Characterization of a broadly expressed human leucocyte surface antigen MEM-43 anchored in membrane through phosphatidylinositol

Stefanová, I; Hilgert, I; Kristofová, H; Brown, Rosemary; Mg, Low; Horejsí,

doi:10.1016/0161-5890(89)90097-7

Cited by 131 publications

(73 citation statements)

References 17 publications

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“…A. Ledbetter (Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ) (46). Two anti-CD43 antibodies reacting with different epitopes were used in this study: L10, which reacts with both sialylated and desialylated CD43 (15), was purchased from Caltag (Burlingame, CA), whereas MEM-59, which is directed against a sialic acid-dependent epitope (47), is a kind gift from Dr. V. Horejski (University of Prague, Czech Republic). Purified goat anti-mouse IgG antibody was obtained from Jackson ImmunoResearch (West Grove, PA).…”

Section: Methodsmentioning

confidence: 99%

Engagement of CD43 Enhances Human Immunodeficiency Virus Type 1 Transcriptional Activity and Virus Production That Is Induced upon TCR/CD3 Stimulation

Barat¹,

Tremblay²

2002

Journal of Biological Chemistry

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Human immunodeficiency virus type 1 (HIV-1) transcriptional activity is regulated by several cytokines and T cell activators. CD43 (sialophorin) is a sialoglycoprotein expressed on the surface of a wide variety of blood cells including T lymphocytes. Several studies have shown that CD43 ligation induces proliferation and activation of human T lymphocytes. We were thus interested in defining whether CD43-mediated signaling events can modulate the life cycle of HIV-1. We demonstrate here that CD43 cross-linking potentiates HIV-1 promoter-driven activity and virus production that is seen following the engagement of the T-cell receptor (TCR)⅐CD3 complex. This effect is independent of the CD28 co-stimulatory molecule and is mediated by both NF-B and NFAT transcription factors. A number of signal transducers known to be involved in the TCR/CD3-dependent signal transduction pathway, including p56 lck , p36 lat , and SLP-76, as well as capacitative entry of calcium, are crucial for the noticed CD43 co-stimulatory effect. Calcium mobilization studies indicate that a synergy is occurring between CD43-and TCR/CD3-mediated signaling events leading to an augmented calcium release. These data suggest that CD43 can be seen as a co-stimulatory cell surface constituent that can modulate HIV-1 expression in T lymphocytes.

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Section: Methodsmentioning

confidence: 99%

Engagement of CD43 Enhances Human Immunodeficiency Virus Type 1 Transcriptional Activity and Virus Production That Is Induced upon TCR/CD3 Stimulation

Barat¹,

Tremblay²

2002

Journal of Biological Chemistry

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“…Monoclonal antibodies directed against rat 5Ј NT (5NT42) (Siddle et al, 1981), rat CD59 (6D1 and TH9) (Hughes et al, 1992), human CD59 (MEM43) (Stefanova et al, 1989), and human folate receptor (MOv19 and MOv18) (Coney et al, 1991) were graciously provided by Dr. J. P. Luzio (University of Cambridge, Cambridge, UK), Dr. B. P. Morgan (University of Wales College of Medicine, Heath Park, Cardiff, UK), Dr. V. Horejsi (Czech Academy of Sciences, Prague, Czech Republic), and Dr. J. Ghrayeb (Centorcor, Malvern, PA), respectively. CTXB was purchased from Sigma Chemical (St. Louis, MO).…”

Section: Cells and Antibodiesmentioning

confidence: 99%

High-Resolution FRET Microscopy of Cholera Toxin B-Subunit and GPI-anchored Proteins in Cell Plasma Membranes

Kenworthy

Petranova

Edidin

2000

MBoC

406

311

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“Lipid rafts” enriched in glycosphingolipids (GSL), GPI-anchored proteins, and cholesterol have been proposed as functional microdomains in cell membranes. However, evidence supporting their existence has been indirect and controversial. In the past year, two studies used fluorescence resonance energy transfer (FRET) microscopy to probe for the presence of lipid rafts; rafts here would be defined as membrane domains containing clustered GPI-anchored proteins at the cell surface. The results of these studies, each based on a single protein, gave conflicting views of rafts. To address the source of this discrepancy, we have now used FRET to study three different GPI-anchored proteins and a GSL endogenous to several different cell types. FRET was detected between molecules of the GSL GM1 labeled with cholera toxin B-subunit and between antibody-labeled GPI-anchored proteins, showing these raft markers are in submicrometer proximity in the plasma membrane. However, in most cases FRET correlated with the surface density of the lipid raft marker, a result inconsistent with significant clustering in microdomains. We conclude that in the plasma membrane, lipid rafts either exist only as transiently stabilized structures or, if stable, comprise at most a minor fraction of the cell surface.

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“…Homologous restriction factor (HRF) (Zalman et al, 1986) or C8 binding protein (C8bp) (Schonermark et al, 1986) and protectin (CD59) (Sugita et al, 1988) regulate the formation and function of MAC. While HRF/C8bp awaits detailed molecular characterization, the processed cell surface form of CD59 is known to have 77 amino acids (Fletcher et al, 1993) linked to the cell membrane via a glycosyl-phosphatidylinositol (GPI) anchor (Stefanova' et al, 1989). CD59 inhibits C lysis by interacting with C8 and C9 in the nascent MAC and thereby restricting the number and polymerization of C9 molecules in the complex (Meri et al, 1990;Rollins and Sims, 1990).…”

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confidence: 99%

Resistance of ovarian teratocarcinoma cell spheroids to complement-mediated lysis

Bjørge

Junnikkala²,

Kristoffersen³

et al. 1997

Br J Cancer

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Summary We have shown previously that it is possible to target complement-mediated killing against cultured ovarian tumour cells in vitro. As malignant ovarian cells usually grow in solid nodules in vivo, we have in the present study examined the effectiveness of complement killing against ovarian teratocarcinoma cells (PA-1) growing in three-dimensional tumour microspheroids (TMSs). Our study shows that PA-1 cells growing in TMSs are less susceptible to complement-mediated killing than cells growing in monolayer cultures, even after neutralization of protectin (CD59), the main inhibitor of complement lysis. Cells in suspension and cells growing in TMSs showed a similar expression of membrane co-factor protein (MCP, CD46) and CD59. Decay-accelerating factor (DAF, CD55) was not detected on the surface of cells in suspension, but appeared focally on the outermost cell layers of the TMSs. Complement-activating antibodies bound to all PA-1 cells in suspension but only to the most peripherally located cells in TMSs, even though the target antigens were similarly expressed in the two systems. Antibody-induced complement activation on PA-1 cells in suspension led to C3 and C5b-9 deposition on most cells, while C3 and C5b-9 were only found on the outermost layers of the TMSs. The increased complement resistance of tumour cells growing in threedimensional spheroids is partly because of an insufficient penetration of antibodies and complement into the TMSs. TMSs are a useful model for the development of more efficient ways to kill malignant cells in micrometastases with monoclonal antibodies and complement.

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Characterization of a broadly expressed human leucocyte surface antigen MEM-43 anchored in membrane through phosphatidylinositol

Cited by 131 publications

References 17 publications

Engagement of CD43 Enhances Human Immunodeficiency Virus Type 1 Transcriptional Activity and Virus Production That Is Induced upon TCR/CD3 Stimulation

Engagement of CD43 Enhances Human Immunodeficiency Virus Type 1 Transcriptional Activity and Virus Production That Is Induced upon TCR/CD3 Stimulation

High-Resolution FRET Microscopy of Cholera Toxin B-Subunit and GPI-anchored Proteins in Cell Plasma Membranes

Resistance of ovarian teratocarcinoma cell spheroids to complement-mediated lysis

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