Abstract
Galectins, the glycan-binding family of lectins, have been known to mediate a multitude of biological functions with the help of their unique ‘sugar-sensing’ carbohydrate recognition domain (CRD). They read and decipher glycan coded information systematically patterned over the cellular surface and regulate growth, development, cell–cell and cell–matrix interactions, vascularization, apoptosis, and many other physiologically relevant processes. The ‘hallmarks of cancer’ include ten, biologically distinctive, yet complementary, characteristics manifested within tumour cells in a multistep cascade process during carcinogenesis. They armour the tumour cells with ability to evade immunogenic response along with growth suppressors, resist apoptosis, promote angiogenesis, trigger genomic instability and inflammation and reprogram cellular metabolomics, thereby conferring invasiveness and replicative immortality, eventually leading to the metastatic spread of the tumour. Aberrant glycosylation in transformed cells plays a defining role in dictating the biological and clinical outcome of each of these hallmarks. By taking control of an array of physiological and immunological cellular processes during different stages of cancer, Galectins meticulously mould the prognostic behaviour of the transformed cells, and hence are identified as effective biomarkers for disease diagnosis and potential targets for therapeutic intervention in cancer. Targeting Galectins or their cognate glycoconjugate partners with specific inhibitors, alone or in combination with existing methods of treating cancer, provides a promising vision in designing effectual next-generation therapeutics for cancer treatment in the near future.
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Abbreviations
- CAF:
-
Cancer associated fibroblast
- CLRs:
-
C-type lectin receptors
- CRC :
-
Colorectal cancer
- CRD :
-
Carbohydrate recognition domain
- CSC:
-
Cancer stem cells
- CTD:
-
C-terminal domain
- DCs:
-
Dendritic cells
- EC :
-
Endothelial cells
- ECM:
-
Extracellular matrix
- EMT:
-
epithelial-to-mesenchymal transition
- HNSCC:
-
Head and neck squamous cell carcinoma
- LacNAc:
-
N-acetyllactoseamine
- MCAM:
-
Melanoma cell adhesion molecule
- MCP:
-
Modified citrus pectin
- MDSC:
-
Myeloid derived suppressor cells
- MMP:
-
Matrix metalloproteinase protein
- NLS:
-
Nuclear localization signal
- OSCC:
-
Oral squamous cell carcinoma
- RCC:
-
Renal cell carcinoma
- TAM:
-
Tumour-associated macrophage
- TDG:
-
Thiodigalactoside
- TF:
-
Thomson–Freidenreich
- TIL:
-
Tumour infiltrating lymphocyte
- TME:
-
Tumour microenvironment
- TN:
-
Triple negative
- VEGF:
-
Vascular endothelial growth factor
- VEGFR:
-
Vascular endothelial growth factor receptor
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Acknowledgements
Authors would like to thanks Mr. Kiran B. Lokhande, Senior Research Fellow and Mr. Sayan Bose for their help in figure preparation. Authors would like to thanks Ms. Parija P. Phadanvis for her help in finalizing the references. Dr. Amit Ranjan would like to thank Dr. Rajiv Kalraiya, PI, TMC, ACTREC, Navi Mumbai who passed away in 2015, for his guidance and warm support.
Conflict of Interest
The authors declare no conflict of interest.
Financial Support
Dr. Rajesh Kumar Gupta would like to acknowledge the Department of Science and Technology-Science and Engineering Research Board (DST-SERB), Government of India under ECRA scheme [grant number ECR/2016/001187] and Dr. D.Y. Patil Vidyapeeth (Deemed to be University) [grant numbers DPU/106/18/2015, DPU/17/2016] for financial support. Dr. Amit Ranjan would like to acknowledge Dr. D.Y. Patil Vidyapeeth (Deemed to be University) [grant number DPU/12/2016] for financial support.
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Nandi, S. et al. (2021). Lectins in Health and Diseases: Galectins and Cancer. In: Elumalai, P., Lakshmi, S. (eds) Lectins. Springer, Singapore. https://doi.org/10.1007/978-981-16-7462-4_11
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