scholarly journals Rosetting of activated human T lymphocytes with autologous erythrocytes. Definition of the receptor and ligand molecules as CD2 and lymphocyte function-associated antigen 3 (LFA-3).

1987 ◽  
Vol 165 (3) ◽  
pp. 664-676 ◽  
Author(s):  
M L Plunkett ◽  
M E Sanders ◽  
P Selvaraj ◽  
M L Dustin ◽  
T A Springer
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
T Lymphocytes ◽  
Cell Surface ◽  
T Lymphocyte ◽  
Surface Protein ◽  
Target Cells ◽  
Lymphocyte Function ◽  
Cell Surface Protein ◽  
Definition Of

CD2, also known as LFA-2, T11, and the E rosette receptor, is a T lymphocyte surface protein functionally important in adhesion to target cells and T cell triggering. LFA-3 is a widely distributed cell surface protein that functions in adhesion on target cells. We find that LFA-3 is expressed on human E, and that CD2 is a receptor for LFA-3 that mediates T cell adhesion to human E. Pretreatment of T lymphocytes with CD2 mAb or of E with LFA-3 mAb inhibits rosetting. Purified CD2 molecules bind to human E and inhibit rosetting. 125I-CD2 binding to E is inhibited by LFA-3 mAb; reciprocally, binding of LFA-3 mAb to human E is inhibited by pretreatment with purified CD2. Higher concentrations of CD2 aggregate human E; aggregation is inhibited by mAb to LFA-3.

scholarly journals Absence of allogeneic restriction in human T-cell-mediated cytotoxicity to Epstein-Barr virus-infected target cells. Demonstration of an HLA-linked control at the effector level.

1979 ◽  
Vol 150 (6) ◽  
pp. 1310-1322 ◽  
Author(s):  
M Lipinski ◽  
W H Fridman ◽  
T Tursz ◽  
C Vincent ◽  
D Pious ◽  
...  
Keyword(s):  
T Cell ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Target Cell ◽  
Epstein Barr Virus ◽  
Target Cells ◽  
Specific Lysis ◽  
Barr Virus ◽  
Positive Target ◽  
Epstein Barr

Peripheral T lymphocytes from patients with infectious mononucleosis (IM) are sensitized in vivo against the Epstein-Barr virus (EBV). The expression of HLA-A, B, or C molecules at the target cell surface is necessary for the cytotoxic reaction because (a) EBV-positive Daudi cells lacking HLA-A, B, and C determinants are resistant to anti-EBV T-cell lysis, (b) cytolysis of EBV-positive target cells can be consistently inhibited by anti-HLA-A, B, and C and anti-beta 2 microglobulin antibodies. However, no evidence for allogeneic restriction in this system was apparent as (a) cytotoxic T lymphocytes (CTL) from one given individual could exert a cytotoxicity of a similar magnitude on different EBV-positive target cells, regardless of the number of HLA-A or B specificities shared by the effectors and targets; (b) CTL from IM patients were able to kill target cells without any HLA-A or B antigen in common; and (c) T5-1 variants lacking one or two HLA antigens at the A, B, or D locus are killed to the same extent as the parental cells. 7 of the 9 IM patients with detectable circulating anti-EBV CTL carried the HLA-A1 antigen, whereas none of the 16 IM patients lacking detectable peripheral CTL were HLA-A1 positive (mean specific lysis of T5-1 target cells by T cells from HLA-A1 positive patients: 29.3 vs. 0.6% in HLA-A1-negative patients) (P less than 10(-9)). These data suggest an HLA-A1-linked gene control of the magnitude of the anti-EBV CTL response. Thus, the HLA region appears to act at two different level sin the T-cell-mediated lysis of EBV-infected cells by controlling first, the development of anti-EBV and second, the expression of HLA-A, B, and C molecules involved as recognition structures at the target cell surface.

scholarly journals Cutaneous T Cell Lymphoma Expresses Immunosuppressive CD80 (B7-1) Cell Surface Protein in a STAT5-Dependent Manner

2014 ◽  
Vol 192 (6) ◽  
pp. 2913-2919 ◽  
Author(s):  
Qian Zhang ◽  
Hong Yi Wang ◽  
Fang Wei ◽  
Xiaobin Liu ◽  
Jennifer C. Paterson ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Cell Lymphoma ◽  
Surface Protein ◽  
T Cell Lymphoma ◽  
Dependent Manner ◽  
Cutaneous T Cell Lymphoma ◽  
Cell Surface Protein

T4: A T-Cell Surface Protein Mediating Cell-Cell and Cell-AIDS Virus Interactions

1987 ◽  
pp. 159-175
Author(s):  
Angus G. Dalgleish ◽  
Paul R. Clapham ◽  
Robin A. Weiss ◽  
Paul J. Maddon ◽  
Maurice Godfrey ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Aids Virus ◽  
Virus Interactions ◽  
Cell Cell

Insights into the ontogeny and activation of T cells

1994 ◽  
Vol 40 (11) ◽  
pp. 2128-2131 ◽  
Author(s):  
T W Mak
Keyword(s):  
T Cells ◽  
T Cell ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Immune Responses ◽  
Tyrosine Phosphatase ◽  
T Cell Development ◽  
Cell Development ◽  
Mutant Mice ◽  
Target Cells

Abstract T lymphocytes recognize antigen peptides and major histocompatibility complex products through their T-cell antigen receptors (TcR), consisting of alpha and beta chains. The interaction between T cells and their target cells or antigen-presenting cells is also assisted by a series of other cell-surface polypeptides, most notably CD4 and CD8, which are selectively expressed on mature helper/inducer and killer/suppressor T cells, respectively. Upon engagement of their ligands, a series of signals is transduced intracytoplasmically via some of these molecules and their associated proteins. Perhaps the most important enzyme in this signal transduction process is the lymphocyte-specific tyrosine kinase lck. Another important component is the cell-surface tyrosine phosphatase CD45. This molecule is alternatively spliced and the different isoforms are expressed on the various hematopoietic and lymphopoietic cells. Signaling through the TcR-CD4 D8-lck-CD45 complex is thought to be insufficient to activate T lymphocytes. A costimulatory signal is believed to be essential, and many investigators have suggested that CD28, a ligand for B7/BB1, is such a signal. Immune responses are also controlled by a number of cytokines and soluble factors. Signaling through the tumor necrosis factor receptor p55 is required for clearance of intracellular pathogens. Transcriptional factors involved in controlling interferon production are also important in T-cell development and immune responses. In an attempt to gain a better understanding of the roles of these molecules in T-lymphocyte functions and ontogeny, we generated a series of mutant mice with disruptions in the genes coding for these molecules. We are analyzing the mutant mice to evaluate the importance of these genes in T-cell development.

The HIV-1 Nef protein shares an antigenic determinant with a T-cell surface protein

AIDS ◽  
1993 ◽  
Vol 7 (5) ◽  
pp. 647-654 ◽  
Author(s):  
Thomas Schneider ◽  
Andreas Beck ◽  
Claudia Röpke ◽  
Reiner Ullrich ◽  
Hans-Peter Harthus ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Antigenic Determinant ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Hiv 1

scholarly journals Signal peptide cleavage is essential for surface expression of a regulatory T cell surface protein, leucine rich repeat containing 32 (LRRC32)

2011 ◽  
Vol 12 (1) ◽  
pp. 27 ◽  
Author(s):  
Derek V Chan ◽  
Ally-Khan Somani ◽  
Andrew B Young ◽  
Jessica V Massari ◽  
Jennifer Ohtola ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Signal Peptide ◽  
Regulatory T Cell ◽  
Surface Protein ◽  
Surface Expression ◽  
Cell Surface Protein ◽  
Leucine Rich Repeat ◽  
Peptide Cleavage

The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family

Cell ◽  
1985 ◽  
Vol 42 (1) ◽  
pp. 93-104 ◽  
Author(s):  
P MADDON ◽  
D LITTMAN ◽  
M GODFREY ◽  
D MADDON ◽  
L CHESS ◽  
...  
Keyword(s):  
T Cell ◽  
Nucleotide Sequence ◽  
Cell Surface ◽  
Gene Family ◽  
Surface Protein ◽  
Immunoglobulin Gene ◽  
Cell Surface Protein

scholarly journals Bovine Milk Antibodies against Cell Surface Protein Antigen PAc-Glucosyltransferase Fusion Protein Suppress Cell Adhesion and Alter Glucan Synthesis of Streptococcus mutans

1999 ◽  
Vol 129 (10) ◽  
pp. 1836-1841 ◽  
Author(s):  
Takahiko Oho ◽  
Yoshihiro Shimazaki ◽  
Morihide Mitoma ◽  
Mamiko Yoshimura ◽  
Yoshihisa Yamashita ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Fusion Protein ◽  
Streptococcus Mutans ◽  
Bovine Milk ◽  
Surface Protein ◽  
Protein Antigen ◽  
Cell Surface Protein ◽  
Milk Antibodies ◽  
Glucan Synthesis

scholarly journals The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin.

1989 ◽  
Vol 109 (2) ◽  
pp. 775-788 ◽  
Author(s):  
G Gennarini ◽  
G Cibelli ◽  
G Rougon ◽  
M G Mattei ◽  
C Goridis
Keyword(s):  
Cell Adhesion ◽  
Amino Acid ◽  
Cell Surface ◽  
Neuronal Cell ◽  
Surface Protein ◽  
Surface Interactions ◽  
Nervous System Development ◽  
Striking Similarity ◽  
Cell Surface Protein ◽  
Nonionic Detergent

Several members of the Ig superfamily are expressed on neural cells where they participate in surface interactions between cell bodies and processes. Their Ig domains are more closely related to each other than to Ig variable and constant domains and have been grouped into the C2 set. Here, we report the cloning and characterization of another member of this group, the mouse neuronal cell surface antigen F3. The F3 cDNA sequence contains an open reading frame that could encode a 1,020-amino acid protein consisting of a signal sequence, six Ig-like domains of the C2 type, a long premembrane region containing two segments that exhibit sequence similarity to fibronectin type III repeats and a moderately hydrophobic COOH-terminal sequence. The protein does not contain a typical transmembrane segment but appears to be attached to the membrane by a phosphatidylinositol anchor. Antibodies against the F3 protein recognize a prominent 135-kD protein in mouse brain. In fetal brain cultures, they stain the neuronal cell surface and, in cultures maintained in chemically defined medium, most prominently neurites and neurite bundles. The mouse f3 gene maps to band F of chromosome 15. The gene transcripts detected in the brain by F3 cDNA probes are developmentally regulated, the highest amounts being expressed between 1 and 2 wk after birth. The F3 nucleotide and deduced amino acid sequence show striking similarity to the recently published sequence of the chicken neuronal cell surface protein contactin. However, there are important differences between the two molecules. In contrast to F3, contactin has a transmembrane and a cytoplasmic domain. Whereas contactin is insoluble in nonionic detergent and is tightly associated with the cytoskeleton, about equal amounts of F3 distribute between buffer-soluble, nonionic detergent-soluble, and detergent-insoluble fractions. Among other neural cell surface proteins, F3 most resembles the neuronal cell adhesion protein L1, with 25% amino acid identity between their extracellular domains. Based on its structural similarity with known cell adhesion proteins of nervous tissue and with L1 in particular, we propose that F3 mediates cell surface interactions during nervous system development.

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