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

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 destruction 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.

Overcoming Microenvironment-Mediated Chemoprotection through Stromal Galectin-3 Inhibition in Acute Lymphoblastic Leukemia

“…Our knock out experiments of Gal3 in the stromal cells provided proof-of-principle that a reduction in Gal3 (activity) with its origin in the stromal cells would be beneficial, for example in reducing the chance of persistence of MRD in the induction chemotherapy phase of treatment of BCP-ALL. However, Gal3 is a relatively abundant protein, and ng/mL amounts have been measured in BCP-ALL bone marrow plasma [12], as well as in the serum and plasma of patients with carcinomas (for example, [52]). We note that the knockout of Gal3 in stroma, as studied here, permanently eliminates production of stromal galectin-3, whereas pharmacological galectin-3 inhibition is temporary.…”

Modulation of the Gal-9/TIM-3 Immune Checkpoint with α-Lactose. Does Anomery of Lactose Matter?

“…It is a potent inducer of cancer cell death in lymphomas and other malignant cell types, such as prostate cancer cells [ 121 ] and colon cancer [ 122 ]. However, Gal-9 is a complex and fragile molecule, with a largely expressed plasma membrane form [ 123 ], an intracellular form [ 124 ] and a circulating soluble form [ 125 ]. The expression and secretion of Gal-9 is promoted by interferon β and γ [ 126 ].…”

Galectin-3 as a Novel Multifaceted and Not Only Cardiovascular Biomarker in Patients with Psoriasis with Regard to Systemic Treatment—Preliminary Data

“…The plasticity of galectins and their wide distribution in tissues (not only in the cytoplasm and nuclei but also in the extracellular space) makes them extremely interesting for research but also clinical usability. Many galectins take part in cancers’ invasiveness, and have been related with higher rates of metastases and poorer survival outcome in different cancers [ 11 , 18 ]. Galectin-7 has been linked not only with lung cancer, but also with being highly expressed in epithelial tissues, and related to the regulation of skin homeostasis or keratinocytes proliferation [ 18 , 19 ].…”

“…Many galectins take part in cancers’ invasiveness, and have been related with higher rates of metastases and poorer survival outcome in different cancers [ 11 , 18 ]. Galectin-7 has been linked not only with lung cancer, but also with being highly expressed in epithelial tissues, and related to the regulation of skin homeostasis or keratinocytes proliferation [ 18 , 19 ]. Chen et al demonstrated that galectin-7 mRNA was downregulated in human psoriatic lesions and a IL-23-induced psoriasis model that proves the role of the lectin in pathogenesis of psoriasis [ 19 ].…”