Ecto-ADP-ribose Transferases: Cell-Surface Response to Local Tissue Injury

Physiology ◽  
2005 ◽  
Vol 20 (6) ◽  
pp. 374-381 ◽  
Author(s):  
Anna Zolkiewska
Keyword(s):  
Cell Surface ◽  
Tissue Injury ◽  
Membrane Receptors ◽  
Surface Proteins ◽  
Main Role ◽  
Membrane Stress ◽  
Cell Surface Proteins ◽  
Physiological Conditions ◽  
Arginine Residues

Ecto-ADP-ribose transferases (ecto-ARTs) catalyze the transfer of ADP-ribose from NAD+ to arginine residues in cell-surface proteins. Since the concentration of extracellular NAD+ is very low under normal physiological conditions but rises significantly upon tissue injury or membrane stress, it is postulated that the main role of ecto-ARTs is to ADP-ribosylate and regulate the function of certain membrane receptors in response to elevated levels of NAD+.

scholarly journals Hyaluronan as an Immune Regulator in Human Diseases

2011 ◽  
Vol 91 (1) ◽  
pp. 221-264 ◽  
Author(s):  
Dianhua Jiang ◽  
Jiurong Liang ◽  
Paul W. Noble
Keyword(s):  
Cell Surface ◽  
Tissue Injury ◽  
Inflammatory Cells ◽  
Cell Types ◽  
Surface Proteins ◽  
Human Diseases ◽  
Inflammatory Genes ◽  
Extracellular Matrix Components ◽  
Injury And Repair

Accumulation and turnover of extracellular matrix components are the hallmarks of tissue injury. Fragmented hyaluronan stimulates the expression of inflammatory genes by a variety of immune cells at the injury site. Hyaluronan binds to a number of cell surface proteins on various cell types. Hyaluronan fragments signal through both Toll-like receptor (TLR) 4 and TLR2 as well as CD44 to stimulate inflammatory genes in inflammatory cells. Hyaluronan is also present on the cell surface of epithelial cells and provides protection against tissue damage from the environment by interacting with TLR2 and TLR4. Hyaluronan and hyaluronan-binding proteins regulate inflammation, tissue injury, and repair through regulating inflammatory cell recruitment, release of inflammatory cytokines, and cell migration. This review focuses on the role of hyaluronan as an immune regulator in human diseases.

Mechanism of antibody stimulation of hexose transport in rat myoblasts

1984 ◽  
Vol 62 (5) ◽  
pp. 255-265 ◽  
Author(s):  
Theodore C. Y. Lo ◽  
Vincent Duronio
Keyword(s):  
Cell Surface ◽  
Covalent Modification ◽  
Membrane Receptors ◽  
Surface Proteins ◽  
Specific Cell ◽  
Activation Process ◽  
Hexose Transport ◽  
Antibody Treatment ◽  
Cell Surface Proteins ◽  
Membrane Components

We have recently demonstrated that exposure of rat myoblasts to anti-rat myoblast antiserum results in two- to three-fold activation of hexose transport. The present communication reports the possible mechanism(s) by which specific antibody can bring about such activation. Studies with Fab and Fc fragments indicate that the binding of Fab to specific cell surface component(s) is not sufficient to trigger activation of hexose transport; the immunoglobulin G (IgG) mediated dimerization of membrane components is required for this process. Although cytochalasin D has no effect on hexose transport in control and antibody-treated cells, pretreatment of cells with this inhibitor prevents antibody-mediated activation of hexose transport. It may be inferred from this observation that proper disposition of membrane components is required for the dimerization of membrane receptors. Since this activation of hexose transport is an irreversible process, it is possible that covalent modification of membrane components may have occurred as a result of antibody treatment. Pretreatment of cells with ammonium chloride or methylamine is found to abolish the antibody-mediated activation of hexose transport, even though these inhibitors have no effect on hexose transport in control and antibody-treated cells. These inhibitors may be acting on transglutaminase and (or) on some other proteins involved in the activation process. Several lines of evidence suggest that limited proteolytic cleavage of membrane components may be involved in the antibody-mediated activation of hexose transport. First, pretreatment with several protease inhibitors prevents activation of hexose transport. Second, several cell surface proteins are missing in antibody-treated cells. Third, limited proteolysis of cell surface proteins with trypsin can also bring about activation of hexose transport. In view of the fact that proteolytic activity cannot be detected in various IgG and serum preparations, it seems likely that endogenous membrane associated proteases may be involved in this activation process.

scholarly journals Find and fuse: Unsolved mysteries in sperm–egg recognition

PLoS Biology ◽  
2020 ◽  
Vol 18 (11) ◽  
pp. e3000953
Author(s):  
Enrica Bianchi ◽  
Gavin J. Wright
Keyword(s):  
Cell Surface ◽  
Sperm Cell ◽  
Surface Proteins ◽  
Secreted Proteins ◽  
Egg Recognition ◽  
Cell Surface Proteins ◽  
Molecular Events ◽  
Eukaryotic Species ◽  
Fundamental Process

Sexual reproduction is such a successful way of creating progeny with subtle genetic variations that the vast majority of eukaryotic species use it. In mammals, it involves the formation of highly specialised cells: the sperm in males and the egg in females, each carrying the genetic inheritance of an individual. The interaction of sperm and egg culminates with the fusion of their cell membranes, triggering the molecular events that result in the formation of a new genetically distinct organism. Although we have a good cellular description of fertilisation in mammals, many of the molecules involved remain unknown, and especially the identity and role of cell surface proteins that are responsible for sperm–egg recognition, binding, and fusion. Here, we will highlight and discuss these gaps in our knowledge and how the role of some recently discovered sperm cell surface and secreted proteins contribute to our understanding of this fundamental process.

The role of cell surface proteins gene expression in diagnosis, prognosis, and drug resistance of colorectal cancer: In silico analysis and validation

2021 ◽  
Vol 123 ◽  
pp. 104688
Author(s):  
Nasrin Nazempour ◽  
Mohammad Hossein Taleqani ◽  
Navid Taheri ◽  
Amir Hossein Haji Ali Asgary Najafabadi ◽  
Alireza Shokrollahi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Colorectal Cancer ◽  
Drug Resistance ◽  
Cell Surface ◽  
In Silico ◽  
In Silico Analysis ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Silico Analysis

scholarly journals Generation and Characterization of Ecto-ADP-Ribosyltransferase ART2.1/ART2.2-Deficient Mice

2002 ◽  
Vol 22 (21) ◽  
pp. 7535-7542 ◽  
Author(s):  
Wiebke Ohlrogge ◽  
Friedrich Haag ◽  
Jürgen Löhler ◽  
Michel Seman ◽  
Dan R. Littman ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Surface ◽  
T Cell Activation ◽  
Cell Activation ◽  
Tissue Injury ◽  
Surface Proteins ◽  
Cell Functions ◽  
Arginine Residues ◽  
Deficient Mice

ABSTRACT This is the first study reporting the inactivation of a member of the mouse gene family of toxin-related ecto-ADP-ribosyltransferases (ARTs). Transfer of the ADP-ribose moiety from NAD onto extracellular arginine residues on T-cell membrane proteins is mediated by glycosylphosphatidylinositol-linked cell surface ARTs. Exposure of T cells to ecto-NAD blocks T-cell activation and induces T-cell apoptosis. To determine a possible role of ecto-ART2.1 and ART2.2 in these processes, we generated ART2.1/ART2.2 double-knockout mice. ART2-deficient mice were healthy and fertile and showed normal development of lymphoid organs. ART2-deficient T cells showed a dramatically reduced capacity to ADP-ribosylate cell surface proteins, indicating that most if not all ART activity on the T-cell surface can be attributed to the ART2s. Moreover, ART2-deficient T cells were completely resistant to NAD-induced apoptosis and partially resistant to NAD-mediated suppression of proliferation. These results demonstrate that the ART2 ectoenzymes are an essential component in the regulation of T-cell functions by extracellular NAD, e.g., following release of NAD upon lysis of cells in tissue injury and inflammation.

scholarly journals Cell Surface Proteins in Hepatocellular Carcinoma: From Bench to Bedside

Vaccines ◽  
2020 ◽  
Vol 8 (1) ◽  
pp. 41
Author(s):  
Gabriel Siracusano ◽  
Maria Tagliamonte ◽  
Luigi Buonaguro ◽  
Lucia Lopalco
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Surface ◽  
Intracellular Signaling ◽  
Surface Proteins ◽  
Signaling Proteins ◽  
Cell Surface Proteins ◽  
Neoplastic Diseases ◽  
Extracellular Environment

Cell surface proteins act as the go-between in carrying the information from the extracellular environment to the intracellular signaling proteins. However, these proteins are often deregulated in neoplastic diseases, including hepatocellular carcinoma. This review discusses several recent studies that have investigated the role of cell surface proteins in the occurrence and progression of HCC, highlighting the possibility to use them as biomarkers of the disease and/or targets for vaccines and therapeutics.

Identification of potential cell-surface proteins inCandida albicansand investigation of the role of a putative cell-surface glycosidase in adhesion and virulence

Yeast ◽  
2004 ◽  
Vol 21 (4) ◽  
pp. 285-302 ◽  
Author(s):  
Christine Alberti-Segui ◽  
Arturo J. Morales ◽  
Heming Xing ◽  
Marco M. Kessler ◽  
Debra Aker Willins ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Proteins ◽  
Cell Surface Proteins
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