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HMC-1 Cells (hmc-1 + cell)

Distribution by Scientific Domains
Medical Sciences60%

Selected Abstracts

Mast cell lines HMC-1 and LAD2 in comparison with mature human skin mast cells , drastically reduced levels of tryptase and chymase in mast cell lines

EXPERIMENTAL DERMATOLOGY, Issue 9 2010
Sven Guhl
Please cite this paper as: Mast cell lines HMC-1 and LAD2 in comparison with mature human skin mast cells , drastically reduced levels of tryptase and chymase in mast cell lines. Experimental Dermatology 2010; 19: 845,847. Abstract:, To circumvent the costly isolation procedure associated with tissue mast cells (MC), two human MC lines, i.e. HMC-1 and LAD2, are frequently employed, but their relation to mature MC is unknown. Here, we quantitatively assessed their expression of MC markers in direct comparison to skin MC (sMC). sMC expressed all lineage markers at highest and HMC-1 cells at lowest levels. LAD2 cells expressed comparable high-affinity IgE receptor , (Fc,RI,) and Fc,RI, but less Fc,RI, than sMC and displayed slightly reduced, but robust Fc,RI-mediated histamine release. Only minor differences were found for total histamine content and c-Kit expression. Huge, and to this level unexpected, differences were found for MC tryptase and chymase, with sMC >>> LAD2 > HMC-1. Taken together, HMC-1 cells represent very immature malignantly transformed MC, whereas LAD2 cells can be considered intermediately differentiated. Because of the minute levels of MC proteases, MC lines can serve as surrogates of tissue MC to a limited degree only. [source]

The role of the cutaneous cholinergic system in guttate psoriasis

EXPERIMENTAL DERMATOLOGY, Issue 7 2008
W. Dyck
In previous studies, high levels of acetylcholine (ACh) have been reported in psoriasis lesions. In addition, patients with guttate psoriasis respond to oral treatment with atropine. We wanted to know how the cutaneous cholinergic system could be involved in this process. Since mast cells (MC) are characteristic components of the inflammatory infiltrate of guttate psoriasis, we compared ACh receptor (AChR) composition and ACh production in both epidermis and mast cells of 10 patients with guttate psoriasis in involved and uninvolved skin on protein level using immunofluorescence and in a MC line (HMC-1) using PCR. We could confirm the presence of numerous MC in guttate psoriasis lesion. Both in vivo and in vitro, MC lacked expression of cholinacetyltransferase (ChAT), vesicular acetylcholintransorter (VAChT) and cholintransporter-1 (ChT-1) but contained high levels of acetylcholinesterase (AChE). In mast cells of both involved and uninvolved skin we found both nicotinic (,3, ,5, ,7, ,9, ,10, ,2 and ,4 subunits) and muscarinic (M1, M3, M4, M5) AChR. In HMC-1 cells all AChR subunits found in skin where present on mRNA level, except ,7 and ,2. In lesional epidermis both ACh production and AChR expression was shifted from the basal to the suprabasal layers especially the nicotinic ,3, ,5, ,9, ,2 and ,4 and the muscarinic M3 and M5 AChR subunits. Our results exclude a role of the cholinergic system in the initiation of keratinocyte proliferation in the basal epidermal layer but point towards a role of epidermal AChR in suprabasal processes, most likely terminal differentiation and barrier formation as has been shown in other systems. Most importantly, mast cells are targets of paracrine and endocrine effects mediated by ACh and choline thus modulating inflammatory processes like guttate psoriasis and explaining the clinical efficacity of anticholinergic drugs like atropine. [source]

Phlomis umbrosa root inhibits mast cell-dependent allergic reactions and inflammatory cytokine secretion

PHYTOTHERAPY RESEARCH, Issue 2 2008
Tae-Yong Shin
Abstract The effect of an aqueous extract of Phlomis umbrosa Turcz. (Labiatae) root (PUAE) on mast cell-dependent allergic reactions and inflammatory cytokine secretion were investigated. PUAE (0.01,1 g/kg) inhibited compound 48/80-induced systemic allergic reaction. When PUAE was employed in a systemic allergic reaction test, the plasma histamine levels were reduced in a dose-dependent manner. PUAE (0.1 and 1 g/kg) also significantly inhibited the local allergic reaction activated by anti-dinitrophenyl (DNP) IgE. PUAE (0.001,1 mg/mL) dose-dependently inhibited the histamine release from rat peritoneal mast cells activated by compound 48/80 or anti-DNP IgE. PUAE (0.01,1 mg/mL) inhibited the secretion of interleukin (IL)-1, in phorbol 12-myristate 13-acetate plus calcium ionophore A23187-stimulated human mast cell line (HMC-1) cells. PUAE (1 mg/mL) inhibited the gene expression and production of the main inflammatory cytokine, TNF- ,, in HMC-1 cells. These results provide evidence that PUAE may be beneficial in the treatment of allergic diseases. Copyright © 2007 John Wiley & Sons, Ltd. [source]

Phytoglycoprotein (75,kDa) inhibits expression of interleukin-1, stimulated by DEHP in human mast cells

CELL BIOCHEMISTRY AND FUNCTION, Issue 5 2010
Phil-Sun Oh
Abstract The purpose of this study is to investigate the inhibitory effect of a glycoprotein (CTB glycoprotein, 75,kDa) isolated from Cudrania tricuspidata Bureau (CTB) on the di-(2-ethylhexyl)phthalate (DEHP) induced expression of allergic-inflammation-related mediators in human mast cells. The changes on the levels of intracellular reactive oxygen species (ROS), mitogen-activated protein kinase (MAPK), transcription factor [nuclear factor (NF)- ,B], and allergic inflammatory mediators [cyclooxygenase (COX)-2 and interleukin (IL)-1,] were evaluated using Western blot and RT-PCR. Our results showed that the CTB glycoprotein in the presence of DEHP inhibits the production of intracellular ROS, the phosphorylation of ERK1/2, and p38 MAPK in HMC-1 cells. In addition, the CTB glycoprotein has suppressive effects on the transcriptional activation of NF- ,B, and on the expression levels of COX-2 and IL-1, in DEHP-treated HMC-1 cells. In conclusion, the CTB glycoprotein has a strong anti-inflammatory effect on the activities of allergic inflammatory mediators indirectly caused by DEHP in HMC-1 cells. Copyright © 2010 John Wiley & Sons, Ltd. [source]