Galectin-3

Source: Wikipedia, the free encyclopedia.
LGALS3
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Ensembl

ENSG00000131981

ENSMUSG00000050335

UniProt

P17931

P16110

RefSeq (mRNA)

NM_001177388
NM_002306
NM_001357678

NM_001145953
NM_010705

RefSeq (protein)

NP_002297
NP_001344607

n/a

Location (UCSC)Chr 14: 55.12 – 55.15 MbChr 14: 47.61 – 47.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Galectin-3 is a protein that in humans is encoded by the LGALS3 gene.[5][6] Galectin-3 is a member of the lectin family, of which 14 mammalian galectins have been identified.[7][8]

Galectin-3 is approximately 30 kDa and, like all galectins, contains a carbohydrate-recognition-binding domain (CRD) of about 130 amino acids that enable the specific binding of β-galactosides.[7][9][10][11]

Galectin-3 (Gal-3) is also a member of the beta-galactoside-binding protein family that plays an important role in

cell-cell adhesion, cell-matrix interactions, macrophage activation, angiogenesis, metastasis, apoptosis
.

Galectin-3 is encoded by a single gene, LGALS3, located on chromosome 14, locus q21–q22.

nucleus, cytoplasm, mitochondrion, cell surface, and extracellular space.[7][9][10]

Function

Galectin-3 has an affinity for

beta-galactosides and exhibits antimicrobial activity against bacteria and fungi.[8]

This

heart disease, and stroke.[7][11][13][14] Studies have also shown that the expression of galectin-3 is implicated in a variety of processes associated with heart failure, including myofibroblast proliferation, fibrogenesis, tissue repair, inflammation, and ventricular remodeling.[13][15][16]

Galectin-3 associates with the

congenital polycystic kidney disease.[17]

The functional roles of galectins in cellular response to membrane damage are rapidly expanding.[18][19][20] It has recently shown that Galectin-3 recruits ESCRTs to damaged lysosomes so that lysosomes can be repaired.[19]

Clinical significance

Fibrosis

A correlation between galectin-3 expression levels and various types of fibrosis has been found. Galectin-3 is upregulated in cases of liver fibrosis, renal fibrosis, and idiopathic pulmonary fibrosis (IPF). In several studies with mice deficient in or lacking galectin-3, conditions that caused control mice to develop IPF, renal, or liver fibrosis either induced limited fibrosis or failed to induce fibrosis entirely.[21][22][23] Companies have developed galectin modulators that block the binding of galectins to carbohydrate structures. The galectin-3 inhibitor, TD139 and GR-MD-02 have the potential to treat fibrosis.[23]

Cardiovascular disease

Elevated levels of galectin-3 have been found to be significantly associated with higher risk of death in both acute decompensated heart failure and chronic heart failure populations.

myocardium.[26]

Galectin-3 also may be used as a

ischaemic origin and elevated galectin-3 levels may benefit from statin treatment.[27] Galectin-3 has also been associated as a factor promoting ventricular remodeling following mitral valve repair, and may identify patients requiring additional therapies to obtain beneficial reverse remodeling.[28]

Cancer

The wide variety of effects of galectin-3 on

therapeutic agents
for cancer treatment.

chemoattraction, apoptosis, immunosuppression, angiogenesis, adhesion, invasion and metastasis.[29]

Galectin-3

tumour cell's evasion of the immune system. Galectin-3 also helps promote angiogenesis.[29]

The roles of galectins and galectin-3, in particular, in cancer have been heavily investigated.[30] Of note, galectin-3 has been suggested to play important roles in cancer metastasis.[31]

Clinical applications

Cardiovascular risk indicator

Chronic heart failure has been found to be indicated by a galectin-3 tests, using the ARCHITECT immunochemistry platform developed by BG Medicine and marketed by Abbott, helping to determine which patients are most at risk for the disease. This test is also offered on the VIDAS platform marketed by bioMérieux.[32] Pecta-Sol C binds to galectin-3 binding sites on the surfaces of cells as a preventative measure created by Isaac Eliaz in conjunction with EcoNugenics.[33]

Galectin-3 is

fibrogenesis. A study concluded that pharmacological inhibition of galectin-3 attenuates cardiac fibrosis, LV dysfunction, and subsequent heart failure development.[34]

Drug development

nonalcoholic steatohepatitis (NASH) and for increasing the effectiveness and reducing side effects of cancer immunotherapy.[37][38][39]

Biomarkers

Galectin-3 is increasingly being used as a diagnostic marker for different cancers. It can be screened for and used as a prognostic factor to predict the progression of the cancer. Galectin-3 has varying effects in different types of cancer.[40] One approach to cancers with high galectin-3 expression is to inhibit galectin-3 to enhance treatment response.[41]

Interactions

LGALS3 has been shown to

interact with LGALS3BP.[42][43][44]

In melanocytic cells LGALS3 gene expression may be regulated by MITF.[45]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000131981 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000050335 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  8. ^ a b "Entrez Gene: LGALS3 lectin, galactoside-binding, soluble, 3".
  9. ^
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  32. ^ Ross, D. "Abbott's Galectin-3 Test Provides Doctors in Europe with New Tool for Assessing the Prognosis of Chronic Heart Failure Patient". Retrieved 28 November 2013.
  33. ^ Brechka N (2009). "Putting the Squeeze on Cancer". Retrieved 28 November 2013. {{cite journal}}: Cite journal requires |journal= (help)
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  36. ^ "Galectin Therapeutics' Preclinical Data Published in PLOS ONE Show Its Galectin Inhibitors Reverse Cirrhosis and Significantly Reduce Fibrosis and Portal Hypertension". Globe Newswire. Retrieved 28 November 2013.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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