Galectin-3 in urine of cancer patients: stage and tissue specificity
- 208 Downloads
Galectin-3 has been implicated in advanced stage of cancer disease. In the current study we examined the possibility of urinary galectin-3 levels to stage cancer disease and to follow up therapy.
Urine was collected from all types of cancer patients at different stages including patients undergoing radio/chemotherapy. Galectin-3 level was determined by anti-galectin-3 based ELISA and agglutination assays. Immunoblotting and purification on lactosyl affinity column further confirmed the presence of galectin-3.
Cancer samples exhibited stage dependent expression of galectin-3 approx. ranging from 1.0 to 3.3, 4.4 to 5.4, 5.4 to 24.7, 13.1 to 31.9, 13.9 to 32.9 ng/mg C (creatinine) for stage I–V, respectively, at P ~ <0.05 level. Galectin-3 levels were decreased by approx. threefolds after 5th day of therapy.
Sample collection being simple and non-invasive, urinary galectin-3 may be used as a potential diagnostic tool for monitoring or follow up of the stage of cancer disease.
KeywordsGalectin-3 Hemagglutination Creatinine Metastasis Radio/chemotherapy Urine
Authors thank Dr. V. Prakash, Director, CFTRI, for his keen interest in the work and encouragement. Authors are also thankful to Dr. S. G. Bhat, former Head, Dr. P. V. Salimath, current Head, Department of Biochemistry and Nutrition. SMD thank Department of Biotechnology, New Delhi, India and Department of Science and Technology, New Delhi, India for financial assistance. SMD and SUV acknowledges the financial assistance from Indian Council of Medical Research as Senior Research Fellowship to SUV.
- Bresalier RS, Yan PS, Byrd JC, Lotan R, Raz A (1997) Expression of the endogenous galactose-binding protein galectin-3 correlates with the malignant potential of tumors in the central nervous system. Cancer Res 80:776–787Google Scholar
- Herrmann J, Truck CW, Atchison RE, Huflej ME, Poulter L, Gitt MA et al (1993) Primary structure of the soluble lactose binding lectin L-29 from rat and dog and interaction of its non-collagenous proline, glycine, tyrosine rich sequence with bacterial and tissue collagenase. J Biol Chem 208:26704–26711Google Scholar
- Lotz MM, Andrews CW, Korzelins CA, Lee EC, Steele GD, Jrclarke A et al (1993) Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma. Proc Natl Acad Sci USA 90:3466–3470. doi:10.1073/pnas.90.8.3466 PubMedCrossRefGoogle Scholar
- Nangia-Makker P, Akahani S, Bresalier R, Raz A (2000) The role of galectin-3 in tumor metastasis. In: Lectins and pathology. Taylor and Francis Incorporation, LondonGoogle Scholar
- Song YK, Billiar TR, Lee YJ (2002) Am J Pathol 160:1069–1075Google Scholar
- Van den Brule FA, Castronovo V (2000) Laminin binding lectins during invasion and metastasis. In: Lectins and pathology. Taylor and Francis Inc., LondonGoogle Scholar