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1.
Clin Appl Thromb Hemost ; 10(4): 311-21, 2004 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-15497017

RESUMO

A molecular mechanism responsible for varicose vein occurrence was investigated. The role of potential cell cycle regulator p21 and programmed cell death in the pathology leading to the proximal long saphenous vein (LSV) incompetence was investigated. Proximal LSV specimens were obtained from 40 patients with primary varicose veins who had undergone crossectomy. The expression of the p21, p53, and fas encoding genes was investigated by the means of real-time RT-QPCR. Immunostaining for gene product presence, proliferating cell nuclear antigen (PCNA), and apoptotic cells (TUNEL assay) was carried out. The results were compared to the control healthy vein specimens and correlated with pathologic examination findings (of the valve and vein structure). A significant increase in p21, p53, and fas mRNA expression were reported in the proximal incompetent veins. The expression of p21 correlated with expression of p53 (r = 0.658; p<0.05) and negative correlation between media apoptotic index and p21 mRNA expression was found (r = -0.493; p<0.05). Decrease in the muscular component within the media and disturbances of the local structure in the incompetent LSVs were reported. Fas overexpression did not correlate with p53 expression level and did not correlate with apoptotic cell number in the respective vein layers. PCNA-positive cells were present more frequently in the media of the control veins, especially in young subjects. Apoptosis downregulation, cell cycle inhibition and smooth muscle cell hypertrophy are important factors influencing vein wall disturbances related to sapheno-femoral junction incompetence.


Assuntos
Proteínas de Ciclo Celular/genética , Veia Safena/patologia , Proteína Supressora de Tumor p53/genética , Varizes/etiologia , Receptor fas/genética , Adulto , Idoso , Apoptose , Estudos de Casos e Controles , Proteínas de Ciclo Celular/análise , Inibidor de Quinase Dependente de Ciclina p21 , Feminino , Humanos , Imuno-Histoquímica , Masculino , Pessoa de Meia-Idade , Músculo Liso Vascular/patologia , Antígeno Nuclear de Célula em Proliferação/análise , Antígeno Nuclear de Célula em Proliferação/genética , RNA Mensageiro/análise , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Veia Safena/química , Distribuição Tecidual , Proteína Supressora de Tumor p53/análise , Receptor fas/análise
2.
Cell Mol Biol Lett ; 8(4): 991-1003, 2003.
Artigo em Inglês | MEDLINE | ID: mdl-14668922

RESUMO

The aim of this study was to determine whether Desulfovibrio desulfuricans-derived LPS stimulate the release of IL-6 and IL-8 from ECs and the expression of their adhesion molecules at the transcriptional level. Confluent monolayers of HUVEC were incubated in the absence or presence of 20 microg/ml and 60 microg/ml LPSs derived from the DdT and DdA bacterial strains. Also, the simultaneous stimulation of cells with LPSs and IL-1beta was evaluated. The levels of cytokines released were measured using ELISA. LPS-activated HUVEC increased the secretion of both IL-6 and IL-8, which was not LPS dose dependent. The expression of E-selectin and VCAM-1 was assessed by TR-PCR. The transcripts were detectable at all the concentrations (20, 40, 60 microg/ml) of LPSs used. These results suggest that D. desulfuricans LPS may activate immune functions in endothelial cells and influence the inflammatory response during bacteremia caused by these bacteria.


Assuntos
Selectina E/metabolismo , Células Endoteliais/metabolismo , Interleucina-8/metabolismo , Lipopolissacarídeos/farmacologia , Molécula 1 de Adesão de Célula Vascular/metabolismo , Células Cultivadas , Desulfovibrio desulfuricans/química , Células Endoteliais/efeitos dos fármacos , Humanos , Interleucina-1/farmacologia , Interleucina-6/metabolismo , Lipopolissacarídeos/isolamento & purificação , RNA Mensageiro/metabolismo , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Veias Umbilicais/metabolismo
3.
J Inorg Biochem ; 90(3-4): 149-54, 2002 Jun 07.
Artigo em Inglês | MEDLINE | ID: mdl-12031807

RESUMO

The structure of the tin(III) complex [Sn(2)(CH(2)CH(2)CN)(6)] has been determined. There are two independent molecules in the crystal, both adopt distorted eclipsed conformation. The molecular and electronic structures of this compound have been studied both at the semiempirical level and with the use of non-empirical ab initio methods. The calculated Sn-Sn distances agree well with those found crystallographically. The results of calculations showed that the eclipsed conformation of complex is more stable as compared with staggered conformation. The compound show modest cytotoxic activity against A549 and HSMC cells.


Assuntos
Antineoplásicos/química , Antineoplásicos/farmacologia , Compostos Orgânicos de Estanho/química , Compostos Orgânicos de Estanho/farmacologia , Antineoplásicos/síntese química , Divisão Celular/efeitos dos fármacos , Linhagem Celular , Cristalografia por Raios X , Eletroquímica , Humanos , Estrutura Molecular , Compostos Orgânicos de Estanho/síntese química , Células Tumorais Cultivadas
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