scholarly journals Relating GPI-Anchored Ly6 Proteins uPAR and CD59 to Viral Infection

Viruses ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 1060 ◽  
Author(s):  
Yu ◽  
Murthy ◽  
Liu
Keyword(s):  
Viral Infection ◽  
Viral Entry ◽  
Current Knowledge ◽  
Cellular Functions ◽  
Lymphocyte Antigen ◽  
Host Interaction ◽  
Type Plasminogen Activator ◽  
Cell Adhesion And Migration ◽  
And Migration

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 (lymphocyte antigen 6 family member E), one key member of the Ly6E/uPAR-family proteins, has been extensively studied, other members have not been well characterized. Here, we summarize current knowledge of Ly6/uPAR proteins related to viral infection, with a focus on uPAR and CD59. Our goal is to provide an up-to-date view of the Ly6/uPAR-family proteins and associated virus–host interaction and viral pathogenesis.

scholarly journals Emerging Role of LY6E in Virus–Host Interactions

Viruses ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 1020 ◽  
Author(s):  
Jingyou Yu ◽  
Shan-Lu Liu
Keyword(s):  
Viral Infection ◽  
Viral Entry ◽  
Current Knowledge ◽  
Cell Physiology ◽  
Host Immune System ◽  
Lymphocyte Antigen ◽  
Host Interactions ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Complex Locus

As a canonical lymphocyte antigen-6/urokinase-type plasminogen activator receptor Ly6/uPAR family protein, lymphocyte antigen 6 complex, locus E (LY6E), plays important roles in immunological regulation, T cell physiology, and oncogenesis. Emerging evidence indicates that LY6E is also involved in the modulation of viral infection. Consequently, viral infection and associated pathogenesis have been associated with altered LY6E gene expression. The interaction between viruses and the host immune system has offered insights into the biology of LY6E. In this review, we summarize the current knowledge of LY6E in the context of viral infection, particularly viral entry.

scholarly journals Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Alena Ivashenka ◽  
Christian Wunder ◽  
Valerie Chambon ◽  
Roger Sandhoff ◽  
Richard Jennemann ◽  
...  
Keyword(s):  
Basolateral Membrane ◽  
Intestinal Barrier ◽  
Growth Factor Signaling ◽  
Dependent Manner ◽  
Galectin 3 ◽  
Cell Adhesion And Migration ◽  
Range Of Functions ◽  
Mouse Intestine ◽  
And Migration

AbstractGlycoproteins and glycolipids at the plasma membrane contribute to a range of functions from growth factor signaling to cell adhesion and migration. Glycoconjugates undergo endocytic trafficking. According to the glycolipid-lectin (GL-Lect) hypothesis, the construction of tubular endocytic pits is driven in a glycosphingolipid-dependent manner by sugar-binding proteins of the galectin family. Here, we provide evidence for a function of the GL-Lect mechanism in transcytosis across enterocytes in the mouse intestine. We show that galectin-3 (Gal3) and its newly identified binding partner lactotransferrin are transported in a glycosphingolipid-dependent manner from the apical to the basolateral membrane. Transcytosis of lactotransferrin is perturbed in Gal3 knockout mice and can be rescued by exogenous Gal3. Inside enterocytes, Gal3 is localized to hallmark structures of the GL-Lect mechanism, termed clathrin-independent carriers. These data pioneer the existence of GL-Lect endocytosis in vivo and strongly suggest that polarized trafficking across the intestinal barrier relies on this mechanism.

scholarly journals Glycocalyx-mediated Cell Adhesion and Migration

2020 ◽  
Author(s):  
Samuel Schmidt ◽  
Bettina Weigelin ◽  
Joost te Riet ◽  
Veronika te Boekhorst ◽  
Mariska te Lindert ◽  
...  
Keyword(s):  
Cell Attachment ◽  
Adaptive Process ◽  
Nanoscale Interactions ◽  
Cell Adhesion And Migration ◽  
3D Environments ◽  
And Migration ◽  
Force Range ◽  
Membrane Deformations

SummaryCell migration is a force-dependent adaptive process mediated by integrin-dependent adhesion as well as other yet poorly defined interactions to the extracellular matrix. Using enzymatic multi-targeted digestion of sugar moieties on the surface of mesenchymal cells and leukocytes after interference with integrin function, we demonstrate that the surface glycocalyx represents an independent adhesion system. The glycocalyx mediates cell attachment to ECM ligand in the 100-500 pN force range and amoeboid migration in 3D environments in vitro and in vivo. Glycan-based adhesions consist of actin-rich membrane deformations and appositions associated with bleb-like and other protrusions forming complex-shaped sub-micron contact sites to ECM fibrils. These data implicate the glycocalyx in mediating generic stickiness to support nanoscale interactions (nanogrips) between the cell surface and ECM, mechano-coupling, and migration.

scholarly journals LIN28B regulates transcription and potentiates MYCN-induced neuroblastoma through binding to ZNF143 at target gene promotors

2020 ◽  
Vol 117 (28) ◽  
pp. 16516-16526 ◽  
Author(s):  
Ting Tao ◽  
Hui Shi ◽  
Luca Mariani ◽  
Brian J. Abraham ◽  
Adam D. Durbin ◽  
...  
Keyword(s):  
Neuroblastoma Cells ◽  
Neuronal Cell ◽  
Distant Metastases ◽  
Malignant Cell ◽  
Gene Promoters ◽  
Invasion And Migration ◽  
Protein Protein Interaction ◽  
Cell Adhesion And Migration ◽  
And Migration

LIN28B is highly expressed in neuroblastoma and promotes tumorigenesis, at least, in part, through inhibition oflet-7microRNA biogenesis. Here, we report that overexpression of either wild-type (WT) LIN28B or a LIN28B mutant that is unable to inhibitlet-7processing increases the penetrance of MYCN-induced neuroblastoma, potentiates the invasion and migration of transformed sympathetic neuroblasts, and drives distant metastases in vivo. Genome-wide chromatin immunoprecipitation coupled with massively parallel DNA sequencing (ChIP-seq) and coimmunoprecipitation experiments show that LIN28B binds active gene promoters in neuroblastoma cells through protein–protein interaction with the sequence-specific zinc-finger transcription factor ZNF143 and activates the expression of downstream targets, including transcription factors forming the adrenergic core regulatory circuitry that controls the malignant cell state in neuroblastoma as well asGSK3BandL1CAMthat are involved in neuronal cell adhesion and migration. These findings reveal an unexpectedlet-7–independent function of LIN28B in transcriptional regulation during neuroblastoma pathogenesis.

scholarly journals The Role of Lipid Rafts in Cancer Cell Adhesion and Migration

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Toshiyuki Murai
Keyword(s):  
Cell Adhesion ◽  
Lipid Rafts ◽  
Cancer Cell ◽  
Cancer Progression ◽  
Migration And Invasion ◽  
Dynamic Features ◽  
Cellular Functions ◽  
Cancer Cell Adhesion ◽  
Cell Adhesion And Migration ◽  
And Migration

Lipid rafts are cholesterol-enriched microdomains of the cell membrane and possess a highly dynamic nature. They have been involved in various cellular functions including the regulation of cell adhesion and membrane signaling through proteins within lipid rafts. The dynamic features of the cancer cell surface may modulate the malignant phenotype of cancer, including adhesion disorders and aggressive phenotypes of migration and invasion. Recently, it was demonstrated that lipid rafts play critical roles in cancer cell adhesion and migration. This article summarizes the important roles of lipid rafts in cancer cell adhesion and migration, with a focus on the current state of knowledge. This article will improve the understanding of cancer progression and lead to the development of novel targets for cancer therapy.

ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors

2006 ◽  
Vol 291 (1) ◽  
pp. C1-C10 ◽  
Author(s):  
Haruhiko Ohtsu ◽  
Peter J. Dempsey ◽  
Satoru Eguchi
Keyword(s):  
G Protein ◽  
Egf Receptor ◽  
Current Knowledge ◽  
G Protein Coupled Receptors ◽  
Surface Proteins ◽  
Egf Receptors ◽  
Cellular Functions ◽  
Egfr Transactivation ◽  
And Migration ◽  
G Protein Coupled

A disintegrin and metalloprotease (ADAM) is a membrane-anchored metalloprotease implicated in the ectodomain shedding of cell surface proteins, including the ligands for epidermal growth factor (EGF) receptors (EGFR)/ErbB. It has been well documented that the transactivation of the EGFR plays critical roles for many cellular functions, such as proliferation and migration mediated through multiple G protein-coupled receptors (GPCRs). Recent accumulating evidence has suggested that ADAMs are the key metalloproteases activated by several GPCR agonists to produce a mature EGFR ligand leading to the EGFR transactivation. In this review, we describe the current knowledge on ADAMs implicated in mediating EGFR transactivation. The major focus of the review will be on the possible upstream mechanisms of ADAM activation by GPCRs as well as downstream signal transduction and the pathophysiological significances of ADAM-dependent EGFR transactivation.

Development of pre-implantation porcine blastocysts cultured within alginate hydrogel systems either supplemented with secreted phosphoprotein 1 or conjugated with Arg-Gly-Asp Peptide

2017 ◽  
Vol 29 (12) ◽  
pp. 2345 ◽  
Author(s):  
Taylor D. Laughlin ◽  
Jeremy R. Miles ◽  
Elane C. Wright-Johnson ◽  
Lea A. Rempel ◽  
Clay A. Lents ◽  
...  
Keyword(s):  
Morphological Changes ◽  
Rgd Peptide ◽  
Peptide Sequence ◽  
Developmental Variation ◽  
Uterine Endometrium ◽  
Alginate Hydrogels ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Secreted Phosphoprotein 1

Although deficiencies in porcine blastocyst elongation play a significant role in early embryonic mortality and establishment of within-litter developmental variation, the exact mechanisms of elongation are poorly understood. Secreted phosphoprotein 1 (SPP1) is increased within the uterine milieu during early porcine pregnancy and contains an Arg-Gly-Asp (RGD) peptide sequence that binds to cell surface integrins on the uterine endometrium and trophectoderm, promoting cell adhesion and migration. The aim of the present study was to evaluate the development of preimplantation porcine blastocysts encapsulated and cultured within alginate hydrogels either supplemented with SPP1 or conjugated with RGD. Blastocysts encapsulated within alginate hydrogels supplemented with SPP1 or conjugated with RGD had increased survival compared with non-encapsulated control blastocysts. In addition, the percentage of blastocysts encapsulated within RGD hydrogels that underwent morphological changes was greater than that of blastocysts encapsulated within standard alginate hydrogels or SPP1-supplemented hydrogels. Finally, only blastocysts encapsulated within RGD hydrogels had both increased expression of steroidogenic and immune responsiveness transcripts and increased 17β-oestradiol production, consistent with blastocysts undergoing elongation in vivo. These results illustrate the importance of the integrin-binding RGD peptide sequence for stimulating the initiation of blastocyst elongation.

scholarly journals ANGPTL3 Stimulates Endothelial Cell Adhesion and Migration via Integrin αvβ3 and Induces Blood Vessel Formation in Vivo

2002 ◽  
Vol 277 (19) ◽  
pp. 17281-17290 ◽  
Author(s):  
Gieri Camenisch ◽  
Maria Teresa Pisabarro ◽  
Daniel Sherman ◽  
Joe Kowalski ◽  
Mark Nagel ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
Blood Vessel ◽  
Integrin Αvβ3 ◽  
Blood Vessel Formation ◽  
Vessel Formation ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Endothelial Cell Adhesion

scholarly journals Gallid Herpesvirus 1 Initiates Apoptosis in Uninfected Cells through Paracrine Repression of p53

2018 ◽  
Vol 92 (18) ◽  
Author(s):  
Hai Li ◽  
Qi Gao ◽  
Yuhao Shao ◽  
Bangyao Sun ◽  
Fengjie Wang ◽  
...  
Keyword(s):  
Viral Infection ◽  
Host Cells ◽  
In Ovo ◽  
Host Interactions ◽  
Host Interaction ◽  
P53 Activation ◽  
Herpesvirus 1 ◽  
Uninfected Host

ABSTRACTApoptosis is a common innate defense mechanism of host cells against viral infection and is therefore suppressed by many viruses, including herpes simplex virus (HSV), via various strategies. A recentin vivostudy reported the apoptosis of remote uninfected cells during Gallid herpesvirus 1 (GaHV-1) infection, yet little is known about this previously unknown aspect of herpesvirus-host interactions. The aim of the present study was to investigate the apoptosis of uninfected host cells during GaHV-1 infection. The present study usedin vitroandin ovomodels, which avoided potential interference by host antiviral immunity, and demonstrated that this GaHV-1–host interaction is independent of host immune responses and important for both the pathological effect of viral infection and early viral dissemination from the primary infection site to distant tissues. Further, we revealed that GaHV-1 infection triggers this process in a paracrine-regulated manner. Using genome-wide transcriptome analyses in combination with a set of functional studies, we found that this paracrine-regulated effect requires the repression of p53 activity in uninfected cells. In contrast, the activation of p53 not only prevented the apoptosis of remote uninfected cells and subsequent pathological damage induced by GaHV-1 infection but also delayed viral dissemination significantly. Moreover, p53 activation repressed viral replication bothin vitroandin ovo, suggesting that dual cell-intrinsic mechanisms underlie the suppression of GaHV-1 infection by p53 activation. This study uncovers the mechanism underlying the herpesvirus-triggered apoptosis of remote host cells and extends our understanding of both herpesvirus-host interactions and the roles of p53 in viral infection.IMPORTANCEIt is well accepted that herpesviruses suppress the apoptosis of host cells via various strategies to ensure sustained viral replication during infection. However, a recentin vivostudy reported the apoptosis of remote uninfected cells during GaHV-1 infection. The mechanism and the biological meaning of this unexpected herpesvirus-host interaction are unclear. This study uncovers the mechanisms of herpesvirus-triggered apoptosis in uninfected cells and may also contribute to a mechanistic illustration of paracrine-regulated apoptosis induced by other viruses in uninfected host cells.

Sign in / Sign up

Export Citation Format

Share Document