Increased Circulating Levels of Galectin Proteins in Patients with Breast, Colon, and Lung Cancer

• Type of Material: Article
• Authors: Bailey B Blair, University of South Carolina; Avery T Funkhouser, University of South Carolina; Jane L Goodwin, University of South Carolina; Alexander M Strigenz, University of South Carolina; Basil H Chaballout, University of South Carolina; Julie C Martin, Prisma Health Cancer Institute; Christopher Ronald Funk, Emory University; Connie Arthur, Emory University; Jeffrey W Edenfield, Prisma Health Cancer Institute; Anna Blenda, Emory University
• Language: English
• Date: 2021-10-01
• Publisher: MDPI
• Publication Version: Final Published Version
• Copyright Statement: © 2021 by the authors.
• License: Creative Commons Attribution 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.3390/cancers13194819
• Title of Journal or Parent Work: CANCERS
• Volume: 13
• Issue: 19
• Grant/Funding Information: This research was funded by the Prisma Health Cancer Institute Philanthropy Grant and Sargent Foundation. The APC was funded by the Biomedical Sciences Department at the University of South Carolina School of Medicine Greenville and Prisma Health Cancer Institute.
• Keywords: Life Sciences & Biomedicine; ADHESION; galectin; THERAPY; ELISA; cancer; CYTOKINES; biorepository; METASTASIS; Oncology; colon; BIOMARKER; TUMOR; breast; Science & Technology; EXPRESSION; lung
• Research Categories: Health Sciences, Pathology; Health Sciences, Oncology

Abstract

Galectins are proteins with high-affinity β-galactoside-binding sites that function in a variety of signaling pathways through interactions with glycoproteins. The known contributions of galectins-1,-3,-7,-8, and-9 to angiogenesis, metastasis, cell division, and evasion of immune de-struction led us to investigate the circulating levels of these galectins in cancer patients. This study compares galectin concentrations by enzyme-linked immunosorbent assay (ELISA) from each stage of breast, lung, and colon cancer. Galectins-1 and-7, which share a prototype structure, were found to have statistically significant increases in breast and lung cancer. Of the tandem-repeat galectins, galectin-8 showed no statistically significant change in these cancer types, but galectin-9 was increased in colon and lung cancer. Galectin-3 is the only chimera-type galectin and was increased in all stages of breast, colon, and lung cancer. In conclusion, there were significant differences in the galectin levels in patients with these cancers compared with healthy controls, and galectin levels did not significantly change from stage to stage. These findings suggest that further research on the roles of galectins early in disease pathogenesis may lead to novel indications for galectin inhibitors.