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Journal articles on the topic 'Ly6/uPAR proteins'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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1

Yu, Murthy, and Liu. "Relating GPI-Anchored Ly6 Proteins uPAR and CD59 to Viral Infection." Viruses 11, no. 11 (2019): 1060. http://dx.doi.org/10.3390/v11111060.

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The Ly6 (lymphocyte antigen-6)/uPAR (urokinase-type plasminogen activator receptor) superfamily protein is a group of molecules that share limited sequence homology but conserved three-fingered structures. Despite diverse cellular functions, such as in regulating host immunity, cell adhesion, and migration, the physiological roles of these factors in vivo remain poorly characterized. Notably, increasing research has focused on the interplays between Ly6/uPAR proteins and viral pathogens, the results of which have provided new insight into viral entry and virus–host interactions. While LY6E (ly

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2

Zaigraev, Maxim M., Ekaterina N. Lyukmanova, Alexander S. Paramonov, Zakhar O. Shenkarev, and Anton O. Chugunov. "Orientational Preferences of GPI-Anchored Ly6/uPAR Proteins." International Journal of Molecular Sciences 24, no. 1 (2022): 11. http://dx.doi.org/10.3390/ijms24010011.

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Ly6/uPAR proteins regulate many essential functions in the nervous and immune systems and epithelium. Most of these proteins contain single β-structural LU domains with three protruding loops and are glycosylphosphatidylinositol (GPI)-anchored to a membrane. The GPI-anchor role is currently poorly studied. Here, we investigated the positional and orientational preferences of six GPI-anchored proteins in the receptor-unbound state by molecular dynamics simulations. Regardless of the linker length between the LU domain and GPI-anchor, the proteins interacted with the membrane by polypeptide part

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3

Bychkov, M. L., A. V. Kirichenko, A. S. Paramonov, M. P. Kirpichnikov та E. N. Lukmanova. "ACCUMULATION OF β-AMYLOID LEADS TO A DECREASE IN LYNX1 AND LYPD6B EXPRESSION IN THE HIPPOCAMPUS AND INCREASED EXPRESSION OF PRO-INFLAMMATORY CYTOKINES IN THE HIPPOCAMPUS AND BLOOD SERUM". Доклады Российской академии наук. Науки о жизни 511, № 1 (2023): 354–59. http://dx.doi.org/10.31857/s2686738922600881.

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Alzheimer’s disease is a rapidly progressive neurodegenerative disease, the development of which is associated with the accumulation of β-amyloid oligomers, dysfunction of the α7-nAChR nicotinic acetylcholine receptor, and activation of inflammation. Previously, we have shown that the neuromodulator Lynx1, which belongs to the Ly6/uPAR family, competes with β-amyloid(1–42) for binding to α7-nAChR. In the present work, we studied the expression and localization of Ly6/uPAR family proteins in the hippocampus of 2xTg-AD transgenic mice that model AD and demonstrate increased amyloidosis in the br

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4

Bychkov, Maxim L., Aizek B. Isaev, Alexander A. Andreev-Andrievskiy та ін. "Aβ1-42 Accumulation Accompanies Changed Expression of Ly6/uPAR Proteins, Dysregulation of the Cholinergic System, and Degeneration of Astrocytes in the Cerebellum of Mouse Model of Early Alzheimer Disease". International Journal of Molecular Sciences 24, № 19 (2023): 14852. http://dx.doi.org/10.3390/ijms241914852.

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Alzheimer disease (AD) is a widespread neurodegenerative disease characterized by the accumulation of oligomeric toxic forms of β-amyloid (Aβ1-42) and dysfunction of the cholinergic system in the different brain regions. However, the exact mechanisms of AD pathogenesis and the role of the nicotinic acetylcholine receptors (nAChRs) in the disease progression remain unclear. Here, we revealed a decreased expression of a number of the Ly6/uPAR proteins targeting nAChRs in the cerebellum of 2xTg-AD mice (model of early AD) in comparison with non-transgenic mice both at mRNA and protein levels. We

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5

Leth, Julie Maja, Katrine Zinck Leth-Espensen, Kristian Kølby Kristensen, et al. "Evolution and Medical Significance of LU Domain−Containing Proteins." International Journal of Molecular Sciences 20, no. 11 (2019): 2760. http://dx.doi.org/10.3390/ijms20112760.

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Proteins containing Ly6/uPAR (LU) domains exhibit very diverse biological functions and have broad taxonomic distributions in eukaryotes. In general, they adopt a characteristic three-fingered folding topology with three long loops projecting from a disulfide-rich globular core. The majority of the members of this protein domain family contain only a single LU domain, which can be secreted, glycolipid anchored, or constitute the extracellular ligand binding domain of type-I membrane proteins. Nonetheless, a few proteins contain multiple LU domains, for example, the urokinase receptor uPAR, C4.

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6

Vasilyeva, N. A., E. V. Loktyushov, M. L. Bychkov, Z. O. Shenkarev, and E. N. Lyukmanova. "Three-finger proteins from the Ly6/uPAR family: Functional diversity within one structural motif." Biochemistry (Moscow) 82, no. 13 (2017): 1702–15. http://dx.doi.org/10.1134/s0006297917130090.

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7

Kriegbaum, Mette C., Ole P. F. Clausen, Ole D. Lærum, and Michael Ploug. "Expression of the Ly6/uPAR-Domain Proteins C4.4A and Haldisin in Non-Invasive and Invasive Skin Lesions." Journal of Histochemistry & Cytochemistry 63, no. 2 (2014): 142–54. http://dx.doi.org/10.1369/0022155414563107.

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8

Shulepko, M. A., E. N. Lyukmanova, Z. O. Shenkarev, et al. "Towards universal approach for bacterial production of three-finger Ly6/uPAR proteins: Case study of cytotoxin I from cobra N. oxiana." Protein Expression and Purification 130 (February 2017): 13–20. http://dx.doi.org/10.1016/j.pep.2016.09.021.

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9

Lyukmanova, Ekaterina N., Maxim L. Bychkov, Andrei M. Chernikov, et al. "In Search of the Role of Three-Finger Starfish Proteins." Marine Drugs 22, no. 11 (2024): 488. http://dx.doi.org/10.3390/md22110488.

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Three-finger proteins (TFPs), or Ly6/uPAR proteins, are characterized by the beta-structural LU domain containing three protruding “fingers” and stabilized by four conserved disulfide bonds. TFPs were initially characterized as snake alpha-neurotoxins, but later many studies showed their regulatory roles in different organisms. Despite a known expression of TFPs in vertebrates, they are poorly studied in other taxa. The presence of TFPs in starfish was previously shown, but their targets and functional role still remain unknown. Here, we analyzed expression, target, and possible function of th

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10

Shelukhina, Irina, Andrei Siniavin, Igor Kasheverov, Lucy Ojomoko, Victor Tsetlin та Yuri Utkin. "α7- and α9-Containing Nicotinic Acetylcholine Receptors in the Functioning of Immune System and in Pain". International Journal of Molecular Sciences 24, № 7 (2023): 6524. http://dx.doi.org/10.3390/ijms24076524.

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Nicotinic acetylcholine receptors (nAChRs) present as many different subtypes in the nervous and immune systems, muscles and on the cells of other organs. In the immune system, inflammation is regulated via the vagus nerve through the activation of the non-neuronal α7 nAChR subtype, affecting the production of cytokines. The analgesic properties of α7 nAChR-selective compounds are mostly based on the activation of the cholinergic anti-inflammatory pathway. The molecular mechanism of neuropathic pain relief mediated by the inhibition of α9-containing nAChRs is not fully understood yet, but the

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11

Busso, N., S. K. Masur, D. Lazega, S. Waxman, and L. Ossowski. "Induction of cell migration by pro-urokinase binding to its receptor: possible mechanism for signal transduction in human epithelial cells." Journal of Cell Biology 126, no. 1 (1994): 259–70. http://dx.doi.org/10.1083/jcb.126.1.259.

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A human epithelial cell line, WISH, and a mouse cell line, LB6-uPAR, transfected with the human urokinase receptor (uPAR), both expressed high affinity uPAR but undetectable levels of urokinase (uPA). In two independent assays, binding of exogenous pro-uPA produced an up to threefold enhancement of migration. The migration was time and concentration dependent and did not involve extracellular proteolysis. This biologic response suggested that uPAR can trigger an intracellular signal. Since this receptor is a glycosyl-phosphatidylinositol-linked protein, we postulated that it must do so by inte

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12

Spivak, Jerry L., Giovanni Barosi, Gianni Tognoni, et al. "Chronic Myeloproliferative Disorders." Hematology 2003, no. 1 (2003): 200–224. http://dx.doi.org/10.1182/asheducation-2003.1.200.

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Abstract The Philadelphia chromosome-negative chronic myeloproliferative disorders (CMPD), polycythemia vera (PV), essential thrombocythemia (ET) and chronic idiopathic myelofibrosis (IMF), have overlapping clinical features but exhibit different natural histories and different therapeutic requirements. Phenotypic mimicry amongst these disorders and between them and nonclonal hematopoietic disorders, lack of clonal diagnostic markers, lack of understanding of their molecular basis and paucity of controlled, prospective therapeutic trials have made the diagnosis and management of PV, ET and IMF

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13

Maxim, Zaigraev, and Chugunov Anton. "Orientational Preferences of GPI-anchored Ly6/uPAR Proteins." December 17, 2022. https://doi.org/10.5281/zenodo.7074188.

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1) <strong>Supplementary movies</strong> are provided as separate <em>mov </em>files. They represent 2-3 μs production phase of molecular dynamics for six different GPI-anchored Ly6 proteins studied: Lynx1, Lynx2, Lypd6, Lypd6B, Ly6H and CD59. Water molecules, ions and non-polar hydrogens are not shown in the movies. 2) <strong>Supplementary MD trajectories</strong> for all the systems are contained in the attached <em>zip</em> archive.

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14

Bychkov, Maxim L., Mikhail A. Shulepko, Olga V. Shlepova та ін. "SLURP-1 Controls Growth and Migration of Lung Adenocarcinoma Cells, Forming a Complex With α7-nAChR and PDGFR/EGFR Heterodimer". Frontiers in Cell and Developmental Biology 9 (14 вересня 2021). http://dx.doi.org/10.3389/fcell.2021.739391.

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Secreted Ly6/uPAR-related protein 1 (SLURP-1) is a secreted Ly6/uPAR protein that negatively modulates the nicotinic acetylcholine receptor of α7 type (α7-nAChR), participating in control of cancer cell growth. Previously we showed, that a recombinant analogue of human SLURP-1 (rSLURP-1) diminishes the lung adenocarcinoma A549 cell proliferation and abolishes the nicotine-induced growth stimulation. Here, using multiplex immunoassay, we demonstrated a decrease in PTEN and mammalian target of rapamycin (mTOR) kinase phosphorylation in A549 cells upon the rSLURP-1 treatment pointing on down-regu

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15

Kristensen, Kristian Kølby, Katrine Zinck Leth-Espensen, Anni Kumari, et al. "GPIHBP1 and ANGPTL4 Utilize Protein Disorder to Orchestrate Order in Plasma Triglyceride Metabolism and Regulate Compartmentalization of LPL Activity." Frontiers in Cell and Developmental Biology 9 (July 15, 2021). http://dx.doi.org/10.3389/fcell.2021.702508.

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Intravascular processing of triglyceride-rich lipoproteins (TRLs) is crucial for delivery of dietary lipids fueling energy metabolism in heart and skeletal muscle and for storage in white adipose tissue. During the last decade, mechanisms underlying focal lipolytic processing of TRLs along the luminal surface of capillaries have been clarified by fresh insights into the functions of lipoprotein lipase (LPL); LPL’s dedicated transporter protein, glycosylphosphatidylinositol-anchored high density lipoprotein–binding protein 1 (GPIHBP1); and its endogenous inhibitors, angiopoietin-like (ANGPTL) p

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