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1.
Int J Mol Sci ; 15(9): 16484-99, 2014 Sep 18.
Artigo em Inglês | MEDLINE | ID: mdl-25238413

RESUMO

Adolescent idiopathic scoliosis (AIS) is a common orthopedic disorder of unknown etiology and pathogenesis. Melatonin and melatonin pathway dysfunction has been widely suspected to play an important role in the pathogenesis. Many different types of animal models have been developed to induce experimental scoliosis mimicking the pathoanatomical features of idiopathic scoliosis in human. The scoliosis deformity was believed to be induced by pinealectomy and mediated through the resulting melatonin-deficiency. However, the lack of upright mechanical spinal loading and inherent rotational instability of the curvature render the similarity of these models to the human counterparts questionable. Different concerns have been raised challenging the scientific validity and limitations of each model. The objectives of this review follow the logical need to re-examine and compare the relevance and appropriateness of each of the animal models that have been used for studying the etiopathogenesis of adolescent idiopathic scoliosis in human in the past 15 to 20 years.


Assuntos
Modelos Animais de Doenças , Melatonina/deficiência , Glândula Pineal/cirurgia , Escoliose/etiologia , Adolescente , Animais , Galinhas , Feminino , Haplorrinos , Humanos , Masculino , Melatonina/fisiologia , Melatonina/uso terapêutico , Camundongos Endogâmicos , Camundongos Knockout , Fenótipo , Glândula Pineal/metabolismo , Postura , Ratos Sprague-Dawley , Roedores , Rotação , Salmão , Escoliose/prevenção & controle , Transdução de Sinais , Especificidade da Espécie , Suporte de Carga
2.
J Chromatogr B Analyt Technol Biomed Life Sci ; 828(1-2): 130-5, 2005 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-16246645

RESUMO

A homotetrameric agglutinin with a molecular mass of 130 kDa was isolated from seeds of the haricot bean. The agglutinin was isolated using a procedure that involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel and gel filtration by fast protein liquid chromatography on Superdex 200. Haricot bean agglutinin was adsorbed on DEAE-cellulose and Affi-gel blue gel. The hemagglutinating activity of the agglutinin was stable up to 40 degrees C. It underwent a 40% decline when the temperature was raised to 50 degrees C and a complete loss when the temperature was further increased to 80 degrees C. The hemagglutinating activity exhibited a time-dependent loss in activity when the agglutinin was incubated at 100 degrees C for different durations. No activity was discernible when the agglutinin was left at 100 degrees C for 1 min. The activity also underwent a decline in the presence of 500 mM FeCl(3) and CaCl(2). Haricot bean agglutinin manifested a weaker mitogenic activity than concanavalin A toward mouse splenocytes. It exhibited antiproliferative activity toward the tumor cell lines M1 [leukemia], HepG2 [hepatoma] and L1210 [leukemia] cells.


Assuntos
Proliferação de Células/efeitos dos fármacos , Fabaceae/química , Mitógenos/farmacologia , Lectinas de Plantas/química , Animais , Linhagem Celular Tumoral , Cromatografia por Troca Iônica , Eletroforese em Gel de Poliacrilamida , Fabaceae/citologia , Hemaglutininas/farmacologia , Concentração de Íons de Hidrogênio , Camundongos , Camundongos Endogâmicos C57BL , Lectinas de Plantas/farmacologia , Baço/citologia , Baço/efeitos dos fármacos , Temperatura
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