THE EFFECT OF GALECTİN-3 ON APOPTOSİS
Vol 1, Issue 1, 2019, Article identifier:
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Abstract
Cancer is a disease caused by changes in the critical genes that control cell proliferation, differentiation, survival and apoptosis. Apoptotic cell death is an important mechanism and target for the anti-cancer treatment. A characteristic finding in many types of cancer is a reduction in apoptosis. Galectin-3 (Gal-3) is a pleiotropic lectin that plays an important role in cell proliferation, adhesion, differentiation, angiogenesis, and apoptosis. Therefore, synthetic galectin-3 inhibitors are of utmost importance for development of new antitumor therapeutic strategies. Galectin-3 is mainly found in the cytoplasm, also seen in the nucleus and can be secreted by non-classical, secretory pathways. In general, secreted galectin-3 mediates cell migration, cell adhesion and cell–cell interactions through the binding with high affinity to galactose-containing glycoproteins on the cell surface. Cytoplasmic galectin-3 exhibits anti-apoptotic activity and regulates several signal transduction pathways, whereas nuclear galectin-3 has been associated with premRNA splicing and gene expression. During the past decade, extensive progress has been made toward understanding the molecular basis for the regulation of apoptosis. In this review, we have focused on the role of galectin-3 in tumor metastasis with special emphasis on apoptosis.
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Referances
Song J, Liu H, Li Z, et al. Cucurbitacin I inhibits cell migration and invasion and enhances chemosensitivity in colon cancer. Oncol Rep 2015; 33: 1867–1871.
Pratima Nangia-Makker · Susumu Nakahara, Victor Hogan · Avraham Raz, Galectin-3 in apoptosis, a novel therapeutic target, J Bioenerg Biomembr (2007) 39:79–84)
Akyol S. Over Kanserinde Sıcak Şok Proteinleri (HSP) ve Progesteron Reseptörleri (PR). Bakırköy Tıp Dergisi 2009; 5: 83–91.
Al-Henhena N, Khalifa SA, Ying RP, et al. Evaluation of chemopreventive potential of Strobilanthes crispus against colon cancer formation in vitro and in vivo. BMC Complement Altern Med 2015; 15(1): 419.
Wu MS, Lien GS, Shen SC, et al. N-acetyl-L-cysteine enhances fisetin-induced cytotoxicity via induction of ROSindependent apoptosis in human colonic cancer cells. Mol Carcinog 2014; 53: E119–E129.
Alam S, Pal A, Kumar R, et al. Nexrutine inhibits azoxymethane-induced colonic aberrant crypt formation in rat colon and induced apoptotic cell death in colon adenocarcinoma cells. Mol Carcinog 2016; 55: 1262–1274.
Ontikatze T, Rudner J, Handrick R, et al. Dihydroartemisinin is a hypoxia-active anti-cancer drug in colorectal carcinoma cells. Front Oncol 2014; 4: 116.
Kamil Vural, Funda Kosova, Feyzan Özdal Kurt and İbrahim Tuğlu, In vitro investigation of the effect of matrix molecules on the behavior of colon cancer cells under the effect of geldanamycin derivative, Tumor Biology October 2017: 1–8.
Watson A.J.M.,Apoptosis and colorectal cancer. Gut 2004; 53:1701–1709.
He X., Dong Y., Wah Wu C., Zhao Z., Simon S.M., Chan F.K.L., Sung J., and Yu J. MicroRNA–218 Inhibits Cell Cycle Progression and Promotes Apoptosis in Colon Cancer by Downregulating BMI1 Polycomb Ring Finger Oncogene. Molecular Medicine, 2012; 18: 1491–1498.
Akpınar G., Kolon kanserinde apoliprotein e (apo e) gen poliferizminin araştırılması.(Doktora Tezi), Kocaeli Üniversitesi;2006.
Duranyıldız D.,Oğuz H., Çamlıca H.,Yasasever V., Topuz E. Malign Melanomalı Hastalarda Serum BCL-2 düzeyleri. Türk Onkoloji Dergisi, 2004;19: 4,131–133
Kosova F, Kasar Z, Tuglu I, Ozdal Kurt F, Gok S, Ari Z, Imren T, Apoptosis of colon cancer cells under the effect of geldanamycin derivate, Bratisl Med J 2017; 118 (5), 288 – 291
Lee I, Lee SJ, Kang TM, Kang WK, Park C., Unconventional role of the inwardly rectifying potassium channel Kir2.2 as a constitutive activator of RelA incancer, Cancer Res. (2012 Dec 26). [E
Boligan K.F., Mesa C., Fernandez L.E., von Gunten S.: Cancer intelligence acquired (CIA): tumor glycosylation and sialylation codes dismantling antitumor defense. Cell. Mol. Life Sci. 72, 1231–1248 (2015)
Vanessa Leiria Campo, Marcelo Fiori Marchiori, Lílian Cataldi Rodrigues, Marcelo Dias-Baruffi, Synthetic glycoconjugates inhibitors of tumor-related galectin-3: an update, Glycoconj J (2016) 33:853–876
Hockl P.F., Wolosiuk A., Sáez J.M., Bordoni A.V., Croci D.O., Terrones Y.T., Illia G.J., Rabinovich G.A.: Glyco-nano-oncology: Novel therapeutic opportunities by combining small and sweet. Pharmacol. (2016). doi:10.1016/j.phrs.2016.02.005
Arthur, C. M.; Baruffi, M. D.; Cummings, R. D.; Stowell, S. R.: Galectins: methods and protocols. Stowell, S. R.; Cummings, R. D. (eds.); human press, Vol. 1, Chapter 1, pp 1–35 (2015)=).
Liu-cheng Li, Jun Li, and Jian Gao, Functions of Galectin-3 and Its Role in Fibrotic Diseases, J Pharmacol Exp Ther 351:336–343, November 2014
Tsogt-Ochır Dondoo, Tomoharu Fukumorı, Keı Daızumoto, Tomoya Fukawa, Mıho Kohzukı, Mınoru Kowada, Yoshıto Kusuhara, Hıdehısa Morı, Hıroyoshı Nakatsujı, Masayukı Takahashı And Hıro-Omı Kanayama. Galectin-3 Is Implicated in Tumor Progression and Resistance to Anti-androgen Drug Through Regulation of Androgen Receptor Signaling in Prostate Cancer, ANTICANCER RESEARCH 37: 125-134 (2017).
Hughes RC (1994) Mac-2: a versatile galactose-binding protein of mammalian tissues. Glycobiology 4:5–12.
Henderson NC, Mackinnon AC, Farnworth SL, Poirier F, Russo FP, Iredale JP, Haslett C, Simpson KJ, and Sethi T (2006) Galectin-3 regulates myofibroblast activation and hepatic fibrosis. Proc Natl Acad Sci USA 103:5060–5065.
Yang RY, Hsu DK, and Liu FT (1996) Expression of galectin-3 modulates T-cell growth and apoptosis. Proc Natl Acad Sci USA 93:6737–6742.
Wang L, Inohara H, Pienta KJ and Raz A. (1995). Biochem. Biophys. Res. Commun., 217, 292–303.
Ste´phane Califice, Vincent Castronovo, Marc Bracke and Fre´de´ ric van den Bruˆ le*, Dual activities of galectin-3 in human prostate cancer: tumor suppression of nuclear galectin-3 vs tumor promotion of cytoplasmic galectin-3, Oncogene (2004) 23, 7527–7536
Sonja A. Selemetjev · Svetlana B. Savin · Ivan R. Paunovic · Svetislav B. Tatic · Dubravka Cvejic, Changes in the expression pattern of apoptotic molecules (galectin-3, Bcl-2, Bax, survivin) during progression of thyroid malignancy and their clinical significance, Wien Klin Wochenschr (2015) 127:337–344.
Takenaka Y, Fukumori T, Yoshii T, Oka N, Inohara H, Kim HR, Bresalier RS and Raz A. (2004). Nuclear export of phosphorylated galectin-3 regulates its antiapoptotic activity in response to chemotherapeutic drugs. Mol. Cell Biol., 24, 4395–4406.
Yu F, Finley Jr RL, Raz A and Kim HR. (2002). Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation. J. Biol. Chem., 277, 15819–15827.
Akahani S, Nangia-Makker P, Inohara H, Kim HR and Raz A. (1997). Galectin-3: a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family. Cancer Res., 57, 5272–5276.
Moon BK, Lee YJ, Battle P, Jessup JM, Raz A and Kim HR. (2001). Galectin-3 protects human breast carcinoma cells against nitric oxide-induced apoptosis: implication of galectin-3 function during metastasis. Am. J. Pathol., 159, 1055–1060.
Matarrese P, Fusco O, Tinari N, Natoli C, Liu FT, Semeraro ML, Malorni W and Iacobelli S. (2000a). Galectin-3 overexpression protects from apoptosis by improving cell adhesion properties. Int. J. Cancer, 85, 545–554.
Kawachi K, Yoshifumi M, Yonezawa S, Nakano S, Shirao K, Natsugoe S, et al. Galectin-3 expression in various thyroid neoplasms and its possible role in metastasis formation. Hum Pathol. 2000;31:428–33.
Deveraux QL, Reed JC. IAP family proteins—suppressors of apoptosis. Genes Dev. 1999;13:239–52.
Mita AC, Mita MM, Nawrocki ST, Giles FJ. Survivin: key regülatör of mitosis and apoptosis and novel target for cancer therapeutics. Clin Cancer Res. 2008;14:5000–5.
Waligórska-Stachura J, Jankowska A, Was´ko R, Liebert W, Biczysko M, Czarnywojtek A, et al. Survivin-prognostic tumor biomarker in human neoplasms-review. Ginekol Pol. 2012;83:537–40.
Tirrò E, Consoli ML, Massimino ML, Manzella L, Frasca F, Sciacca L, et al. Altered expression of c-IAP1, survivin, and Smac contributes to chemotherapy resistance in thyroid cancer cells. Cancer Res. 2006;66:4263–72.
Ito Y, Yoshida H, Uruno T, Nakano K, Miya A, Kobayashi K, et al. Survivin expression is significantly linked to the dedifferentiation of thyroid carcinoma. Oncol Rep. 2003;10:1337–40.
Hafiz Ahmed and Dina M. M. AlSadek, Galectin-3 as a Potential Target to Prevent Cancer Metastasis, Clinical Medicine Insights: Oncocology 2015:9, 113-121
DOI: http://dx.doi.org/10.18063/ctr.v1i1.614
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