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1.
Prostate Cancer Prostatic Dis ; 7(4): 343-9, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-15356680

RESUMO

INTRODUCTION: Treatment options for lymph node positive prostate cancer are limited. We retrospectively compared patients who underwent external radiotherapy (ERT) to patients treated by radical prostatectomy (RPX). MATERIALS AND METHODS: A total of 102 lymph node positive patients from the RPX series at Ulm University were evaluated. In all, 76 patients received adjuvant androgen withdrawal as part of their primary treatment. In the ERT group, 44 patients were treated at the University of Michigan using a fractionated regimen. Of these, 21 patients received early adjuvant hormonal therapy. Patients with neoadjuvant therapy before RPX or ERT were excluded. RESULTS: In the RPX group, PSA nadir (nadir < or = 0.2 vs > 0.2 ng/ml) showed a strong association with outcome. In the ERT group, pretreatment PSA was an independent predictor of outcome (P = 0.04) and patients with adjuvant hormonal therapy had a significant longer recurrence-free interval compared to patients without adjuvant therapy (P = 0.004). Comparing only patients with adjuvant hormonal treatment after cancer-specific therapy, the ERT-treated patients had a borderline longer PSA recurrence-free survival time compared to the RPX-treated patients (P = 0.05). CONCLUSIONS: In case of positive lymph nodes, RPX and ERT might be considered and need to be explained to the patient. For future treatment decisions, the presented findings and a potential survival benefit need to be evaluated in a larger prospective setting.


Assuntos
Linfonodos/patologia , Prostatectomia , Neoplasias da Próstata/radioterapia , Neoplasias da Próstata/cirurgia , Idoso , Quimioterapia Adjuvante , Humanos , Masculino , Pessoa de Meia-Idade , Terapia Neoadjuvante , Recidiva Local de Neoplasia/radioterapia , Recidiva Local de Neoplasia/cirurgia , Estadiamento de Neoplasias , Antígeno Prostático Específico/metabolismo , Neoplasias da Próstata/patologia , Dosagem Radioterapêutica , Estudos Retrospectivos
2.
J Histochem Cytochem ; 40(9): 1309-18, 1992 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-1506668

RESUMO

We used a modification of fracture-flip to reveal the nanoanatomy of the inner surface of the plasma membrane in promastigotes of Leishmania. After freeze-fracture, lightly fixed promastigotes were coated with a stabilizing layer of carbon evaporated from an electron gun, thawed, and washed. Fractured promastigotes attached to the carbon casts by the protoplasmic (i.e., inner) halves of their plasma membranes were treated with Triton X-100, followed by exposure to low concentrations of trypsin and thorough washing. This was followed by picking up and flipping of the replicas, followed by air-drying. The actual inner surfaces of the plasma membrane were then imaged by platinum shadowing. Extended, three-dimensional, high-resolution views of the inner surface of the plasma membrane showed parallel arrays of microtubules (average spacing 47 nm) closely apposed to the inner surface. Cytochemical labeling confirmed the morphological identification of both subpellicular and flagellar microtubules, as determined by treatment with mouse monoclonal anti-alpha- or anti-beta-tubulin, followed by labeling with goat anti-mouse IgG adsorbed to colloidal gold. Removal of the microtubules revealed parallel arrays of particles (average diameter 17 nm). We hypothesize that these particles represent the cytoplasmic portion of proteins that link the microtubules to the plasma membrane.


Assuntos
Leishmania/ultraestrutura , Microtúbulos/metabolismo , Animais , Membrana Celular/metabolismo , Membrana Celular/ultraestrutura , Técnica de Fratura por Congelamento , Ouro , Imuno-Histoquímica , Microscopia Eletrônica , Microtúbulos/ultraestrutura
3.
Invest Ophthalmol Vis Sci ; 33(7): 2284-92, 1992 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-1607240

RESUMO

Heightened interest in meibomian glands dysfunction prompted the authors to examine the ultrastructure of the glandular epithelium in specimens of surgical origin, by thin section and freeze-fracture electron microscopies. In meibomian glands, the morphology and ultrastructure of acinar cells varies considerably according to their stage of holocrine differentiation. This study shows close interdependence between fat droplets and Golgi apparatus or endoplasmic reticulum. As the cells initiate their differentiation, the smooth endoplasmic reticulum and the Golgi apparatus become prominent and the first small lipid droplets appear in the cytoplasm. When fractured through a plane close to their surface, lipid droplets appear onion-like structured, ie made up of a variable number of irregular shaped concentric lamellae. This lamellar organization suggests that membranes are not only involved in synthesis, but also that some of their components are incorporated in the fat droplets. The authors conclude that human meibomian glands are a holocrine glandular complex that, despite great differences in type and location, present basic similarities with sebaceous glands.


Assuntos
Glândulas Tarsais/ultraestrutura , Organelas/ultraestrutura , Adolescente , Adulto , Epitélio/ultraestrutura , Feminino , Técnica de Fratura por Congelamento , Humanos , Masculino , Pessoa de Meia-Idade
4.
Cell Growth Differ ; 2(5): 257-65, 1991 May.
Artigo em Inglês | MEDLINE | ID: mdl-1832292

RESUMO

The product of protooncogene c-mos, pp39mos, is expressed and functions during oocyte maturation. We have previously found that pp39mos is complexed with and phosphorylates tubulin. In addition, part of pp39mos is localized on mitotic spindle and spindle pole regions in c-mosxe-transformed NIH/3T3 cells. Here, we further characterized the interaction between pp39mos and tubulin. We show that mos product synthesized in vitro appears in a 500 kD complex and can oligomerize with tubulin in vitro under tubulin polymerization conditions. Moreover, conditions which favor microtubule depolymerization facilitate pp39mos extraction from c-mosxe-transformed NIH/3T3 cells. We also show by immunofluorescence and immunoelectron microscopy that pp39mos is localized on microtubules. Thus, in vitro and in vivo the mos product is associated with tubulin and microtubules, respectively. Therefore, the mos product may be involved in the modification of microtubules and formation of the spindle.


Assuntos
Microtúbulos/metabolismo , Proteínas Proto-Oncogênicas/metabolismo , Tubulina (Proteína)/metabolismo , Animais , Linhagem Celular , Técnicas In Vitro , Camundongos , Microscopia Eletrônica , Oócitos/metabolismo , Ligação Proteica , Proteínas Proto-Oncogênicas c-mos
5.
Mol Reprod Dev ; 28(4): 410-8, 1991 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-2064784

RESUMO

Freeze-fracture electron microscopy reveals that intramembrane particles are concentrated in a band encircling the posterior portion of the acrosome of Strongylocentrotus purpuratus sperm. Two colloidal gold labeling methods, label-fracture and replica-staining fracture-flip, were employed to show that the plant lectin wheat germ agglutinin, which recognizes a 210 kDa sperm surface glycoprotein, binds to this localized band of intramembrane particles. Monoclonal antibody J18/2, which also recognizes the 210 kDa surface glycoprotein, shows this localized binding in approximately 20% of the sperm observed in this study. The majority of sperm displayed a uniform distribution of receptor sites for monoclonal antibody J18/2. Since wheat germ agglutinin and monoclonal antibody J18/2 are known to agglutinate Strongylocentrotus purpuratus sperm but not sperm of another sea urchin, Lytechinus pictus, similar determinations were made for the latter species. Lytechinus pictus sperm are not labeled with wheat germ agglutinin and are only sparsely labeled with monoclonal antibody J18/2. The acrosomal localizations of wheat germ agglutinin and monoclonal antibody J18/2 receptors in Strongylocentrotus purpuratus sperm are consistent with the involvement of the 210 kDa surface glycoprotein in an egg jelly-induced sperm acrosome reaction. Low-temperature post-embed labeling of thin sections with wheat germ agglutinin and monoclonal antibody J18/2 show concentrations of label within the acrosomal vesicle of Strongylocentrotus purpuratus sperm, suggesting the presence of an intracellular storage site for the 210 kDa glycoprotein.


Assuntos
Sítios de Ligação de Anticorpos , Glicoproteínas de Membrana/análise , Receptores Mitogênicos/análise , Cabeça do Espermatozoide/ultraestrutura , Animais , Anticorpos Monoclonais/imunologia , Técnica de Fratura por Congelamento , Imuno-Histoquímica , Masculino , Glicoproteínas de Membrana/metabolismo , Microscopia Eletrônica , Receptores Mitogênicos/metabolismo , Ouriços-do-Mar , Aglutininas do Germe de Trigo/metabolismo
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