rs4652

This is a protein-altering variant in the LGALS3 gene.

Research that mentions this SNP (2)

Genetic Variants in the Vicinity of LGALS‐3 Gene and LGALS‐3 mRNA Expression in Advanced Carotid Atherosclerosis: An Exploratory Study
AssociationN=785Ana Djordjevic et al.(2016)· Journal of Clinical Laboratory Analysis

This case-control study of 785 Serbian subjects (485 advanced carotid atherosclerosis patients, 300 controls) examined two genetic variants in the LGALS-3 gene (rs2274273 and rs17128183) for association with carotid atherosclerosis risk and LGALS-3 mRNA expression. No statistically significant associations were found between either variant and advanced carotid atherosclerosis or plaque phenotypes (all p > 0.0125 after Bonferroni correction). However, rare allele carriers of both variants showed significantly higher LGALS-3 mRNA expression in carotid plaque tissue (p = 0.039), suggesting these variants may affect gene expression despite lacking association with disease risk.

Traits studied:advanced carotid atherosclerosiscarotid plaque phenotypes
A galectin‐3 sequence polymorphism confers TRAIL sensitivity to human breast cancer cells
FunctionalNachman Mazurek et al.(2011)· Cancer

A galectin-3 sequence polymorphism (rs4644, P64H) influences TRAIL sensitivity in breast cancer cells. The His64 variant confers TRAIL sensitivity through PTEN upregulation and PI3K/Akt pathway inactivation, while the Pro64 variant results in TRAIL resistance. This functional finding suggests the polymorphism could explain disparities in breast cancer outcomes across populations.

Traits studied:Breast cancerDoxorubicin sensitivityTRAIL sensitivity

About LGALS3

This gene encodes a member of the galectin family of carbohydrate binding proteins. Members of this protein family have an affinity for beta-galactosides. The encoded protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. This protein can self-associate through the N-terminal domain allowing it to bind to multivalent saccharide ligands. This protein localizes to the extracellular matrix, the cytoplasm and the nucleus. This protein plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion and T-cell regulation. The protein exhibits antimicrobial activity against bacteria and fungi. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Oct 2014]

View all LGALS3 variants →

Gene information from NCBI Gene. Variant classifications from ClinVar.

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