The effects of hormonal and other stimuli on cell-surface Ro/SSA antigen expression by human keratinocytes in vitro: their possible role in the induction of cutaneous lupus lesions

2008 ◽  
Vol 126 (6) ◽  
pp. 554-560 ◽  
Author(s):  
S. K. JONES
Keyword(s):  
Cell Surface ◽  
Antigen Expression ◽  
Human Keratinocytes ◽  
Cutaneous Lupus

scholarly journals Distinct cell surface ligands mediate T lymphocyte attachment and rolling on P and E selectin under physiological flow.

1994 ◽  
Vol 127 (5) ◽  
pp. 1485-1495 ◽  
Author(s):  
R Alon ◽  
H Rossiter ◽  
X Wang ◽  
T A Springer ◽  
T S Kupper
Keyword(s):  
T Cells ◽  
T Cell ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Antigen Expression ◽  
Lymphocyte Antigen ◽  
Selectin Ligands ◽  
Distinct Cell ◽  
Cutaneous Lymphocyte Antigen

Memory T lymphocytes extravasate at sites of inflammation, but the mechanisms employed by these cells to initiate contact and tethering with endothelium are incompletely understood. An important part of leukocyte extravasation is the initiation of rolling adhesions on endothelial selectins; such events have been studied in monocytes and neutrophils but not lymphocytes. In this study, the potential of T lymphocytes to adhere and roll on endothelial selectins in vitro was investigated. We demonstrate that T cells can form tethers and rolling adhesions on P selectin and E selectin under physiologic flow conditions. Tethering and rolling on P selectin was independent of cell-surface cutaneous lymphocyte antigen (CLA) expression, which correlated strictly with the capacity of T cells to form rolling adhesions under flow on E selectin. T cell tethering to P selectin was abolished by selective removal of cell surface sialomucins by a P. haemolytica O-glycoprotease, while cutaneous lymphocyte antigen expression was unaffected. A sialomucin molecule identical or closely related to P selectin glycoprotein ligand-1 (PSGL-1), the major P selectin ligand on neutrophils and HL-60 cells, appears to be a major T cell ligand for P selectin. P selectin glycoprotein ligand-1 does not appear to support T cell rolling on E selectin. In turn, E selectin ligands do not appear to be associated with sialomucins. These data demonstrate the presence of structurally distinct ligands for P or E selectins on T cells, provide evidence that both ligands can be coexpressed on a single T cell, and mediate tethering and rolling on the respective selectins in a mutually exclusive fashion.

scholarly journals Upregulation of CD22 by Chidamide promotes CAR T cells functionality

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Xin Yang ◽  
Qiuxia Yu ◽  
Hao Xu ◽  
Jianfeng Zhou
Keyword(s):  
T Cells ◽  
Cell Surface ◽  
Antigen Expression ◽  
Target Antigen ◽  
Tumor Escape ◽  
Protein Distribution ◽  
Post Translational Modification ◽  
Car T Cells ◽  
Car T

AbstractTreatment failure or relapse due to tumor escape caused by reduction in target antigen expression has become a challenge in the field of CART therapy. Target antigen density is closely related to the effectiveness of CART therapy, and reduced or lost target antigen expression limits the efficacy of CART therapy and hinders the durability of CAR T cells. Epigenetic drugs can regulate histones for molecular modifications to regulate the transcriptional, translational and post-translational modification processes of target agents, and we demonstrated for the first time the role in regulating CD22 expression and its effect on the efficacy of CD22 CART. In this paper, we found that Chidamide promoted the expression of CD22 on the surface of B-cell tumor cells in vitro and in vivo, and enhanced the function of CD22 CART. As for mechanisms, we demonstrated that Chidamide did not affect CD22 mRNA transcription, but significantly increased the expression of total CD22 protein, indicating that Chidamide may upregulate cell surface CD22 expression by affecting the distribution of CD22 protein. In summary, our results suggest that Chidamide may enhance the efficacy of CD22 CART by inhibiting histone deacetylases to regulate post-transcriptional modifications that affect protein distribution to increase the expression of CD22 on the cell surface.

scholarly journals Investigation of the Filamin A–Dependent Mechanisms of Tissue Factor Incorporation into Microvesicles

2017 ◽  
Vol 117 (11) ◽  
pp. 2034-2044 ◽  
Author(s):  
Mary Collier ◽  
Camille Ettelaie ◽  
Benjamin Goult ◽  
Anthony Maraveyas ◽  
Alison Goodall
Keyword(s):  
Cell Surface ◽  
Tissue Factor ◽  
Lipid Rafts ◽  
Antigen Expression ◽  
Procoagulant Activity ◽  
Proximity Ligation Assay ◽  
Filamin A ◽  
Knock Down ◽  
The Individual

AbstractWe have previously shown that phosphorylation of tissue factor (TF) at Ser253 increases the incorporation of TF into microvesicles (MVs) following protease-activated receptor 2 (PAR2) activation through a process involving filamin A, whereas phosphorylation of TF at Ser258 suppresses this process. Here, we examined the contribution of the individual phosphorylation of these serine residues to the interaction between filamin A and TF, and further examined how filamin A regulates the incorporation of TF into MVs. In vitro binding assays using recombinant filamin A C-terminal repeats 22–24 with biotinylated phospho-TF cytoplasmic domain peptides as bait showed that filamin A had the highest binding affinities for phospho-Ser253 and double-phosphorylated TF peptides, while the phospho-Ser258 TF peptide had the lowest affinity. Analysis of MDA-MB-231 cells using an in situ proximity ligation assay revealed increased proximity between the C-terminus of filamin A and TF following PAR2 activation, which was concurrent with Ser253 phosphorylation and TF-positive MV release from these cells. Knock-down of filamin A expression suppressed PAR2-mediated increases in cell surface TF procoagulant activity without reducing cell surface TF antigen expression. Disrupting lipid rafts by pre-incubation with methyl-β-cyclodextrin prior to PAR2 activation reduced TF-positive MV release and cell surface TF procoagulant activity to the same extent as filamin A knock-down. In conclusion, this study shows that the interaction between TF and filamin A is dependent on the differential phosphorylation of Ser253 and Ser258. Furthermore, the interaction of TF with filamin A may translocate cell surface TF to cholesterol-rich lipid rafts, increasing cell surface TF activity as well as TF incorporation and release into MVs.

Proteasome Inhibitor Does Not Affect the Function of Human Immune Systems: Effects on Dendritic Cells, T Lymphocytes and NK Cells.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 3930-3930
Author(s):  
Jooeun E. Bae ◽  
Tai Yu-Tzu ◽  
Teru Hidesima ◽  
Larence Catley ◽  
Xianfeng Li ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Immune Function ◽  
Nk Cells ◽  
Proteasome Inhibitor ◽  
Antigen Expression ◽  
Antigen Uptake ◽  
Human Immune

Abstract Bortezomib is the first proteasome inhibitor approved for the therapy of multiple myeloma (MM) based on its in vitro and in vivo activity in myeloma. However, the toxicity and effects of this drug on the human immune function have not been entirely studied. In the present study, we evaluated the effects of Bortezomib on normal human immune cells including dendritic cells (DC), T lymphocytes and NK cells for cell survival, antigen expression, production of cytokines, and other key parameters of immune cell function. In our evaluation of effect of Bortezomib on DC, we did not observe significant change in the expression of cell surface antigens including CD40, CD80, CD83, CD86, HLA-ABC and HLA-DPQR molecules in terms of percentage of cells positive as well as mean fluorescence intensity (MFI). Bortezomib treated immature DC maintained the ability for antigen uptake as measured by uptake of Dextran-FITC (untrt vs. trt = 798 MFI vs. 802 MFI), maintained the expression levels of antigen uptake receptors including mannose (untrt vs. trt = 85% vs. 79%) and DEC-205 (untrt vs. trt = 49% vs. 42%), and the capacity to produce IL-12 (untrt vs. trt = 135 vs. 125 pg/ml). In addition, Bortezomib treated mature DC was able to induce comparable levels of allogenic T cell proliferation to the untreated mature DC as measured by 3[H]-Thymidine incorporation (untrt vs. trt = 212556 cpm vs. 220571 cpm). Furthermore, cell surface antigen expression including CD3, CD4, CD8, CD28, CD154 (CD40L) and TCRab on T lymphocytes were not changed by Bortezomib treatment. The treated T cells also maintained the ability to secrete IFN-g secretion in response to allogenic DC (untrt vs. trt = 85 vs. 88 pg/ml) or Staphylococcal enterotoxin B (untrt vs. trt = 131 vs. 154 pg/ml). The cytolytic activity of the NK cell population was comparable between proteasome inhibitor treated and untreated control cells against the McCAR (untrt vs. trt = 44% vs. 52%) and MM1S (49% vs. 42%) target MM cell lines. This observation was correlated with similar expression levels of CD2, CD11a, CD94, NKp30, NKp44, NKp46, and KARp50.3 activation antigens in treated versus untreated NK cells. These, in vitro results confirm lack of adverse effects of Bortezomib on immune function, and allow us to incorporate of Bortezomib in multimodality therapy that includes immunotherapy.

T cell surface antigen expression on lymphocytes of patients with AIDS during in vitro mitogen stimulation

1984 ◽  
Vol 18 (3) ◽  
Author(s):  
C. Gwyneth Munn ◽  
JamesM. Reuben ◽  
EvanM. Hersh ◽  
PeterW.A. Mansell ◽  
GuyR. Newell
Keyword(s):  
T Cell ◽  
Cell Surface ◽  
Surface Antigen ◽  
Antigen Expression ◽  
Cell Surface Antigen ◽  
Mitogen Stimulation ◽  
Surface Antigen Expression

Alterations of ultrastructure and elemental composition in cultured human epidermal keratinocytes after treatment with nitrofurazone and silver sulfadiazine

1987 ◽  
Vol 45 ◽  
pp. 676-677
Author(s):  
A. R. Crooker ◽  
M. C. Myers ◽  
T. L. Beard ◽  
E. S. Graham
Keyword(s):  
Electron Microscopy ◽  
Elemental Composition ◽  
Pyrolytic Carbon ◽  
Human Keratinocytes ◽  
Silver Sulfadiazine ◽  
Epidermal Keratinocytes ◽  
Human Epidermal Keratinocytes ◽  
Culture Systems ◽  
Cytotoxicity Endpoints

Cell culture systems have become increasingly popular as a means of screening toxic agents and studying toxic mechanisms of drugs and other chemicals at the cellular and subcellular levels. These in vitro tests can be conducted rapidly in a broad range of relevant mammalian culture systems; a variety of biological and biochemical cytotoxicity endpoints can be examined. The following study utilized human keratinocytes to evaluate the relative cytotoxicities of nitrofurazone (NF) and silver sulfadiazine (SS), the active ingredients of FURACIN(R) Topical Cream and SILVADENE(R) Cream, respectively. These compounds are anti-infectives used in the treatment of burn patients. Cell ultrastructure and elemental composition were utilized as cytotoxicity endpoints.Normal Human Epidermal Keratinocytes (HK) were prepared from the EpiPackTM culture system (Clonetics Corporation, Boulder, CO). For scanning electron microscopy (SEM) and transmission electron microscopy (TEM), cells were seeded on sterile 35 mm Falcon plastic dishes; for elemental microanalysis, cells were plated on polished pyrolytic carbon discs (E. Fullam, Latham, NY) placed in the culture dishes.

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