whether these proteins are secreted. Following incubation of HT1080 cells with 32P, labelled STC1 and STC2 were found to be secreted into the medium. STC1 was phosphorylated in vitro by protein kinase C (PKC). In vitro and in vivo phosphorylation both occurred exclusively on serine and the phosphopeptide maps were similar, suggesting that PKC might be the in vivo kinase. STC2 was phosphorylated in vitro by casein kinase II (CK2), in vitro and in vivo phosphorylation were exclusively on serine and the phosphopeptide maps were indistinguishable. Phosphorylation of STC2 in intact cells resulted from the action of an ecto-protein kinase, since exogenous STC2 was phosphorylated by HT1080 cells and no phosphorylated STC2 was detectable inside the cells. The ectokinase activity was abolished by heparin and GTP could substitute for ATP as the phosphate donor, indicative of an ecto-CK2-like activity. The in vitro CK2 phosphorylation site was shown by matrix-assisted laser-desorption ionization–time-of-flight MS to be a single serine located between Ser-285 and Ser-298 in the C-terminal region of STC2. This is the first report of the secretion of STC1 or STC2 from mammalian cells. We conclude that these human fibrosarcoma cells express both STC1 and STC2 as secreted phosphoproteins in vivo, with STC2 being phosphorylated by an ecto-CK2-like enzyme.
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23

Volland, Sonja, Wilfried Kugler, Lothar Schweigerer, Jörg Wilting, and Jürgen Becker. "Stanniocalcin 2 promotes invasion and is associated with metastatic stages in neuroblastoma." International Journal of Cancer 125, no. 9 (July 6, 2009): 2049–57. http://dx.doi.org/10.1002/ijc.24564.

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24

Chang, Andy C. M., Jeff Hook, Frances A. Lemckert, Michelle M. McDonald, Mai-Anh T. Nguyen, Edna C. Hardeman, David G. Little, Peter W. Gunning, and Roger R. Reddel. "The Murine Stanniocalcin 2 Gene Is a Negative Regulator of Postnatal Growth." Endocrinology 149, no. 5 (February 7, 2008): 2403–10. http://dx.doi.org/10.1210/en.2007-1219.

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Stanniocalcin (STC), a secreted glycoprotein, was first studied in fish as a classical hormone with a role in regulating serum calcium levels. There are two closely related proteins in mammals, STC1 and STC2, with functions that are currently unclear. Both proteins are expressed in numerous mammalian tissues rather than being secreted from a specific endocrine gland. No phenotype has been detected yet in Stc1-null mice, and to investigate whether Stc2 could have compensated for the loss of Stc1, we have now generated Stc2−/− and Stc1−/−Stc2−/− mice. Although Stc1 is expressed in the ovary and lactating mouse mammary glands, like the Stc1−/− mice, the Stc1−/−Stc2−/− mice had no detected decrease in fertility, fecundity, or weight gain up until weaning. Serum calcium and phosphate levels were normal in Stc1−/−Stc2−/− mice, indicating it is unlikely that the mammalian stanniocalcins have a major physiological role in mineral homeostasis. Mice with Stc2 deleted were 10–15% larger and grew at a faster rate than wild-type mice from 4 wk onward, and the Stc1−/−Stc2−/− mice had a similar growth phenotype. This effect was not mediated through the GH/IGF-I axis. The results are consistent with STC2 being a negative regulator of postnatal growth.
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25

Harper, Tod A., Aditya D. Joshi, and Cornelis J. Elferink. "Identification of Stanniocalcin 2 as a Novel Aryl Hydrocarbon Receptor Target Gene." Journal of Pharmacology and Experimental Therapeutics 344, no. 3 (December 26, 2012): 579–88. http://dx.doi.org/10.1124/jpet.112.201111.

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26

Tamura, Kenji, Mutsuo Furihata, Su-Yong Chung, Motohide Uemura, Hiroki Yoshioka, Tatsuo Iiyama, Shingo Ashida, et al. "Stanniocalcin 2 overexpression in castration-resistant prostate cancer and aggressive prostate cancer." Cancer Science 100, no. 5 (February 26, 2009): 914–19. http://dx.doi.org/10.1111/j.1349-7006.2009.01117.x.

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27

Law, Alice Y. S., Keng P. Lai, Carman K. M. Ip, Alice S. T. Wong, Graham F. Wagner, and Chris K. C. Wong. "Epigenetic and HIF-1 regulation of stanniocalcin-2 expression in human cancer cells." Experimental Cell Research 314, no. 8 (May 2008): 1823–30. http://dx.doi.org/10.1016/j.yexcr.2008.03.001.

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28

Law, Alice Y., Richard L. Hébert, Rania Nasrallah, Robert Langenbach, Chris K. C. Wong, and Graham F. Wagner. "Cyclooxygenase-2 mediates induction of the renal stanniocalcin-1 gene by arginine vasopressin." Molecular and Cellular Endocrinology 381, no. 1-2 (December 2013): 210–19. http://dx.doi.org/10.1016/j.mce.2013.07.008.

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29

Coulson-Gilmer, Camilla, Matthew P. Humphries, Sreekumar Sundara Rajan, Alastair Droop, Sharon Jackson, Alexandra Condon, Gabor Cserni, et al. "Stanniocalcin 2 expression is associated with a favourable outcome in male breast cancer." Journal of Pathology: Clinical Research 4, no. 4 (August 23, 2018): 241–49. http://dx.doi.org/10.1002/cjp2.106.

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Yuan, Qiong, Lin Zhan, Li-Li Zhang, Qiang Wang, Juan Liu, Zhen-Yu Jiang, Xia-Min Hu, and Xin-Chu Yuan. "Stanniocalcin 2 induces oxaliplatin resistance in colorectal cancer cells by upregulating P-glycoprotein." Canadian Journal of Physiology and Pharmacology 94, no. 9 (September 2016): 929–35. http://dx.doi.org/10.1139/cjpp-2015-0530.

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Multidrug resistance (MDR) limits the anticancer effects of chemotherapy in patients with metastatic colorectal cancer (CRC). Oxaliplatin is a common component of combinational therapeutic regimens administered to patients with metastatic CRC; however, it is also used as a constituent of adjuvant therapy for patients at a risk of recurrent disease. In the present study, we investigated the role of stanniocalcin 2 (STC2) in chemoresistance. STC2 knockdown sensitized chemoresistant CRC cells to oxaliplatin. Moreover, the expression of exogenous STC2 in chemonaïve CRC cells induced oxaliplatin resistance. We confirmed that STC2 upregulated P-glycoprotein (P-gp) expression in CRC cells. Furthermore, shRNA against phosphoinositide 3-kinase (PI3K) or Akt inhibited the action of STC2 on P-gp upregulation and MDR in CRC. To our knowledge, this is the first report to demonstrate the induction of oxaliplatin resistance in CRC cells in response to STC2 stimulation of P-gp via the PI3K/Akt signaling pathway.
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Yahata, Kensei, Kiyoshi Mori, Masashi Mukoyama, Akira Sugawara, Takayoshi Suganami, Hisashi Makino, Tetsuya Nagae, Yuriko Fujinaga, Yo-ichi Nabeshima, and Kazuwa Nakao. "Regulation of stanniocalcin 1 and 2 expression in the kidney by klotho gene." Biochemical and Biophysical Research Communications 310, no. 1 (October 2003): 128–34. http://dx.doi.org/10.1016/j.bbrc.2003.08.131.

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Frystyk, Jan, Enrique Teran, Mette Faurholdt Gude, Mette Bjerre, and Rikke Hjortebjerg. "Pregnancy-associated plasma proteins and Stanniocalcin-2 – Novel players controlling IGF-I physiology." Growth Hormone & IGF Research 53-54 (August 2020): 101330. http://dx.doi.org/10.1016/j.ghir.2020.101330.

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33

Law, Alice Y. S., and Chris K. C. Wong. "Stanniocalcin-2 is a HIF-1 target gene that promotes cell proliferation in hypoxia." Experimental Cell Research 316, no. 3 (February 2010): 466–76. http://dx.doi.org/10.1016/j.yexcr.2009.09.018.

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Law, Alice Y. S., and Chris K. C. Wong. "Stanniocalcin-2 promotes epithelial–mesenchymal transition and invasiveness in hypoxic human ovarian cancer cells." Experimental Cell Research 316, no. 20 (December 2010): 3425–34. http://dx.doi.org/10.1016/j.yexcr.2010.06.026.

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Staehler, Michael. "Editorial Comment on: Identification of Stanniocalcin 2 as Prognostic Marker in Renal Cell Carcinoma." European Urology 55, no. 3 (March 2009): 678. http://dx.doi.org/10.1016/j.eururo.2008.04.002.

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Na, Sang-su, Mark Borris Aldonza, Hye-Jin Sung, Yong-In Kim, Yeon Sung Son, Sukki Cho, and Je-Yoel Cho. "Stanniocalcin-2 (STC2): A potential lung cancer biomarker promotes lung cancer metastasis and progression." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1854, no. 6 (June 2015): 668–76. http://dx.doi.org/10.1016/j.bbapap.2014.11.002.

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Byun, Jong-Seon, Jae-Won Lee, Su Young Kim, Kwang Jun Kwon, Jong-Hee Sohn, Kyunyoung Lee, Dahlkyun Oh, Sung-Soo Kim, Wanjoo Chun, and Hee Jae Lee. "Neuroprotective effects of stanniocalcin 2 following kainic acid-induced hippocampal degeneration in ICR mice." Peptides 31, no. 11 (November 2010): 2094–99. http://dx.doi.org/10.1016/j.peptides.2010.08.002.

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38

Moore, E., R. Kuestner, D. Conklin, T. Whitmore, W. Downey, M. Buddle, R. Adams, et al. "Stanniocalcin 2: Characterization of the Protein and its Localization to Human Pancreatic Alpha Cells." Hormone and Metabolic Research 31, no. 07 (July 1999): 406–14. http://dx.doi.org/10.1055/s-2007-978764.

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Panagiotou, Grigorios, Athanasios D. Anastasilakis, Georgios Kynigopoulos, Elpida C. Skouvaklidou, Zacharias G. Saridakis, Jagriti Upadhyay, Eirini Pagkalidou, Aggeliki Apostolou, Thomai Karagiozoglou-Lampoudi, and Christos S. Mantzoros. "Physiological parameters regulating circulating levels of the IGFBP-4/Stanniocalcin-2/PAPP-A axis." Metabolism 75 (October 2017): 16–24. http://dx.doi.org/10.1016/j.metabol.2017.07.003.

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Li, Ji-Bin, Zhe-Xian Liu, Rui Zhang, Si-Ping Ma, Tao Lin, Yan-Xi Li, Shi-Hua Yang, Wan-Chuan Zhang, and Yong-Peng Wang. "Sp1 contributes to overexpression of stanniocalcin 2 through regulation of promoter activity in colon adenocarcinoma." World Journal of Gastroenterology 25, no. 22 (June 14, 2019): 2776–87. http://dx.doi.org/10.3748/wjg.v25.i22.2776.

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He, Huocong, Shuo Qie, Qiaojuan Guo, Shuyang Chen, Changyan Zou, Tianzhu Lu, Ying Su, et al. "Stanniocalcin 2 (STC2) expression promotes post-radiation survival, migration and invasion of nasopharyngeal carcinoma cells." Cancer Management and Research Volume 11 (July 2019): 6411–24. http://dx.doi.org/10.2147/cmar.s197607.

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ARIGAMI, TAKAAKI, YOSHIKAZU UENOSONO, SUMIYA ISHIGAMI, SHIGEHIRO YANAGITA, TAKAHIKO HAGIHARA, NAOTO HARAGUCHI, DAISUKE MATSUSHITA, et al. "Clinical significance of stanniocalcin 2 expression as a predictor of tumor progression in gastric cancer." Oncology Reports 30, no. 6 (October 1, 2013): 2838–44. http://dx.doi.org/10.3892/or.2013.2775.

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Ferreira do Carmo, Andreia, Mauricio Rocha Dourado, Carine Ervolino de Oliveira, Débora Campanella Bastos, Catherine Bueno Domingueti, Lívia Máris Ribeiro Paranaíba, Íris Sawazaki-Calone, et al. "Stanniocalcin 2 contributes to aggressiveness and is a prognostic marker for oral squamous cell carcinoma." Experimental Cell Research 393, no. 2 (August 2020): 112092. http://dx.doi.org/10.1016/j.yexcr.2020.112092.

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Jepsen, Malene R., Søren Kløverpris, Jakob H. Mikkelsen, Josefine H. Pedersen, Ernst-Martin Füchtbauer, Lisbeth S. Laursen, and Claus Oxvig. "Stanniocalcin-2 Inhibits Mammalian Growth by Proteolytic Inhibition of the Insulin-like Growth Factor Axis." Journal of Biological Chemistry 290, no. 6 (December 22, 2014): 3430–39. http://dx.doi.org/10.1074/jbc.m114.611665.

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Fazio, Elena N., Gabriel E. DiMattia, Sami A. Chadi, Kristin D. Kernohan, and Christopher L. Pin. "Stanniocalcin 2 alters PERK signalling and reduces cellular injury during cerulein induced pancreatitis in mice." BMC Cell Biology 12, no. 1 (2011): 17. http://dx.doi.org/10.1186/1471-2121-12-17.

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Feng, Linsen, Jianhua Ma, Haiming Ji, Yichun Liu, and Weixing Hu. "MiR-184 Retarded the Proliferation, Invasiveness and Migration of Glioblastoma Cells by Repressing Stanniocalcin-2." Pathology & Oncology Research 24, no. 4 (September 8, 2017): 853–60. http://dx.doi.org/10.1007/s12253-017-0298-z.

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Aydin, Hulya Ayik, Tayfun Toptas, Selen Bozkurt, Armagan Aydin, Gulgun Erdogan, Elif Pestereli, and Tayup Simsek. "Stanniocalcin-2 May Be a Potentially Valuable Prognostic Marker in Endometrial Cancer: a Preliminary Study." Pathology & Oncology Research 25, no. 2 (January 19, 2019): 751–57. http://dx.doi.org/10.1007/s12253-018-00576-y.

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Joshi, Aditya D., Ekram Hossain, and Cornelis J. Elferink. "Epigenetic Regulation by Agonist-Specific Aryl Hydrocarbon Receptor Recruitment of Metastasis-Associated Protein 2 Selectively Induces Stanniocalcin 2 Expression." Molecular Pharmacology 92, no. 3 (July 10, 2017): 366–74. http://dx.doi.org/10.1124/mol.117.108878.

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Meidan, Rina, Eyal Klipper, Yulia Zalman, and Ronit Yalu. "The role of hypoxia-induced genes in ovarian angiogenesis." Reproduction, Fertility and Development 25, no. 2 (2013): 343. http://dx.doi.org/10.1071/rd12139.

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Abstract:
The hypoxic microenvironment that occurs in fast-growing tissue such as the corpus luteum (CL) is a major contributor to its ability to survive via the induction of an intricate vascular network. Cellular responses to hypoxia are mediated by hypoxia-inducible factor-1 (HIF-1), an oxygen-regulated transcriptional activator. HIF-1, a heterodimer consisting of a constitutively-expressed β subunit and an oxygen-regulated α subunit, binds to the hypoxia responsive element (HRE) present in the promoter regions of responsive genes. This review summarises evidence for the involvement of hypoxia and HIF-1α in CL development and function. Special emphasis is given to hypoxia-induced, luteal cell-specific expression of multiple genes (vascular endothelial growth factor A (VEGFA), fibroblast growth factor 2 (FGF-2), prokineticin receptor 2 (PK-R2), stanniocalcin 1 (STC-1) and endothelin 2 (EDN-2) that participate in the angiogenic process during CL formation.
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López, José Javier, Isaac Jardín, Carlos Cantonero Chamorro, Manuel Luis Duran, María José Tarancón Rubio, Maria Reyes Panadero, Francisca Jiménez, et al. "Involvement of stanniocalcins in the deregulation of glycaemia in obese mice and type 2 diabetic patients." Journal of Cellular and Molecular Medicine 22, no. 1 (October 9, 2017): 684–94. http://dx.doi.org/10.1111/jcmm.13355.

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