Human Galectin-8 Isoforms and Cancer

Overview

Journal Glycoconj J

Publisher Springer

Specialties Biochemistry
Endocrinology

Date 2004 Feb 6

PMID 14758080

Citations 40

Authors

Nathalie Bidon-Wagner

Jean-Paul Le Pennec

Affiliations

Soon will be listed here.

Abstract

Galectins are animal lectins that can specifically bind beta-galactosides. Thirteen galectins have already been described. This review focuses on a specific member of this family: galectin-8. This galectin was discovered in prostate cancer cells eight years ago and has been studied extensively in the last few years. The galectin-8 gene ( LGALS8) encodes numerous mRNAs by alternate splicing and the presence of three unusual polyadenylation signals. These mRNAs encode six different isoforms of galectin-8: three belong to the tandem-repeat galectin group (with two CRDs linked by a hinge peptide) and three to the prototype group (with one CRD). Various studies showed that galectin-8 is widely expressed in tumor tissues as well as in normal tissues. The level of galectin-8 expression may correlate with the malignancy of human colon cancers and the degree of differentiation of lung squamous cell carcinomas and neuro-endocrine tumors. Recently, the differences in galectin-8 expression levels between normal and tumor tissues have been used as a guide for the selection of strategies for the prevention and treatment of lung squamous cell carcinoma. These experiments are still under investigation, but demonstrate the potential of galectin-8 research to enhance our understanding of, and possibly prevent, the process of neoplastic transformation.

Citing Articles

Galectin-8N-Selective 4-Halophenylphthalazinone-Galactals Double π-Stack in a Unique Pocket.

van Klaveren S, Hassan M, Hakansson M, Johnsson R, Larsson J, Jakopin Z ACS Med Chem Lett. 2024; 15(8):1319-1324.

PMID: 39140038 PMC: 11318003. DOI: 10.1021/acsmedchemlett.4c00212.

The role of galectins in mediating the adhesion of circulating cells to vascular endothelium.

Souchak J, Mohammed N, Lau L, Dimitroff C Front Immunol. 2024; 15:1395714.

PMID: 38840921 PMC: 11150550. DOI: 10.3389/fimmu.2024.1395714.

Inhibition of sugar-binding activity of Galectins-8 by thiogalactoside (TDG) attenuates secondary brain damage and improves long-term prognosis following intracerebral hemorrhage.

Song J, Bai H, Chen S, Xing Y, Lou J Heliyon. 2024; 10(9):e30422.

PMID: 38737270 PMC: 11088311. DOI: 10.1016/j.heliyon.2024.e30422.

Sex Differences in Cochlear Transcriptomes in Horseshoe Bats.

Wu J, Duan C, Lan L, Chen W, Mao X Animals (Basel). 2024; 14(8).

PMID: 38672325 PMC: 11047584. DOI: 10.3390/ani14081177.

Significance of the Galectin-8 Immunohistochemical Profile in Ovarian Cancer.

Avadanei E, Caruntu I, Amalinei C, Pavaleanu I, Giusca S, Rusu A Biomedicines. 2024; 12(2).

PMID: 38397905 PMC: 10887174. DOI: 10.3390/biomedicines12020303.

References

Gopalkrishnan R, Roberts T, Tuli S, Kang D, Christiansen K, Fisher P . Molecular characterization of prostate carcinoma tumor antigen-1, PCTA-1, a human galectin-8 related gene. Oncogene. 2000; 19(38):4405-16. DOI: 10.1038/sj.onc.1203767. View

Nagy N, Bronckart Y, Camby I, Legendre H, Lahm H, Kaltner H . Galectin-8 expression decreases in cancer compared with normal and dysplastic human colon tissue and acts significantly on human colon cancer cell migration as a suppressor. Gut. 2002; 50(3):392-401. PMC: 1773143. DOI: 10.1136/gut.50.3.392. View

Danielsen E, van Deurs B . Galectin-4 and small intestinal brush border enzymes form clusters. Mol Biol Cell. 1997; 8(11):2241-51. PMC: 25705. DOI: 10.1091/mbc.8.11.2241. View

Bassen R, Brichory F, Caulet-Maugendre S, Bidon N, Delaval P, Desrues B . Expression of Po66-CBP, a type-8 galectin, in different healthy, tumoral and peritumoral tissues. Anticancer Res. 2000; 19(6B):5429-33. View

Desrues B, Brichory F, Lena H, Bourguet P, Delaval P, Toujas L . Treatment of human lung carcinoma xenografts with a combination of 131I-labelled monoclonal antibody Po66 and doxorubicin. Cancer Immunol Immunother. 1996; 43(5):269-74. PMC: 11037616. DOI: 10.1007/s002620050333. View

Bourguet P, Dazord L, Desrues B, Collet B, Ramee M, Delaval P . Immunoscintigraphy of human lung squamous cell carcinoma using an iodine-131 labelled monoclonal antibody (Po66). Br J Cancer. 1990; 61(2):230-4. PMC: 1971389. DOI: 10.1038/bjc.1990.43. View

Gorski J, Liu F, Artigues A, Castagna L, Osdoby P . New alternatively spliced form of galectin-3, a member of the beta-galactoside-binding animal lectin family, contains a predicted transmembrane-spanning domain and a leucine zipper motif. J Biol Chem. 2002; 277(21):18840-8. DOI: 10.1074/jbc.M109578200. View

Hadari Y, Paz K, Dekel R, Mestrovic T, Accili D, Zick Y . Galectin-8. A new rat lectin, related to galectin-4. J Biol Chem. 1995; 270(7):3447-53. DOI: 10.1074/jbc.270.7.3447. View

Drickamer K . Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem. 1988; 263(20):9557-60. View

10.

Gitt M, Colnot C, Poirier F, Nani K, Barondes S, Leffler H . Galectin-4 and galectin-6 are two closely related lectins expressed in mouse gastrointestinal tract. J Biol Chem. 1998; 273(5):2954-60. DOI: 10.1074/jbc.273.5.2954. View

11.

Desrues B, Lena H, Brichory F, Ramee M, Toujas L, Delaval P . Monoclonal antibody Po66 uptake by human lung tumours implanted in nude mice: effect of co-administration with doxorubicin. Br J Cancer. 1995; 72(5):1076-82. PMC: 2033938. DOI: 10.1038/bjc.1995.468. View

12.

Hughes R . Mac-2: a versatile galactose-binding protein of mammalian tissues. Glycobiology. 1994; 4(1):5-12. DOI: 10.1093/glycob/4.1.5. View

13.

Desrues B, Collet B, Rame M, Bourel D, Bourguet P, Martin A . Distribution of radiolabelled monoclonal antibody Po66 after intravenous injection into nude mice bearing human lung cancer grafts. Cancer Immunol Immunother. 1989; 30(5):295-9. PMC: 11038156. DOI: 10.1007/BF01744897. View

14.

Leffler H, Masiarz F, Barondes S . Soluble lactose-binding vertebrate lectins: a growing family. Biochemistry. 1989; 28(23):9222-9. DOI: 10.1021/bi00449a039. View

15.

Cho M, Cummings R . Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis. J Biol Chem. 1995; 270(10):5207-12. DOI: 10.1074/jbc.270.10.5207. View

16.

Danguy A, Rorive S, Decaestecker C, Bronckart Y, Kaltner H, Hadari Y . Immunohistochemical profile of galectin-8 expression in benign and malignant tumors of epithelial, mesenchymatous and adipous origins, and of the nervous system. Histol Histopathol. 2001; 16(3):861-8. DOI: 10.14670/HH-16.861. View

17.

Ahmed H, Vasta G . Galectins: conservation of functionally and structurally relevant amino acid residues defines two types of carbohydrate recognition domains. Glycobiology. 1994; 4(5):545-8. DOI: 10.1093/glycob/4.5.545. View

18.

Hadari Y, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y . Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis. J Cell Sci. 2000; 113 ( Pt 13):2385-97. DOI: 10.1242/jcs.113.13.2385. View

19.

Bidon N, Brichory F, Thomas D, Cavalier A, Caulet-Maugendre S, Bourguet P . Sodium butyrate induces growth inhibition and modulates galectin-8 expression in human lung carcinoma cells. Anticancer Res. 2001; 21(2A):1049-55. View

20.

Hughes R . The galectin family of mammalian carbohydrate-binding molecules. Biochem Soc Trans. 1998; 25(4):1194-8. DOI: 10.1042/bst0251194. View