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1.
Radiology ; 189(3): 915-7, 1993 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-8234725

RESUMO

The authors present phantom test results for a stereotaxic device that may permit simple, rapid, and accurate needle biopsy and localization of breast lesions detected at contrast material-enhanced magnetic resonance (MR) mammography. The mechanical accuracy of this prototype MR breast localizer is approximately plus or minus 3.5 mm at 5 cm.


Assuntos
Neoplasias da Mama/diagnóstico , Mama/patologia , Imageamento por Ressonância Magnética , Técnicas Estereotáxicas/instrumentação , Biópsia por Agulha/métodos , Feminino , Humanos , Modelos Estruturais
2.
J Cell Biol ; 104(5): 1291-7, 1987 May.
Artigo em Inglês | MEDLINE | ID: mdl-3494733

RESUMO

The lateral mobility of the epidermal growth factor (EGF) receptor in the plane of the plasma membrane of cultured A431 cells was investigated using direct and indirect fluorescent probes to measure the generation and relaxation of electric field-induced receptor asymmetry. A steady electric field of 15 V/cm for 30 min at 23 degrees C induced a redistribution of the unoccupied EGF receptor such that there was approximately a three-fold higher concentration of receptors at the cathode-facing pole. After termination of the field, the unoccupied receptors back diffused at 37 degrees C with a rate corresponding to a diffusion coefficient of 2.6-3.5 X 10(-10) cm2/s. No diffusion was detected at 4 degrees C. Formation of the hormone-receptor complex is known to induce receptor clustering and internalization. By inhibiting internalization with metabolic poisons, we were able to study the cell surface mobility of clusters of the hormone-receptor complex. The same degree of asymmetry was induced when the occupied receptor was exposed to an electric field and the rate of back diffusion of clusters of the hormone-receptor complex corresponded to a diffusion coefficient of 0.68-0.95 X 10(-10) cm2/s. Although the unoccupied receptor is somewhat more mobile than the hormone-receptor complex, it was still far less mobile than one would predict for an unconstrained protein imbedded in a phospholipid bilayer.


Assuntos
Membrana Celular/fisiologia , Receptores ErbB/fisiologia , Linhagem Celular , Membrana Celular/ultraestrutura , Difusão , Estimulação Elétrica , Fator de Crescimento Epidérmico/metabolismo , Humanos
3.
Exp Cell Res ; 155(1): 213-21, 1984 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-6541589

RESUMO

A class of proteins from mouse mammary epithelial cells has been isolated which, like the calcium-binding protein calmodulin (CaM), binds to phenothiazine in a calcium-dependent manner. These proteins do not bind to phenothiazine through binding to CaM; we infer that they are calcium-binding proteins, and that they may be related to the similarly isolated 'calcimedins' of Moore, P D & Dedman, J, J biol chem 257 (1982) 9663 [8]. In primary cultures of mouse mammary cells on collagen gels, synthesis of certain of these proteins is associated with the spreading of cells to form monolayers; failure of cells to spread and differentiate, through omission of serum from culture medium, results in the inhibition of calcium-binding protein synthesis, with the exception of CaM and a 15 kD species. The CaM/15 kD pair are prominent during all phases of culture, and are secreted during the secretory differentiation phase of culture (floating gels). We propose that these calcium-binding proteins play a specific role in the motility of mammary epithelial cells and that they may also be involved in mammary secretory differentiation.


Assuntos
Proteínas de Ligação ao Cálcio/biossíntese , Diferenciação Celular , Movimento Celular , Glândulas Mamárias Animais/metabolismo , Animais , Calmodulina , Células Cultivadas , Cromatografia de Afinidade , Células Epiteliais , Epitélio/metabolismo , Glândulas Mamárias Animais/fisiologia , Camundongos , Camundongos Endogâmicos , Peso Molecular , Fenotiazinas
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