LGALS13 Human
Description
Immunomodulation in Pregnancy
PP13 regulates immune tolerance at the maternal-fetal interface:
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Neutrophil Polarization: Promotes a "tumor-permissive" neutrophil phenotype by reducing apoptosis, upregulating PD-L1, and increasing production of HGF, TNF-α, ROS, and MMP-9 .
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T Cell Regulation: Inhibits T cell activation in the decidua, supporting placental growth .
Vasodilation and Placental Growth
PP13 induces endothelial nitric oxide and prostaglandin signaling, lowering blood pressure in pregnant animals . This mechanism is linked to its potential therapeutic use in preeclampsia .
Preeclampsia Biomarker
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Mechanisms: Reduced GCM1 and ESRRG transcription factors in preterm preeclampsia suppress LGALS13 expression. Epigenetic methylation may further impair PP13 synthesis .
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Limitations: Late-second-trimester PP13 levels alone lack predictive value for preeclampsia, necessitating integration with angiogenic factors (e.g., sFlt-1) .
Gestational Diabetes Mellitus (GDM)
PP13 serum levels rise in early second trimester but decline in term placentas, suggesting dysregulated inflammatory pathways .
Tissue-Specific Expression
Evolutionary Conservation
PP13 expression patterns are conserved in anthropoid primate placentas, highlighting its adaptive role in longer gestations .
Neutrophil Modulation by PP13
Therapeutic Applications
Product Specs
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN
Q&A
FAQs for Researchers on LGALS13 (Galectin-13) in Human Academic Research
Advanced Research Questions
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How do LGALS13 promoter polymorphisms (−98A/C) influence gene regulation?
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The −98A allele reduces promoter activity by 13–26% compared to −98C in trophoblast-like cells (BeWo), as shown by luciferase reporter assays .
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Experimental design: Transfect cells with promoter-reporter constructs (e.g., pGL3-basic vector) and measure activity under differentiation (e.g., forskolin treatment) to mimic placental development .
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What evolutionary mechanisms drove LGALS13 emergence in primates?
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LGALS13 evolved via LINE-mediated rearrangements in a galectin gene cluster on chromosome 19, unique to anthropoid primates. Phylogenetic analysis of 24 sequences across 10 species reveals amino acid substitutions in the CRD, suggesting functional diversification .
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Key data:
Species Group LGALS13 Presence Expression Pattern Old World monkeys Present Placental-specific New World monkeys Absent N/A Non-primate mammals Absent N/A
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How can LGALS13 variants be functionally validated in preeclampsia models?
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Step 1: Genotype maternal cfDNA for −98A/C and exon 3 variants (e.g., 221delT) using nested PCR and Sanger sequencing .
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Step 2: Use CRISPR/Cas9 to introduce variants into trophoblast organoids and assess invasion capacity or cytokine secretion (e.g., IL-10, TNF-α) .
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Confounding factors: Address population-specific allele frequencies (e.g., −98A/A prevalence in Black cohorts) and epigenetic modifiers like DNA methylation .
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Methodological Challenges and Solutions
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How to resolve contradictions in LGALS13’s role as an immunomodulator vs. pro-inflammatory agent?
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Context-dependent design: Test LGALS13 in both M1/M2 macrophage polarization assays and placental explant models. For example, low doses may induce Th2 cytokines (IL-4, IL-13), while high doses activate complement .
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Data integration: Combine transcriptomic (RNA-seq) and proteomic (LC-MS/MS) profiles to map LGALS13 interaction networks.
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What are the limitations of recombinant LGALS13 in functional studies?
Key Citations
Product Science Overview
Galectins are a family of carbohydrate-binding proteins that play crucial roles in various physiological and pathological processes. They are characterized by their affinity for β-galactoside residues and are involved in inflammation, immune responses, cell migration, autophagy, and signaling . Galectins are synthesized as cytosolic proteins and can interact with both carbohydrate and non-carbohydrate binding partners .
Galectins were initially discovered due to their galactoside-binding activity. They were defined as a protein family based on conserved β-galactoside-binding sites within their characteristic carbohydrate recognition domains (CRDs), which are approximately 130 amino acids long . The galectin family has evolved through tandem and en-mass genome duplications, resulting in over 15 known vertebrate galectins .
Galectin-13, also known as placental protein 13 (PP13), is a member of the galectin family. It is predominantly expressed in the placenta and has been implicated in various reproductive processes. Galectin-13 is involved in the regulation of immune responses at the maternal-fetal interface, promoting immune tolerance and contributing to successful pregnancy outcomes .
Galectin-13 has several important functions:
- Immune Modulation: Galectin-13 modulates immune responses by interacting with immune cells and influencing cytokine production. It promotes the differentiation of regulatory T cells and suppresses the activation of effector T cells, thereby contributing to immune tolerance during pregnancy .
- Angiogenesis: Galectin-13 plays a role in angiogenesis, the formation of new blood vessels, which is essential for placental development and function. It promotes the proliferation and migration of endothelial cells, facilitating the establishment of a functional placental vasculature .
- Apoptosis: Galectin-13 can induce apoptosis, or programmed cell death, in certain cell types. This function is important for maintaining tissue homeostasis and preventing excessive inflammation .
Recombinant Galectin-13 has several potential applications:
- Research: Recombinant Galectin-13 is used in research to study its functions and mechanisms in various biological processes. It serves as a valuable tool for investigating the role of galectins in immune regulation, angiogenesis, and apoptosis .
- Therapeutics: Due to its immunomodulatory and angiogenic properties, recombinant Galectin-13 holds promise as a therapeutic agent for conditions such as preeclampsia, a pregnancy complication characterized by high blood pressure and organ damage .
