Abstract
The diagnostic and therapeutic potential of Maackia amurensis agglutinin (MAA) have been reported in various malignancies. Earlier, we have found that MAA specifically interacted with human non-small cell lung-cancer (NSCLC) cells and induced apoptosis in these cells. The present study was designed to identify M. amurensis leukoagglutinin (MAL-I, one of the components of MAA, having the same carbohydrate specificity as MAA) interacting membrane sialoglycoprotein(s) of two subtypes of human NSCLC cell lines. Nine proteins were identified using two-dimensional (2D)-polyacrylamide gel electrophoresis (PAGE) followed by MAL-I-overlay transblotting and matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS). Among these proteins, HSP60 was selected for further characterization. The sialoglycoprotein nature of membrane-HSP60 of NSCLC cell lines was confirmed by its reduced reactivity with MAL-I in Western blots in the presence of GM2 and by dual staining of the cell lines with MAL-I and HSP60-antibody. These findings were further substantiated by enzymatic analysis of membrane-HSP60 as well as in-silico evidence regarding this protein. Our observations were validated by immunohistochemical analysis of both subtypes of NSCLC tissue sections. Membrane-HSP60 was found to be involved in the inhibition of MAL-I-induced morphological alteration of NSCLC cells and also in the proliferation and migration of these cells, indicating the probable role of sialylated membrane-HSP60 in this disease.
Highlights
Lung cancer is one of the major causes of cancer-a ssociated deaths worldwide (Bray et al, 2018)
The representative two-dimensional (2D)-polyacrylamide gel electrophoresis (PAGE) profiles of the membrane proteins of non-small cell lungcancer (NSCLC) cell lines are shown in Figure 2B (I and V)
Several MAL-I interacting proteins in the respective representative transblots were found to be highlighted in the molecular weight (Mr) range of 20–100 kDa and the isoelectric point range of 4 .5–6.8, as depicted in Figure 2B (II and VI)
Summary
Lung cancer is one of the major causes of cancer-a ssociated deaths worldwide (Bray et al, 2018). The prevalence of this disease is increasing in developing countries including India (Parikh et al, 2016). Sialylation is a hallmark of cancer cells. Aberrant sialylation of cellular glycoconjugates were shown to modulate different cellular processes associated with tumorigenesis (Isaji et al, 2019). Altered sialylation has been detected in various epithelial cancers (Ma et al, 2016; Munkley and Scott, 2019). The carbohydrate specific biomolecules, have been used to predict such altered patterns of glycosylation in cancer (Singh et al, 2019). Several lectins were shown to have anticancer properties (Yau et al, 2015; Ribeiro et al, 2018)
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