scholarly journals The influence of LTS-4, a saponoside from Lysimachia thyrsiflora L., on human skin fibroblasts and human melanoma cells

Author(s):  
Agnieszka Galanty ◽  
Marta Michalik ◽  
Łukasz Sędek ◽  
Irma Podolak

AbstractWe investigated the effect of a triterpene saponoside from Lysimachia thyrsiflora L. upon the viability, proliferation, morphology and cell motility of human melanoma HTB-140 cells and human skin fibroblasts (HSFs). The compound, denoted LTS-4, decreased the viability and rate of cell growth of both cell types in a time-and dose-dependent manner, and proved cytotoxic against cancer cells at significantly lower concentrations than for fibroblasts. LTS-4 also affected the morphology of the examined cells, causing vacuolisation and actin cytoskeleton disintegration, and had an inhibitory effect on the tumour cell motility.

1999 ◽  
Vol 277 (4) ◽  
pp. C755-C765 ◽  
Author(s):  
William P. Schilling ◽  
William G. Sinkins ◽  
Mark Estacion

Maitotoxin (MTX), a potent cytolytic agent, activates Ca2+ entry via nonselective cation channels in virtually all types of cells. The identity of the channels involved and the biochemical events leading to cell lysis remain unknown. In the present study, the effect of MTX on plasmalemmal permeability of human skin fibroblasts was examined. MTX produced a time- and concentration-dependent increase in cytosolic free Ca2+ concentration that depended on extracellular Ca2+ and was relatively insensitive to blockade by extracellular lanthanides. MTX also produced a time- and concentration-dependent increase in plasmalemma permeability to larger molecules as indicated by 1) uptake of ethidium (314 Da), 2) uptake of YO-PRO-1 (375 Da), 3) release of intracellular fura 2 (636 Da), 4) uptake of POPO-3 (715 Da), and, ultimately, 5) release of lactate dehydrogenase (relative molecular weight of 140,000). At the single cell level, uptake of YO-PRO-1 correlated in time with the appearance of large MTX-induced membrane currents carried by the organic cation, N-methyl-d-glucamine (167 Da). Thus MTX initially activates Ca2+-permeable cation channels and later induces the formation of large pores. These effects of MTX on plasmalemmal permeability are similar to those seen on activation of P2Z/P2X7 receptors in a variety of cell types, raising the intriguing possibility that MTX and P2Z/P2X7 receptor stimulation activate a common cytolytic pore.


1989 ◽  
Vol 180 (1) ◽  
pp. 84-93 ◽  
Author(s):  
H.Peter Rodemann ◽  
Klaus Bayreuther ◽  
Pal I. Francz ◽  
Klaus Dittmann ◽  
Mario Albiez

2004 ◽  
Vol 49 (3) ◽  
pp. 265-274 ◽  
Author(s):  
Yan-Tao Han ◽  
Zhi-Wu Han ◽  
Guo-Ying Yu ◽  
Yue-Jun Wang ◽  
Rui-Yao Cui ◽  
...  

1986 ◽  
Vol 19 (1) ◽  
pp. 39-47 ◽  
Author(s):  
G. L. Whitson ◽  
W. L. Carrier ◽  
Andrew A. Francis ◽  
C. C. Shih ◽  
S. Georghiou ◽  
...  

1992 ◽  
Vol 127 (1) ◽  
pp. 44-51 ◽  
Author(s):  
Yoshimasa Shishiba ◽  
Yumi Imai ◽  
Ritsuko Odajima ◽  
Yasunori Ozawa ◽  
Taeko Shimizu

Hyaluronic acid and proteoglycan accumulate in the affected skin of Graves' disease patients with pretibial myxedema (PTM). We aimed to determine whether an autoantibody IgG circulating in PTM patients stimulates proteoglycan synthesis in human skin fibroblasts, resulting in PTM. IgGs were purified from 14 normal subjects, 11 Graves' disease patients with PTM, 5 Graves' disease patients with active ophthalmopathy and 15 Graves' disease patients with neither PTM nor ophthalmopathy. Human skin fibroblasts were incubated with the IgGs and labeled with [35S]sulfate. The medium and cell layer were separated and the proteoglycan was extracted. The 35S radioactivity in the proteoglycan fraction was measured. Compared with normal IgGs or with those of Graves' disease without PTM or ophthalmopathy, PTM IgGs significantly increased the incorporation of the 35S into the proteoglycan. The effect of PTM IgG was dose-dependent. As PTM IgG did not alter degradation of the 35S labeled proteoglycan, an increase in 35S incorporation reflects increased synthesis. The effect was mediated through a mechanism other than adenylate cyclase activation. The present study demonstrates the presence of an autoantibody in PTM IgG that stimulates proteoglycan production through human skin fibroblasts. This is not correlated with the thyroid stimulating antibody activity. It is suggested that the activity of this antibody leads to the development of PTM.


1999 ◽  
Vol 33 (3) ◽  
pp. 267-276
Author(s):  
Munehiro Iketani ◽  
Yukiko Matsunaga ◽  
Toshio Nishiyama ◽  
Minoru Fukuda ◽  
Tasuku Takamatsu

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