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Biomedicines
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Membrane Microdomains as Targets for New Therapies
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Membrane Microdomains as Targets for New Therapies

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Molecular and Translational Medicine".

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 3015

Special Issue Editor

Prof. Dr. Sandro Sonnino

E-Mail Website
Guest Editor
Department of Medical Biotechnology and Translational Medicine, University of Milano, 20054 Segrate, MI, Italy
Interests: gangliosides; Parkinson’s disease; mebrane organization; complex lipids; sphingosine; ceramide
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Complex amphiphilic lipids are functional components of membrane lipid domains, now known as lipid rafts. Lipid rafts are membrane portions developed by glycosphingolipids, sphingomyelin, ceramide, and dipalmitoylphosphatidylcholine. Lipid rafts contain a few proteins, receptors, and enzymes that are strategic for the correct physiology of cells. Within glycosphingolipids, gangliosides have been found to be associated with membrane lipid rafts, which are necessary for the activity of membrane receptors and membrane enzymes working as starting switches for the transduction of information through the plasma membrane or the beginning of functional processes. Several pathologies involve gangliosides that follow genetic derailments or enzyme kinetics, changing the incorrect quantity or incorrect positions of the results. Thus, incorrect or incomplete ganglioside–protein interaction is followed by a pathological condition or impairs a physiological function. Therefore, lipid rafts represent a starting opportunity for studies that aim to develop innovative and useful drugs for new treatments of neurodegenerative disease, tumors, and lysosomal storage diseases.

Prof. Dr. Sandro Sonnino
Guest Editor

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • gangliosides
  • lipid rafts
  • neurodegeneration
  • cancer
  • ganglioside biosynthesis
  • ganglioside catabolism

Published Papers (3 papers)

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Research

11 pages, 3094 KiB  
Article
Sialidase NEU3 Contributes to the Invasiveness of Bladder Cancer
by Takeo Tatsuta, Jun Ito, Koji Yamamoto, Shigeki Sugawara, Masahiro Hosono, Makoto Sato and Taeko Miyagi
Biomedicines 2024, 12(1), 192; https://doi.org/10.3390/biomedicines12010192 - 16 Jan 2024
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Abstract
Bladder cancer is the 10th most commonly diagnosed cancer worldwide. The current standard treatment for advanced bladder cancer is neoadjuvant cisplatin (NAC)-based chemotherapy followed by cystectomy. However, the response rate to chemotherapy is only 50%, owing to cisplatin resistance, and there is a [...] Read more.
Bladder cancer is the 10th most commonly diagnosed cancer worldwide. The current standard treatment for advanced bladder cancer is neoadjuvant cisplatin (NAC)-based chemotherapy followed by cystectomy. However, the response rate to chemotherapy is only 50%, owing to cisplatin resistance, and there is a need for novel therapies. Because the invasiveness of bladder cancer greatly influences patient prognosis, a mechanistic analysis of the invasive function can lead to therapeutic targets. Sialidases, which remove sialic acid residues from the nonreducing ends of sugar chains and catalyze the initial reaction in the degradation of sugar chains, are predicted to be involved in cell invasion and motility. However, the involvement of sialidases in bladder cancer, especially their relationship with the invasive ability, remains unclear. Here, using patient tissues and multiple bladder cancer cell lines, we show that the sialidase NEU3 is highly expressed in bladder cancer. Analysis of NEU3’s function using its siRNA-mediated knockdown revealed that NEU3 contributes to bladder cancer invasiveness. Mechanistic analysis showed that NEU3 activates ERK and PI3K signaling. Our results show that NEU3 is involved in the malignancy of bladder cancer, and its suppression may lead to novel treatments for bladder cancer. Full article
(This article belongs to the Special Issue Membrane Microdomains as Targets for New Therapies)
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14 pages, 5384 KiB  
Communication
Integrin-Dependent Transient Density Increase in Detergent-Resistant Membrane Rafts in Platelets Activated by Thrombin
by Keisuke Komatsuya, Masaki Ishikawa, Norihito Kikuchi, Tetsuya Hirabayashi, Ryo Taguchi, Naomasa Yamamoto, Morio Arai and Kohji Kasahara
Biomedicines 2024, 12(1), 69; https://doi.org/10.3390/biomedicines12010069 - 27 Dec 2023
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Abstract
Platelet lipid rafts are critical membrane domains for adhesion, aggregation, and clot retraction. Lipid rafts are isolated as a detergent-resistant membrane fraction via sucrose density gradient centrifugation. The platelet detergent-resistant membrane shifted to a higher density on the sucrose density gradient upon thrombin [...] Read more.
Platelet lipid rafts are critical membrane domains for adhesion, aggregation, and clot retraction. Lipid rafts are isolated as a detergent-resistant membrane fraction via sucrose density gradient centrifugation. The platelet detergent-resistant membrane shifted to a higher density on the sucrose density gradient upon thrombin stimulation. The shift peaked at 1 min and returned to the control level at 60 min. During this time, platelets underwent clot retraction and spreading on a fibronectin-coated glass strip. Thrombin induced the transient tyrosine phosphorylation of several proteins in the detergent-resistant membrane raft fraction and the transient translocation of fibrin and myosin to the detergent-resistant membrane raft fraction. The level of phosphatidylserine (36:1) was increased and the level of phosphatidylserine (38:4) was decreased in the detergent-resistant membrane raft fraction via the thrombin stimulation. Furthermore, Glanzmann’s thrombasthenia integrin αIIbβ3-deficient platelets underwent no detergent-resistant membrane shift to a higher density upon thrombin stimulation. As the phosphorylation of the myosin regulatory light chain on Ser19 was at a high level in Glanzmann’s thrombasthenia resting platelets, thrombin caused no further phosphorylation of the myosin regulatory light chain on Ser19 or clot retraction. These observations suggest that the fibrin–integrin αIIbβ3–myosin axis and compositional change of phosphatidylserine species may be required for the platelet detergent-resistant membrane shift to a higher density upon stimulation with thrombin. Full article
(This article belongs to the Special Issue Membrane Microdomains as Targets for New Therapies)
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12 pages, 2772 KiB  
Article
Role of Lipid Rafts on LRP8 Signaling Triggered by Anti-β2-GPI Antibodies in Endothelial Cells
by Gloria Riitano, Antonella Capozzi, Serena Recalchi, Mariaconcetta Augusto, Fabrizio Conti, Roberta Misasi, Tina Garofalo, Maurizio Sorice and Valeria Manganelli
Biomedicines 2023, 11(12), 3135; https://doi.org/10.3390/biomedicines11123135 - 24 Nov 2023
Cited by 1 | Viewed by 826
Abstract
Antiphospholipid antibody syndrome is an autoimmune disease characterized by thrombosis and/or pregnancy morbidity in association with circulating antiphospholipid antibodies, mainly anti-β2 glycoprotein 1 antibodies (anti-β2-GPI antibodies). Previous studies demonstrated that the signaling pathway may involve lipid rafts, plasma membrane microdomains enriched in glycosphingolipid [...] Read more.
Antiphospholipid antibody syndrome is an autoimmune disease characterized by thrombosis and/or pregnancy morbidity in association with circulating antiphospholipid antibodies, mainly anti-β2 glycoprotein 1 antibodies (anti-β2-GPI antibodies). Previous studies demonstrated that the signaling pathway may involve lipid rafts, plasma membrane microdomains enriched in glycosphingolipid and cholesterol. In this study, we analyzed the signaling pathway of LRP8/ApoER2, a putative receptor of anti-β2-GPI antibodies, through lipid rafts in human endothelial cells. LRP8, Dab2 and endothelial nitric oxide synthase (e-NOS) phosphorylation were evaluated using Western blot, Nitric Oxide (NO) production with cytofluorimetric analysis, LRP8 enrichment in lipid rafts via sucrose gradient fractionation, and scanning confocal microscopy analysis of its association with ganglioside GM1 was also conducted. The analyses demonstrated that affinity-purified anti-β2-GPI antibodies induced LRP8 and Dab-2 phosphorylation, together with a significant decrease in e-NOS phosphorylation, with consequent decrease in NO intracellular production. These effects were almost completely prevented by Methyl-β-cyclodextrin (MβCD), indicating the involvement of lipid rafts. It was supported with the observation of LRP8 enrichment in lipid raft fractions and its association with ganglioside GM1, detected with scanning confocal microscopy. These findings demonstrate that LRP8 signaling triggered by anti-β2-GPI antibodies in endothelial cells occurs through lipid rafts. It represents a new task for valuable therapeutic approaches, such as raft-targeted therapy, including cyclodextrins and statins. Full article
(This article belongs to the Special Issue Membrane Microdomains as Targets for New Therapies)
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