scholarly journals Evolutionarily Conserved TCR Binding Sites, Identification of T Cells in Primary Lymphoid Tissues, and Surprising Trans-Rearrangements in Nurse Shark

2010 ◽  
Vol 184 (12) ◽  
pp. 6950-6960 ◽  
Author(s):  
Michael F. Criscitiello ◽  
Yuko Ohta ◽  
Mark Saltis ◽  
E. Churchill McKinney ◽  
Martin F. Flajnik
Keyword(s):  
T Cells ◽  
Binding Sites ◽  
Lymphoid Tissues ◽  
Nurse Shark ◽  
Evolutionarily Conserved

scholarly journals Dok-related protein negatively regulates T cell development via its RasGTPase-activating protein and Nck docking sites

2002 ◽  
Vol 158 (1) ◽  
pp. 115-125 ◽  
Author(s):  
Raffi Gugasyan ◽  
Cathy Quilici ◽  
Stacey T.T. I ◽  
Dianne Grail ◽  
Anne M. Verhagen ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Binding Sites ◽  
Lymphoid Tissues ◽  
Related Protein ◽  
Colony Stimulating Factor ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

Downstream of kinase (Dok)–related protein (DokR, also known as p56dok/FRIP/Dok-R) is implicated in cytokine and immunoreceptor signaling in myeloid and T cells. Tyrosine phosphorylation induces DokR to bind the signal relay molecules, RasGTPase-activating protein (RasGAP) and Nck. Here, we have examined the function of DokR during hematopoietic development and the requirement for RasGAP and Nck binding sites in its biological function. Retroviral-mediated expression of DokR in bone marrow cells dramatically inhibited their capacity to form colonies in vitro in response to the cytokines macrophage colony–stimulating factor and stem cell factor, whereas responses to interleukin-3 and granulocyte macrophage colony–stimulating factor were only weakly affected. When introduced into lethally irradiated mice, hematopoietic cells expressing DokR showed a drastically reduced capacity to repopulate lymphoid tissues. Most notably, DokR dramatically reduced repopulation of the thymus, in part by reducing the number of T cell precursors seeding in the thymus, but equally, through inhibiting the transition of CD4−CD8− to CD4+CD8+ T cells. Consequently, the number of mature peripheral T cells was markedly reduced. In contrast, a minimal effect on B cell and myeloid lineage development was observed. Importantly, functional RasGAP and Nck binding sites were found to be essential for the biological effects of DokR in vitro and in vivo.

Receptor Mediated Binding of the Fibrinolytic Components, Plasminogen and Urokinase, to Peripheral Blood Cells

1987 ◽  
Vol 58 (03) ◽  
pp. 936-942 ◽  
Author(s):  
Lindsey A Miles ◽  
Edward F Plow
Keyword(s):  
T Cells ◽  
B Cell ◽  
Peripheral Blood ◽  
Binding Sites ◽  
Blood Cells ◽  
High Capacity ◽  
Red Cells ◽  
Peripheral Blood Cells ◽  
Cellular Functions ◽  
Fibrinolytic Proteins

SummaryGlu-plasminogen binds to platelets; the monocytoid line, U937, and the human fetal fibroblast line, GM1380 bind both plasminogen and its activator, urokinase. This study assesses the interaction of these fibrinolytic proteins with circulating human blood cells. Plasminogen bound minimally to red cells but bound saturably and reversibly to monocytes, granulocytes and lymphocytes with apparent Kd values of 0.9-1.4 μM. The interactions were of high capacity with 1.6 to 49 × 105 sites/cell and involved the lysine binding sites of plasminogen. Both T cells and non-rosetting lymphocytes and two B cell lines saturably bound plasminogen. Urokinase bound saturably to gianulocytes, monocytes, non-rosetting lymphocytes and a B cell line, but minimally to T cells, platelets and red cells. Therefore, plasminogen binding sites of high capacity, of similar affinities, and with common recognition specificities are expressed by many peripheral blood cells. Urokinase receptors are also widely distributed, but less so than plasminogen binding sites. The binding ol plasminogen and/ or urokinase to these cells may lead to generation of cell- associated proteolytic activity which contributes to a variety of cellular functions.

Selective Generation of Gut-Tropic T Cells in Gut-Associated Lymphoid Tissues: Requirement for GALT Dendritic Cells and Adjuvant

2004 ◽  
Vol 1029 (1) ◽  
pp. 405-407 ◽  
Author(s):  
MARCUS SVENSSON ◽  
BENGT JOHANSSON-LINDBOM ◽  
MARC-ANDRÉ WURBEL ◽  
BERNARD MALISSEN ◽  
GABRIEL MÁRQUEZ ◽  
...  
Keyword(s):  
T Cells ◽  
Dendritic Cells ◽  
Lymphoid Tissues ◽  
Selective Generation

scholarly journals Trichloroethylene-induced alterations in DNA methylation were enriched in polycomb protein binding sites in effector/memory CD4+ T cells

2017 ◽  
Vol 3 (3) ◽  
Author(s):  
Kathleen M. Gilbert ◽  
Sarah J. Blossom ◽  
Brad Reisfeld ◽  
Stephen W. Erickson ◽  
Kanan Vyas ◽  
...  
Keyword(s):  
Dna Methylation ◽  
T Cells ◽  
Protein Binding ◽  
Binding Sites ◽  
Cd4 T Cells ◽  
Effector Memory ◽  
Protein Binding Sites ◽  
Polycomb Protein ◽  
Memory Cd4 T Cells

scholarly journals Nuclear Import of TFIIB Is Mediated by Kap114p, a Karyopherin with Multiple Cargo-binding Domains

2005 ◽  
Vol 16 (7) ◽  
pp. 3200-3210 ◽  
Author(s):  
Jennifer L. Hodges ◽  
Jennifer H. Leslie ◽  
Nima Mosammaparast ◽  
Yurong Guo ◽  
Jeffrey Shabanowitz ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Binding Sites ◽  
Binding Domains ◽  
Transcription Factor Iib ◽  
General Transcription Factor ◽  
Proteomic Approach ◽  
Evolutionarily Conserved ◽  
Import And Export ◽  
Transport Factors

Nuclear import and export is mediated by an evolutionarily conserved family of soluble transport factors, the karyopherins (referred to as importins and exportins). The yeast karyopherin Kap114p has previously been shown to import histones H2A and H2B, Nap1p, and a component of the preinitiation complex (PIC), TBP. Using a proteomic approach, we have identified several potentially new cargoes for Kap114p. These cargoes include another PIC component, the general transcription factor IIB or Sua7p, which interacted directly with Kap114p. Consistent with its role as a Sua7p import factor, deletion of KAP114 led to specific mislocalization of Sua7p to the cytoplasm. An interaction between Sua7p and TBP was also detected in cytosol, raising the possibility that both Sua7p and TBP can be coimported by Kap114p. We have also shown that Kap114p possesses multiple overlapping binding sites for its partners, Sua7p, Nap1p, and H2A and H2B, as well as RanGTP and nucleoporins. In addition, we have assembled an in vitro complex containing Sua7p, Nap1p, and histones H2A and H2B, suggesting that this Kap may import several proteins simultaneously. The import of more than one cargo at a time would increase the efficiency of each import cycle and may allow the regulation of coimported cargoes.

scholarly journals Lipocortin 1 binding sites on human T-cells: The population of cells with the binding sites is larger in CD8 T-lymphocytes than in CD4 T-lymphocytes

IUBMB Life ◽  
1996 ◽  
Vol 40 (6) ◽  
pp. 1167-1173
Author(s):  
Ha Won Kim ◽  
Euna Choi ◽  
Bin Yoo ◽  
Jung Ryul Choi ◽  
Young Min Park ◽  
...  
Keyword(s):  
T Cells ◽  
T Lymphocytes ◽  
Binding Sites ◽  
Cd8 T Lymphocytes ◽  
Human T Cells

scholarly journals Mechanisms regulating IgA class-specific immunoglobulin production in murine gut-associated lymphoid tissues. II. Terminal differentiation of postswitch sIgA-bearing Peyer's patch B cells.

1983 ◽  
Vol 158 (3) ◽  
pp. 649-669 ◽  
Author(s):  
H Kawanishi ◽  
L Saltzman ◽  
W Strober
Keyword(s):  
T Cells ◽  
T Cell ◽  
B Cells ◽  
Present Report ◽  
Protein A ◽  
Cell Subset ◽  
Terminal Differentiation ◽  
Lymphoid Tissues ◽  
T Cell Subset ◽  
Iga Production

Our previous studies indicated that cloned T cells obtained from Peyer's patches (PP) (Lyt-1+, 2-, Ia+, and H-2K/D+) evoked immunoglobulin (Ig) class switching of PP B cells from sIgM to sIgA cells in vitro; however, these switch T cells could not in themselves provide optimal help for the differentiation of postswitch sIgA-bearing PP B cells to IgA-secreting cells. Thus, in the present report we described studies focused on mechanisms regulating terminal differentiation of the postswitch PP sIgA-bearing B cells. First, to explore the effect of T cell-derived B cell differentiation factor(s) (BCDF) and macrophage factor(s) (MF) on the terminal maturation of PP B cells, LPS-stimulated PP B cells were co-cultured for 7 d with cloned T cells in the presence or absence of the above factors. In the absence of PP cloned T cells the BCDF and MF had only a modest effect on IgA production, whereas in the presence of PP, but not spleen cloned T cells, IgA production was increased. Next, to investigate the effect of T cells derived from a gut-associated lymphoid tissue (GALT), mesenteric lymph nodes (MLN), as well as from spleen on terminal differentiation of postswitch sIgA PP B cells, LPS-driven PP B cells were precultured with the cloned T cells to induce a switch to sIgA, and subsequently cultured with MLN or spleen T cells or a Lyt-2+-depleted T cell subset in the presence of a T-dependent polyclonal mitogen, staphylococcal protein A. Alternatively, in the second culture period BCDF alone was added, instead of T cells and protein A. Here it was found that B cells pre-exposed to switch T cells from PP, but not spleen, were induced to produce greatly increased amounts of IgA in the presence of protein A and T cells or a Lyt-2+-depleted T cell subset as well as in the presence of BCDF alone. Furthermore, in the presence of BCDF alone many B cells expressed cytoplasmic IgA. These observations strongly support the view that the terminal differentiation of postswitch sIgA B cells is governed by helper T cells and macrophages, or factors derived from such cells. Such cells or factors do not affect preswitch B cells.

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