ArticleThe Journal of biological chemistry2015
Induction and activation of latent transforming growth factor-β1 are carried out by two distinct domains of pregnancy-specific glycoprotein 1 (PSG1).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Unmasking the invisible: Proteomic traces of depression in human serum - A pilot study.Indian journal of psychiatry · 2026Article
- Human Platelets Internalize Pregnancy-Specific Glycoprotein-1 (PSG1).Thrombosis and haemostasis · 2026Article
- Two waves of evolution in the rodent pregnancy-specific glycoprotein (Psg) gene family lead to structurally diverse PSGs.BMC genomics · 2023Article
- Article
- A unique maternal and placental galectin signature upon SARS-CoV-2 infection suggests galectin-1 as a key alarmin at the maternal-fetal interface.Frontiers in immunology · 2023Article
- Recombinant pregnancy-specific glycoprotein-1-Fc reduces functional deficit in a mouse model of permanent brain ischaemia.Brain, behavior, & immunity - health · 2022Article
- Effects of Pregnancy-Specific Glycoproteins on Trophoblast Motility in Three-Dimensional Gelatin Hydrogels.Cellular and molecular bioengineering · 2022Article
- Influenza A and B Virus-Triggered Epithelial-Mesenchymal Transition Is Relevant to the Binding Ability of NA to Latent TGF-β.Frontiers in microbiology · 2022Article
- Effect of Pregnancy Specific β1-Glycoprotein on the Replicative Potential of Naïve T Cells and Immune Memory T Cells.Bulletin of experimental biology and medicine · 2021Article
- The immune-modulating pregnancy-specific glycoproteins evolve rapidly and their presence correlates with hemochorial placentation in primates.BMC genomics · 2021Article
- Pregnancy-specific glycoprotein 9 acts as both a transcriptional target and a regulator of the canonical TGF-β/Smad signaling to drive breast cancer progression.Clinical and translational medicine · 2020Article
- Pro-angiogenic effects of pregnancy-specific glycoproteins in endothelial and extravillous trophoblast cells.Reproduction (Cambridge, England) · 2020Article
- Equine pregnancy-specific glycoprotein CEACAM49 secreted by endometrial cup cells activates TGFB.Reproduction (Cambridge, England) · 2020Article
- The effects of human pregnancy-specific β1-glycoprotein preparation on Th17 polarization of CD4BMC immunology · 2020Article
- Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand.Glycobiology · 2020Article
- Spatiotemporal Regulation of ΔNp63 by TGFβ-Regulated miRNAs Is Essential for Cancer Metastasis.Cancer research · 2020Article
- Article
- Risk of spontaneous preterm birth and fetal growth associates with fetal SLIT2.PLoS genetics · 2019Article
- iTRAQ and PRM-based quantitative proteomics in early recurrent spontaneous abortion: biomarkers discovery.Clinical proteomics · 2019Article
- Activation of latent transforming growth factor-β1, a conserved function for pregnancy-specific beta 1-glycoproteins.Molecular human reproduction · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Pregnancy-specific glycoproteins (PSGs) are a family of Ig-like proteins secreted by specialized placental cells. The PSG1 structure is composed of a single Ig variable region-like N-terminal domain and three Ig constant region-like domains termed A1, A2, and B2. Members of the human and murine PSG family have been shown to induce anti-inflammatory cytokines from monocytes and macrophages and to stimulate angiogenesis. We recently showed that recombinant forms of PSG1 (PSG1-Fc and PSG1-His) and PSG1 purified from the serum of pregnant women are associated with the immunoregulatory cytokine TGF-β1 and activated latent TGF-β1. Here, we sought to examine the requirement of specific PSG1 domains in the activation of latent TGF-β1. Plasmon surface resonance studies showed that PSG1 directly bound to the small latent complex and to the latency-associated peptide of TGF-β1 and that this binding was mediated through the B2 domain. Furthermore, the B2 domain alone was sufficient for activating the small latent complex. In separate experiments, we found that the PSG1-mediated induction of TGF-β1 secretion in macrophages was dependent on the N-terminal domain. Mutagenesis analysis revealed that four amino acids (LYHY) of the CC' loop of the N-terminal domain were required for induction of latent TGF-β1 secretion. Together, our results show that two distinct domains of PSG1 are involved in the regulation of TGF-β1 and provide a mechanistic framework for how PSGs modulate the immunoregulatory environment at the maternal-fetal interface for successful pregnancy outcome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.