New Insights into Molecular Organization of Human Neuraminidase-1: Transmembrane Topology and Dimerization Ability

Maurice, Pascal; Baud, Stéphanie; Bocharova, Olga V.; Bocharov, Eduard V.; Kuznetsov, Andrei; Kawecki, Charlotte; Bocquet, Olivier; Romier, Béatrice; Gorisse, Laëtitia; Ghirardi, Maxime; Duca, Laurent; Blaise, Sébastien; Martiny, Laurent; Dauchez, Manuel; Efremov, Roman G.; Debelle, Laurent

doi:10.1038/srep38363

Cited by 48 publications

(65 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…One neuraminidase mediating platelet desialylation is neuraminidase-1 (NEU1), which resides in the platelet lysosome and is trafficked to the plasma membrane after refrigeration 5 . NEU1 is membrane-bound and can desialylate platelet glycoproteins including GPIbα 5, 24 . However, it was not clear how refrigeration induces movement of NEU1 from the lysosome to the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

Refrigeration-Induced Binding of von Willebrand Factor Facilitates Fast Clearance of Refrigerated Platelets

Chen

Druzak

Wang

et al. 2017

ATVB

View full text Add to dashboard Cite

Objective Apheresis platelets for transfusion treatment are currently stored at room temperature because after refrigeration platelets are rapidly cleared upon transfusion. In this study, the role of von Willebrand factor (VWF) in the clearance of refrigerated platelets is addressed. Approach and Results Human and murine platelets were refrigerated in gas-permeable bags at 4°C for 24 hours. VWF binding, platelet signaling events, and platelet post-transfusion recovery and survival were measured. After refrigeration the binding of plasma VWF to platelets was drastically increased, confirming earlier studies. The binding was blocked by peptide OS1 that bound specifically to platelet glycoprotein (GP)Ibα and was absent in VWF−/− plasma. Although surface expression of GPIbα was reduced after refrigeration, refrigeration-induced VWF binding under physiological shear induced unfolding of the GPIbα mechanosensory domain on the platelet, as evidenced by increased exposure of a linear epitope therein. Refrigeration and shear treatment also induced small elevation of intracellular Ca2+, phosphatidylserine exposure and desialylation of platelets, which were absent in VWF−/− platelets or inhibited by OS1. Furthermore, refrigerated VWF−/− platelets displayed increased post-transfusion recovery and survival than wild-type ones. Similarly, adding OS1 to transgenic murine platelets expressing only human GPIbα during refrigeration improved their post-transfusion recovery and survival. Conclusions Refrigeration-induced binding of VWF to platelets facilitates their rapid clearance by inducing GPIbα-mediated signaling. Our results suggest that inhibition of the VWF-GPIbα interaction may be a potential strategy to enable refrigeration of platelets for transfusion treatment.

show abstract

Section: Discussionmentioning

confidence: 99%

Refrigeration-Induced Binding of von Willebrand Factor Facilitates Fast Clearance of Refrigerated Platelets

Chen

Druzak

Wang

et al. 2017

ATVB

View full text Add to dashboard Cite

show abstract

“…Furthermore, EDP induce an enhanced invasion of melanoma cells (46)(47)(48). Implication of EDP and Neu-1 in other cancer types has also been shown: Neu-1 is involved in the development of hepatocellular carcinoma (49) and ovarian cancer (50). Altogether, these data indicate that Neu-1 plays a key role in the development and the amplification of several cancers and can constitute a new target to slow down cancer progression.…”

Section: Neu-1 Tm Domain As a Potential Target In Cancersmentioning

confidence: 85%

Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?

et al. 2020

Self Cite

View full text Add to dashboard Cite

Cellular functions are regulated by extracellular signals such as hormones, neurotransmitters, matrix ligands, and other chemical or physical stimuli. Ligand binding on its transmembrane receptor induced cell signaling and the recruitment of several interacting partners to the plasma membrane. Nowadays, it is well-established that the transmembrane domain is not only an anchor of these receptors to the membrane, but it also plays a key role in receptor dimerization and activation. Indeed, interactions between transmembrane helices are associated with specific biological activity of the proteins as cell migration, proliferation, or differentiation. Overexpression or constitutive dimerization (due notably to mutations) of these transmembrane receptors are involved in several physiopathological contexts as cancers. The transmembrane domain of tyrosine kinase receptors as ErbB family proteins (implicated in several cancers as HER2 in breast cancer) or other receptors as Neuropilins has been described these last years as a target to inhibit their dimerization/activation using several strategies. In this review, we will focus on the strategy which consists in using peptides to disturb in a specific manner the interactions between transmembrane domains and the signaling pathways (induced by ligand binding) of these receptors involved in cancer. This approach can be extended to inhibit other transmembrane protein dimerization as neuraminidase-1 (the catalytic subunit of elastin receptor complex), Discoidin Domain Receptor 1 (a tyrosine kinase receptor activated by type I collagen) or G-protein coupled receptors (GPCRs) which are involved in cancer processes.

show abstract

“…How these enzymes are associated with the membrane remains controversial. For Neu1, some studies suggested a C-terminal transmembrane domain, whereas other studies excluded a transmembrane region proposing a lipid anchor 75,76 . Subcellular location and activity of sialidases might differ depending on the physiological conditions and the cell types, as demonstrated by the polysialic acid processing by Neu1 77 and the involvement of Neu4 in hippocampal memory processing 78 .…”

Section: Identified Sialidases and Sialyltransferases In Synaptosomesmentioning

confidence: 99%

Synaptic transmission induces site-specific changes in sialylation onN-linked glycoproteins in rat nerve terminals

Boll

Jensen

Schwämmle

et al. 2020

Preprint

View full text Add to dashboard Cite

Synaptic transmission leading to release of neurotransmitters in the nervous system is a fast and highly dynamic process. Previously, protein interaction and phosphorylation have been thought to be the main regulators of synaptic transmission. Here we show a novel potential modulator of synaptic transmission, sialylation of N-linked glycosylation. The negatively charged sialic acids can be modulated, similarly to phosphorylation, by the action of sialyltransferases and sialidases thereby changing local structure and function of membrane glycoproteins. We characterized site-specific alteration in sialylation on N-linked glycoproteins in isolated rat nerve terminals after brief depolarization using quantitative sialiomics. We identified 1965 formerly sialylated N-linked glycosites in synaptic proteins and found that the abundances of 430 glycosites changed after five seconds depolarization. We observed changes on essential synaptic proteins such as synaptic vesicle proteins, ion channels and transporters, neurotransmitter receptors and cell adhesion molecules. This study is to our knowledge the first to describe ultra-fast site-specific modulation of the sialiome after brief stimulation of a biological system.

show abstract

New Insights into Molecular Organization of Human Neuraminidase-1: Transmembrane Topology and Dimerization Ability

Cited by 48 publications

References 61 publications

Refrigeration-Induced Binding of von Willebrand Factor Facilitates Fast Clearance of Refrigerated Platelets

Refrigeration-Induced Binding of von Willebrand Factor Facilitates Fast Clearance of Refrigerated Platelets

Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?

Synaptic transmission induces site-specific changes in sialylation onN-linked glycoproteins in rat nerve terminals

Contact Info

Product

Resources

About