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1.
Exp Oncol ; 38(3): 198-201, 2016 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-27685530

RESUMO

This case report describes a rare clinical condition: metastasis of synchronous multiple primary tumors - skin melanoma and breast cancer in one axillary lymph node, confirmed with the results of clinical, morphological and immunohistochemical study of surgical material from 40 year-old woman.


Assuntos
Neoplasias da Mama/patologia , Linfonodos/patologia , Metástase Linfática/patologia , Melanoma/patologia , Neoplasias Cutâneas/patologia , Adulto , Mama/patologia , Neoplasias da Mama/terapia , Feminino , Humanos , Melanoma/terapia , Pele/patologia , Neoplasias Cutâneas/terapia
2.
J Mol Histol ; 37(8-9): 381-9, 2006 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-17103249

RESUMO

Treatment of rats with a single dose of thioacetamide (TAA) provokes centrilobular inflammation and a significant expression of heat shock protein HSP25 in hepatocytes surrounding the area of inflammation. The HSP25 accumulation in hepatocytes adjacent to inflammatory regions was confirmed by identification of positive hepatocytes concentrated at periportal areas after treatment of rats with allyl alcohol (AA) or distributed diffusely throughout liver lobule after treatment with D-galactosamine (D-gal). In our model of TAA-treated rats the use of the anti-inflammatory drug-indomethacin, and the redox-regulating drug-N-acetylcysteine (NAC), significantly attenuated TAA-induced HSP25 expression and evoked morphological changes of recruited ED1+ macrophages. Treatment of rats with gadolinium chloride (GdCl(3)) decreased considerably the number of Kupffer cells (ED2+ macrophages) without affecting significantly the number and morphology of ED1+ macrophages as well as the expression pattern of TAA-induced HSP25. Our data shows for the first time that ED1+ macrophages recruited into the liver by treatment with TAA play a significant role in HSP25 induction in hepatocytes.


Assuntos
Galactosamina/farmacologia , Proteínas de Choque Térmico/metabolismo , Fígado/metabolismo , Macrófagos/metabolismo , Proteínas de Neoplasias/metabolismo , Propanóis/farmacologia , Tioacetamida/farmacologia , Animais , Hepatócitos/efeitos dos fármacos , Hepatócitos/metabolismo , Inflamação/induzido quimicamente , Fígado/efeitos dos fármacos , Macrófagos/efeitos dos fármacos , Macrófagos/fisiologia , Masculino , Chaperonas Moleculares , Ratos
4.
J Plant Growth Regul ; 19(1): 31-44, 2000 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-11010990

RESUMO

In turgid multicellular organs, it is convenient to differentiate between the two kinds of tensile forces acting in cell walls as a result of turgor pressure. The primary forces occur both in situ and in cells isolated from the organ, whereas the secondary forces occur only in situ. The latter are an unavoidable physical consequence of the variation in mechanical parameters of tissues forming layers or strands. The most rigid tissue is under maximal tensile force, whereas the least rigid is under maximal compressive force. These forces cause tissue stresses (that is, certain tissues are under tensile stress, whereas others are under compressive stress in the organ). The primary and secondary forces result in primary and secondary stress in cell walls, respectively. The anisotropy of the primary stress is a function of cell shape. For instance, in cylindric cells the anisotropy expressed as the ratio of longitudinal to transverse stresses is 0.5. The anisotropy of the secondary stress is a function of the compound structure of the organ. For example, in the epidermis of sunflower hypocotyl, the longitudinal secondary stress is much higher than the transverse stress. The primary and secondary stresses are superimposed, and, as a consequence, the stress anisotropy in the outer thick walls of epidermal cells is greater than 1. These outer epidermal walls transmit most of the tissue stress. When the epidermis is peeled but remains turgid, only primary stress remains, but loading of the peel can reestablish the original stress anisotropy. We studied the effect of stress anisotropy changes on the orientation of cortical microtubules (CMTs) in the sunflower hypocotyl epidermis. We showed that changes in stress anisotropy cause the CMT orientation to change in the direction of maximal wall stress. In situ, the relatively high tensile tissue stress in the epidermis causes maximal stress in the longitudinal direction and relatively steep CMT orientation. When the tissue stress is removed from the epidermis by peeling, the CMTs tend to reorient toward the transverse direction, which is the direction of maximal stress in the primary component. On application of external longitudinal stress, to substitute for tissue stress, CMTs tend to reorient in the longitudinal direction. However, a relatively high rate of plastic strain is caused by the stress applied to the peel in an acid medium. This produces a less steep orientation of CMTs. It appears that the change in stress anisotropy orients the CMT in the direction in which the stress is maximal after the change, but there is also some effect of the growth rate on the orientation.

5.
Acta Biochim Pol ; 43(4): 611-21, 1996.
Artigo em Inglês | MEDLINE | ID: mdl-9104497

RESUMO

Two members of the nuclear receptor superfamily, EcR and Ultraspiracle (Usp) heterodimerize to form a functional receptor for 20-hydroxyecdysone-the key ecdysteroid controlling induction and modulation of morphogenetic events through Drosophila development. In order to study aspects of receptor function and ultimately the structural basis of the ecdysteroid receptor-DNA interaction, it is necessary to produce large quantities of purified EcR and Usp DNA-binding domains. Toward this end, we have expressed the EcR DNA-binding domain and the Usp DNA-binding domain as proteins with an affinity tag consisting of six histidine residues (6xHis-EcRDBD and 6xHis-UspDBD, respectively) using the expression vector pQE-30. Under optimal conditions, elaborated in this study, bacteria can express the recombinant 6xHis-EcRDBD to the levels of 11% of total soluble proteins and the 6xHis-UspDBD to the levels of 16%. Both proteins were purified to homogeneity from the soluble protein fraction using combination of ammonium sulphate fractionation and affinity chromatography on Ni-NTA agarose. The gel mobility shift experiments demonstrated that the purified 6xHis-EcRDBD and the 6xHis-UspDBD interact specifically with an 20-hydroxyecdysone response element from the promoter region of the hsp 27 Drosophila gene.


Assuntos
DNA Recombinante/metabolismo , Proteínas de Ligação a DNA/genética , Histidina/metabolismo , Receptores de Esteroides/genética , Animais , Cromatografia em Agarose , Clonagem Molecular , Proteínas de Ligação a DNA/isolamento & purificação , Proteínas de Ligação a DNA/metabolismo , Drosophila melanogaster , Escherichia coli/genética , Proteínas de Choque Térmico/genética , Receptores de Esteroides/isolamento & purificação , Receptores de Esteroides/metabolismo
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