UNIVERSA MEDICINA
Univ Med 2025.
44:101-112
pISSN: 1907-3062 / eISSN: 2407-2230 DOI: https://doi.
org/10.
18051/UnivMed.
REVIEW ARTICLE
Galectin-3 and galectin-1 interactions in breast cancer therapy Vanitha Innocent Rani1 .
Aleti Lakshmi Manohari2 .
Uthamalingam Murali3 Mohd Imran4 .
Mary Anelia Correya5* .
Tamalika Chakraborty6 .
Preenon Bagchi7 , and Gunamoni Das8 Department of Community & Psychiatric Nursing.
Faculty of Nursing.
King Khalid University.
Mahayil.
Asir Region.
Saudi Arabia Department of Biochemistry.
Balvir Singh Tomar Institute of Medical Sciences and Research.
Jaipur.
Rajasthan.
India Department of General Surgery.
Manipal University College Malaysia.
Melaka.
Malaysia Department of Pharmaceutical Chemistry.
College of Pharmacy.
Northern Border University.
Rafha.
Saudi Arabia Center for Health Research.
Northern Border University.
Arar 73213.
Saudi Arabia *Department of Pathology.
Sree Balaji Medical College and Hospital.
Chennai.
India Department of Life Sciences Guru Nanak Institute of Pharmaceutical Science and Technology.
Kolkata.
West Bengal.
India Department of Computer Science.
Madhav University.
Bharja.
Abu Road.
Pindwara.
Rajasthan.
India Programme of Botany.
Faculty of Science.
Assam down town University.
Guwahati.
Assam.
India * Correspondence Author:
maryaneliacorreya598@gmail.
Date of first submission.
February 25, 2025 Date of final revised submission.
April 7, 2025 Date of acceptance.
April 17, 2025 Cite this article as: Rani VI.
Manohari AL.
Murali U.
Imran M.
Correya MA.
Chakraborty T.
Bagchi P.
Das G.
Galectin-3 and galectin-1 interactions in breast cancer therapy.
Univ Med 2025.
44:101-112
ABSTRACT
Galectins, a family of -galactoside-binding proteins, play critical roles in tumor progression, angiogenesis, and immune evasion, making them significant therapeutic targets in cancer treatment.
By binding -galactosidecontaining glycoconjugates, galectins modulate immune responses, apoptosis, and tumor development.
The increasing recognition of their oncogenic roles has led to the development of carbohydrate- and peptide-based inhibitors that competitively bind to the carbohydrate recognition domain (CRD), disrupting galectin-mediated immune evasion.
T-cell apoptosis, and angiogenesis.
Given their intricate functions in the tumor microenvironment, a comprehensive evaluation of galectin inhibitors is warranted.
This review synthesizes recent advancements in galectin-targeted therapies, including their mechanisms of action, efficacy in preclinical models, and potential synergy with chemotherapeutic agents and monoclonal antibodies.
Despite promising developments, challenges remain in optimizing treatment regimens, overcoming resistance mechanisms, and identifying predictive biomarkers for patient stratification.
Patient stratification, based on molecular or genetic profiles, is essential for enhancing therapeutic efficacy and ensuring personalized treatment approaches.
systematic literature search .
4Ae2.
was conducted using Google Scholar.
ProQuest.
Science Direct, and Scopus databases, with key terms including galectin inhibitors, cancer therapy, tumor microenvironment, immune evasion, and targeted therapy.
This review highlights the role of galectin-1 and galectin-3 in breast cancer therapy, emphasizing their impact on tumor progression, immune modulation, and resistance to conventional treatments.
Further translational research is necessary to refine clinical applications, optimize combination strategies, and establish biomarkers that enhance the integration of galectin inhibitors into existing treatment paradigms.
Keywords: Galectins, cancer therapy, galectin inhibitors, tumor microenvironment, immune evasion, personalized treatment Copyright@Author.
- https://univmed.
org/ejurnal/index.
php/medicina/article/view/1712 Rani VI.
Manohari AL.
Murali U, et al
INTRODUCTION
Cancers of the stomach, colon, prostate, breasts, and lungs are the most common malignancies worldwide.
Breast cancer is the most common cause of cancer-related mortality, tracheal, lung, and malignancies make up the bulk of cancer-related .
The incidence of colorectal cancer fatalities has more than doubled in the last 30 .
Lifestyle factors such as diet, lack of physical activity, and obesity contribute to an increase in colorectal cancer diagnoses, but the overall survival rate remains low.
Public health initiatives and early detection can reduce colorectal cancer prevalence, while genetic abnormalities such as breast cancer 1, early onset (BRCA.
and breast cancer 2, early onset (BRCA.
increase breast cancer risk, accounting for 25% of cases.
Similarly.
CDH1 mutations affect cell adhesion, contributing to cancer spread and metastasis.
Genetic vulnerabilities and family history can significantly influence the likelihood and aggressiveness of breast cancer, emphasizing the need for personalized screening and prevention strategies due to these genetic and .
Healthcare recommend early breast cancer screenings and genetic counseling for individuals with a family history of tumors or with known gene mutations, enabling informed decision-making about preventive measures.
Breast cancer risk is significantly influenced by DNA repair gene mutations, such as CHEK2.
BRIP1, and ATM, which interact with BRCA1 and BRCA2 pathways, leading to impaired DNA repair mechanisms, increased susceptibility to cancerous changes, genomic instability, tumor progression, and therapeutic resistance.
Genetic testing and personalized medicine have advanced to understand genetic risks, with galectin-3, a betagalactoside-binding protein, playing a significant role in breast cancer progression and .
Galectin-3, a key player in cell adhesion, migration, and immune response, is linked to increased metastatic potential in breast cancer, making it a promising biomarker for advanced disease.
The role of galectin-3 in the cellular stress response and apoptosis resistance complicates treatment outcomes, highlighting the need for personalized intervention strategies in breast cancer management.
This review aimed to explore and summarize the recent scientific findings on the interactions of galectin-3 and galectin-1 with key signaling pathways, tumor microenvironment components, and their crosstalk with immune cells, epithelialmesenchymal transition (EMT), and extracellular matrix remodeling in breast cancer.
Galectin-3, a key cancer cell survival factor, regulates autophagy, antioxidant defenses, and hypoxiainducible factor-1 (HIF-.
stability under metabolic stress.
It interacts with Beclin-1, preventing apoptosis and enhancing autophagic Under hypoxic conditions, galectin-3
HIF-1
angiogenesis and metabolic adaptation.
High Gal3 expression correlates with poor prognosis and resistance to therapy, making it a potential biomarker for personalized treatment.
This review summarizes 11 years of research on galectin-3's effects on tumor progression, metastasis, therapeutic targeting in breast cancer, that was retrieved from various sources, including Science Direct.
PubMed.
Nature, and Biomedicine.
Research methods A systematic search was conducted on electronic databases such as PubMed.
Science Direct, and Google Scholar to find English publications on galectin-3 and galectin-1 interactions in breast cancer therapy.
Fifty publications were selected from 230, excluding duplicates and non-compliant articles (Figure .
The selected articles were analyzed and reviewed (Table .
A member of the galectin family that has been extensively examined is galectin-3, which was initially discovered as a 32 kDa antigen on the surfaces of murine macrophages,.
has a key immune cell function and has gained significant research due to its unique structure and functional Its N-terminal part has 14 amino acid repetitions, while its C-terminal part has a single carbohydrate recognition domain (CRD).
This suggests a specialized cell signaling and molecular Galectin-3's oligomerization upon ligand binding enhances its interactions with other cellular components, increasing its role in cellular communication and allowing it to engage in various pathways.
QuinckeAos disease, a rare clinical disorder Figure 1.
Flow chart of selection of publications Table 1.
Studies on galectin-3 and its role in breast cancer progression, diagnosis, and therapeutics Study type/methodology Reference Key focus area Cao et al.
Global cancer burden trends Breast cancer Secondary analysis Morgan et al.
Cancer incidence GLOBOCAN data Adebayo et al.
Cancer treatments Review Nathan et al.
TP53 mutations in CDH1 mutations & Molecular study PTEN tumor suppressor function Review Bashar & Begam .
Aitchison et al.
Parsons .
Review Case study Key findings Rising cancer Breast cancer surpassing lung Projected increase in Future therapeutic Mutational impact on tumor growth Genetic predisposition PTEN-PI3K-AKT Potential application in Background on cancer burden Cancer Cancer trends & Galectin-3 in colorectal cancer Genetic factors linked to galectin-3 Role of mutations in cancer Connection to galectin-3 function Rani VI.
Manohari AL.
Murali U, et al Rashidi et al.
Singh et al.
Boutas et al.
Hara et al.
Di Gregoli et al.
Ahmed et al.
Wang et al.
Capone et al.
Miller et al.
Ernur, 2024 .
Guo et al.
, 2020 .
Suthahar.
Setayesh et al.
Pang.
Breast disease risk Breast cancer Galectin-3 in breast Galectin-3 as a Comparative study Galectin-3 & Galectin-3 Galectin-3 & HIV Experimental study Galectin-3 binding Targeting galectin-3 Review Serum galectin-3 in breast cancer Galectin-3 & tumor Galectin-3 in Galectin-3 in liver Survey Systematic review Review Pharmaceutical Cellular study Drug study Clinical study Activation/inhibition Experimental study Overexpression in HCC Scholarly Research Study Explores ligand binding and cancer Identifies galectinmediated bacterial Confirms necessity of full-length galectin-3 for binding Galectin-1 as a molecular target in Nuclear translocation of galectin-3 independent of carbohydrate binding Combination with lncRNA HOTAIR improves diagnosis Higher expression in squamous cell Galectin-3 regulates EMT via AMPK/TGF- Role of galectins in multiple cancers Review Kim et al.
Non-classical role of Experimental study Li et al.
Diagnostic value of galectin-3 in thyroid Clinical study Pokharel et al.
Galectin-3 in lung Clinical study Galectin-3 and Translational Chang et al.
Impact on tumor Allosteric modulation Scholarly Research Goud et al.
Role in Therapeutic Membrane lipid raft Experimental study Experimental study Wu et al.
Association with Early disease Pre-/post-op level Impact on metabolism Galectin-3-ligand interaction and cancer cell behavior Galectin-2 interactions with Full-length galectin3 in microbial Sasaki et al.
Risk factors for Gaps in awareness Experimental study Breast cancer Public health Core discussion on galectin-3 in cancer Diagnostic potential of Immune response in cancer Potential treatment targeting galectin-3 Mechanistic insights on galectin-3 binding Galectin-3Aos role in Drug discovery Biomarker potential Tumor growth and Broader implications of Role in Supports 'Ligand Affinity of galectin3' Provides insight into galectin-3Aos structural makeup Helps explain ligand affinity and tumor progression Supports 'Galectin3 Throughout Cancer' Supports 'The Structural Makeup of galectin-3' Supports potential clinical applications Supports 'Growth of Tumors due to galectin-3' Explains galectin-3 in tumor QuinckeAos disease, a rare clinical disorder Srejovic et al.
Mayo et al.
Dimitrijevic et Galectin-3 in immune responses Structural interactions in Galectin-3 in Immunology study Biochemical study Review Modulates T-cellmediated Phosphorylationdependent interaction with N-terminal tail Highlights complex galectin-3 interactions in pancreatic cancer Overexpression in Regulates tumor cell and macrophage Regulates endothelial functions in tumor Examines glycan interactions with Setayesh et al.
Galectin-3 in liver Experimental study Wan et al.
Galectin-3 in tumor Experimental study Thijssen.
Role of Galectins in Review Hoffmann et al.
Galectin-3 binding to TF-antigen Glycoconjugate Grazier et al.
Galectins in breast cancer metastasis Review Role of galectin-3 in cancer spread Abourehab et al.
Chondroitin sulfatebased biomaterials Materials Explores biomedical applications of glycan Moure et al.
Protein binding to NMR spectroscopy Reveals selective binding epitopes Immunology study Impacts T-cell development and Immunology study Identifies protective glycan epitopes Camptothecin nanoformulations in cancer treatment Systematic Review Improved efficacy of camptothecin through nano-drug delivery Lipophilic Salirasib analogs and tumor Experimental Study Vicente et al.
Sendid et al.
Ghanbari-Movahed et al.
Ballari et al.
Pang et al.
Aldabaan .
Funkhouser et al.
Glycans and immune system Mannan immune response and Galectins Transcriptomic analysis of tocotrienols in EMT reversal in TNBC by Tocotrienol Genetic mutations and galectin-3 levels in breast cancer Experimental Study Scholarly Research Study Correlation Analysis Enhanced activity of Salirasib Identifies molecular changes in treated with -Tocotrienol inhibits EMT and androgen receptor expression Links genetic mutations to galectin3 expression in breast Links galectin-3 to cancer-related immune responses Supports 'The Structural Makeup of Galectin-3' Supports 'Galectin3 Throughout Cancer' Supports 'Growth of Tumors due to Galectin-3' Supports 'Galectin3 Throughout Cancer' Supports tumor Supports 'Ligand Affinity of Galectin-3' Supports 'Growth of Tumors due to Galectin-3' Provides insights into galectin-3based therapeutics Supports 'Ligand Affinity of Galectin-3' Links galectin-3 to immune system Supports Galectin-3 in immune Provides insights into targeted drug Potential role of galectin-3 in modulating tumor Explains galectin-3 involvement in tumor response to Supports role of galectin-3 in Demonstrates galectin-3's structural influence on cancer growth Rani VI.
Manohari AL.
Murali U, et al Iwamoto et al.
Galectin-3 phosphorylation in Chen et al.
Tim-3/Galectin-9 in T-cell function and cervical carcinoma Vrbata et al.
Mechahougui et Markalunas et al.
Glycopolymers as inhibitors of Advances in Genetic mutations and galectin-3 in breast cancer Experimental Study Immunology Study Medicinal Chemistry Study Review Correlation Analysis Galectin-3, a soluble S-type lectin, is primarily present in the cytoplasm and released extracellularly through non-classical mechanisms.
It bypasses the conventional secretion pathway, allowing it to quickly respond to cellular signals and influence cell behavior at multiple levels.
Being a surface localized protein, galectin-3 is essential for cell-environment interactions and regulation of processes such as inflammation, apoptosis, cell division, and immunological Its involvement in these processes may be linked to cancer progression and immune modulation, highlighting its versatility in both intracellular and extracellular communication.
This multifunctional protein influences membrane dynamics, cell signaling, and tissue remodeling, thereby impacting health and disease.
It plays a significant role in tumor development and metastasis, particularly in cancer biology.
Galectin-3's binding properties make it a potential target for therapeutic interventions.
Its structural flexibility allows it to adapt to various molecular partners, amplifying its regulatory impact.
Understanding galectin-3's roles may provide insights into new therapeutic strategies for managing cancer, inflammation, and immune .
Galectin-3 is the only chimera-type galectin with a C-terminal CRD and flexible N-terminal domain for oligomerization.
Galectins can dimerize and interact with glycopeptides at each CRD,.
identifying carbohydrates, particularly N-acetyllactosamine residues, influenced by glycosylation in glycoproteins and glycans.
Galectin-3 modulates E-cadherin downregulation and tumor metastasis Galectin-3 interactions affect immune evasion in Development of galectin-3 inhibitors Discusses biomarkerbased cancer Reinforces galectin3's structural and functional role in Supports galectin3's role in EMT and Highlights galectin3's role in tumor Highlights ligandbinding potential of Supports role of galectin-3 in precision medicine Supports structural and ligand-binding Ligand affinity of galectin-3 Galectin-3's interactions with cellular glycans, including matrix and cell surface glycoproteins, suggest it may play a crucial role in cellular communication and signaling pathways, opening new therapeutic research avenues.
Galectin-3 interacts with growth factor receptors and integrins, regulating tumor cell adhesion, migration, and invasion, highlighting its role in cancer metastasis and enhancing or reducing integrin activity.
Galectin-3's interaction with CD98 on the cell membrane initiates integrin-mediated cell attachment, influencing cancer progression and therapeutic It also interacts with EGFR in lung CL1-5 cells, increasing EGFR .
Galectin-3, a bacterial glycan binder, plays a crucial role in promoting hematogenous metastasis by stabilizing tumor cells within the vascular system.
Targeting galectin-3 can prevent cancer cell spread to new .
Galectin-3's functional versatility and role in immune responses against microbial infections, including interactions with diverse glycans, may relate to inflammatory conditions and identify Neisseria .
The mechanism of galectin-3 interaction with microbial glycans remains unclear, but is crucial for understanding host-pathogen modulation, as well as for developing targeted antimicrobial therapies.
Galectin-3 fusion proteins have potential for cancer treatment, offering personalized treatments through medication delivery and imaging in theranostics, highlighting their potential in precision medicine.
QuinckeAos disease, a rare clinical disorder Growth of breast cancer due to galectin-3 Overexpression of galectin-3, often found in malignancies such as breast cancer, may serve as a biomarker for cancer diagnosis and prognosis, as demonstrated in human papillary thyroid .
Galectin-3's potential role in cancer cell survival, particularly in breast cancer, is evident in its ability to inhibit apoptosis and to cause a serum-independent growth of cDNAtransfected normal thyroid follicular cells.
Galectin-3's resistance indicates its ability to promote cancer cell proliferation, including breast cancer, through various molecular pathways, including its interaction with K-Ras at the plasma .
Galectin-3 plays a crucial role in cancer signaling cascades, promoting tumor It increases cyclin D and c-MYC production through -catenin interaction, accelerating cell division and causing aggressive Understanding these mechanisms could lead to new therapeutic targets and treatments for galectin-3-related cancers, including breast Interventions targeting galectin-3's role in cell cycle progression could also be explored.
Serum-independent in aggressive cancers such as breast cancer can lead to new ways of retarding tumor growth and spread.
By halting galectin3interactions, targeted medicines could be developed, focusing on specific cancer cell This could reduce side effects associated with broad-spectrum treatments and be a major advancement in cancer therapy (Figure .
Galectin-3-induced apoptosis Galectin-3, a member of the lectin family, can either stimulate or inhibit apoptosis, depending on its location inside the cell.
This lectin facilitates the movement of the annexin family member to the mitochondria by binding to synexin in the cytoplasm and prevents apoptosis in cells by preventing cytochrome C release.
Its apoptotic activity may be due to interaction with Nucling Galectin-3 is involved in growth, adhesion, proliferation, and apoptosis.
Being a protein in tumor cells, this lectin is a diagnostic marker for differentiated thyroid carcinoma due to its high expression and its ability to promote cellular transformation, suppress apoptosis, and increase cell viability through pro-survival .
Figure 2.
Roles of galectin-3 in breast cancer progression, metastasis, apoptosis, molecular pathways, and targeted therapies Rani VI.
Manohari AL.
Murali U, et al Galectin-3 in breast cancer metastasis and Tumor cells can spread by penetrating endothelium and entering lymphatic or circulatory systems, complicating treatment and leading to poorer prognoses.
Overexpression of galectin-3 improves cell-ECM adhesion and encourages tumor cell migration.
Galectin-3 enhances tumor cell invasiveness by promoting aggregation in circulation and avoiding anoikis during It also increases cancer cell adherence to endothelial cells by interacting with surface glycans such as MUC1 and Gal1-3GalNAc-.
Oncofetal antigens, produced during fetal development, are crucial for cancer prognosis, diagnosis, and therapeutic monitoring, enhancing patient care and treatment personalization.
Galectin-3, through binding with integrins and activating focal adhesion kinase (FAK), ,significantly influences neovascularization, stimulating angiogenesis by controlling VEGF and FGF, and accelerating this process through interaction with aminopeptidase N (CD.
Galectin-3 is crucial for cell aggregation, tumor angiogenesis, and cancer spread.
It triggers angiogenesis and metastasis in various cancers.
Galectin-3's role in tumor-endothelial cell interactions and early metastasis interactions is External Thomsen-Friedenreich (TF) antigen could inhibit galectin-3-mediated tumor .
Galectin-3-TF interactions could be a promising therapeutic strategy for aggressive cancers, limiting tumor proliferation and reducing metastatic potential.
Functions of galectins in glycan biology The Golgi apparatus, which contains glycosyltransferases, plays a role in posttranslational modification of glycoproteins, and the N-glycan content in SKBR-3 breast cancer cells reduces doxorubicin sensitivity.
The glycocalyx, a structural barrier in cancer cells, can evade therapeutic targeting, highlighting the complexity of cancer treatment.
When treated with tunicamycin, glycocalyx cells were less responsive to mitogenic growth factors and more sensitive to doxorubicin, suggesting potential targets for improved treatment outcomes.
Glycan degradation decreases cell adhesion, potentially limiting cancer spread.
The glycocalyx regulates integrin activity, guiding integrins to adhesion sites and forming a barrier across epithelial cells.
Structural integrity is crucial for maintaining epithelial cell cohesion, which can impact tumor progression.
Galectins and glycans interact through complex mechanisms, such as oligomeric structure and multivalency.
Galectin-3 plays a role in T-cell activation, possibly by interacting with N-glycans on T-cell receptors (TCR).
MGAT5, a branching enzyme, influences immune receptor accessibility and activation potential, limiting TCR clustering.
Glycan structure influences immune cell responsiveness and autoimmunity.
Galectin-3 prevents IL-5 production and interacts with pathogen glycans, promoting antigenic properties in macrophages.
eradicates Candida albicans by binding to 1-2 oligomannosyl residues.
Studies on genetically engineered mice deficient in certain galectins highlight their importance in the innate immune response to microbial infections, offering potential therapeutic targets for infectious disease control.
GalectinAc3 as a therapeutic target Galectin inhibitors, such as G3-C12, have shown promising results in preclinical research, preventing breast cancer cells from spreading to the lungs in athymic nude mice.
Recent research has successfully inhibited metastasis in mucin-secreting breast cancer cells using a highaffinity antibody.
Salirasib, a derivative of salicylic acid, is being studied as a potential galectin inhibitor, which prevents farnesylated Ras activation and Ras isoform aggregation in cancer cells.
Tocotrienol, a natural vitamin E variant, may enhance the anticancer effects of tocotrienol in metastatic breast cancer cells due to its hydrophobic and hydrophilic properties.
tocotrienol significantly induces apoptosis and hinders metastasis in breast cancer cell lines by inhibiting processes such as epithelial-tomesenchymal transition (EMT), lipid raft stability, and invasion, while minimizing normal mammary epithelial cell survival.
MDA-MB-231 human breast cancer cells produce large, metastatic polyploid cancer cells, which can be reduced by antioxidant therapy due to decreased mitochondria and reactive oxygen species levels.
Galectin-3's function in the biology of breast Galectin-1 increases Foxp3 Treg cells in breast cancer tumors, aiding immune evasion and modulating immune tolerance.
It interacts with neuropilin-1 to initiate signaling pathways, stimulating hepatic stellate cell migration and .
Galectin-1 promotes tumor growth and invasion, while galectin-3 prevents human QuinckeAos disease, a rare clinical disorder breast cancer cells from apoptosis due to nitric Galectin-3's role in tumor cell survival and cancer persistence may be linked to chemotherapy Its knockdown in breast cancer cells improves treatment efficacy, suggesting it could be a target for enhancing treatment efficacy in resistant cancers.
Galectin-3 disrupts cell Galectin-9, an anti-tumor and tumor-promoting protein, may cause apoptosis in colon cancer by increasing receptor tyrosine kinase phosphorylation, suppressing the immune system, and causing death.
Galectin-9's interaction with immune cells makes it a promising target for immunotherapy, potentially suppressing or boosting immune responses in cancer treatment, while galectins are intriguing candidates for therapeutic suppression.
Inhibitors of galectin Galectin inhibitors, discovered decades ago, are being researched to slow or halt cancer growth and spread.
Two main types are carbohydratesbased and non-carbohydrate-based, designed to mimic natural sugar-binding sites for targeted interactions with galectins.
Thiodigalactoside, a carbohydrate-based inhibitor of galectin-1, has shown promise in mouse models of breast cancer by causing apoptosis and reducing tumor development and .
Research shows that reducing angiogenesis by means of anginex, a peptidebased inhibitor of galectin-1, can impede tumor growth and cell proliferation, potentially slowing or reversing cancer spread.
Modified citrus pectin, a carbohydrate-based inhibitor, targets galectin-3 and has antimetastatic properties, preventing metastasis and enhancing T-cell immune These findings highlight the importance of these inhibitors in cancer treatment.
Galectin inhibitors are being studied in clinical trials, both alone and in combination with chemotherapeutic medications or monoclonal antibodies, to maximize effectiveness and reduce side effects, a strategy influenced by genetargeting therapies.
Olaparib targets specific gene mutations, demonstrating precision medicine's potential for better patient outcomes.
Alpelisib is approved for breast cancer treatment in PIK3CA mutant breast cancer.
AlpelisibAos approval highlights genetic marker-based cancer treatment.
A phase I clinical trial tested the galectin-1 and -3 inhibitor GM-CT- 01 in advanced solid tumors, including breast cancer, to evaluate disease impact and chemotherapy response.
The trial demonstrates the potential of galectin inhibitors in integrating into existing treatment regimens, potentially leading to new therapeutic protocols.
The ATM inhibitor AZD1930 and a galectin-9 inhibitor showed synergistic properties in a mouse model, allowing for better-targeted therapy and personalized treatment, potentially improving patient survival and quality of life.
CONCLUSION
Galectin inhibitors are promising in cancer therapeutics, targeting angiogenesis, metastasis, and immune surveillance.
Both carbohydratebased and peptide-based inhibitors show potential in preclinical models.
However, challenges remain in optimizing dosing strategies, understanding resistance mechanisms, and identifying biomarkers.
Future research should focus on elucidating pathways, refining inhibitor development, and conducting larger trials to establish safety and efficacy.
Acknowledgement The authors extend their appreciation to the Deanship of Scientific Research at Northern Border University.
Arar.
KSA for fundi ng this research work through the project number "NBUFFR-2025-2043-05Ay.
Author Contributions VIR and ALM were responsible for the conception and design of the study.
contributed to the acquisition of data.
MI and MAC were involved in the analysis and interpretation of data, as well as drafting the Critical revisions were made by VIR and MAC.
All authors have read and approved the final manuscript.
Ethical Statement and Informed Consent Not applicable.
Data Availability Statement There were no new data generated, data sharing is not applicable.
Conflict of Interest The authors declare that no conflicts exist.
Rani VI.
Manohari AL.
Murali U, et al Financial Disclosure The authors declared no financial support.
Declaration the Use of AI in Scientific Writing Nothing to declare.
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