Márquez C, Martínez C, Boscá L
Centro de Biología Molecular, Universidad Autónoma, Madrid, Spain.
J Immunol. 1991 Jul 15;147(2):627-32.
The subcellular distribution of protein kinase C has been analyzed in murine B lymphocytes exposed to LPS, anti-IgM antibodies and phorbol dibutyrate. An accurate determination of the enzyme mobilized from the soluble to the particulate fractions by these activators, has been made possible by the use of B cells in which the major part of the activity was present in the cytosol. Upon stimulation, we have analyzed the isoenzymatic forms translocated to the B cell membrane, showing a differential pattern of isoenzyme mobilization between LPS and anti-IgM antibodies. These data, together with the different Ca2+ requirements for the activation of the translocated protein kinase C isoenzymes, might help to unravel the mechanism responsible for the clonal expansion and differentiation of B lymphocytes, induced by the two ligands.
已对暴露于脂多糖（LPS）、抗IgM抗体和佛波酯的小鼠B淋巴细胞中蛋白激酶C的亚细胞分布进行了分析。通过使用大部分活性存在于细胞质中的B细胞，得以准确测定这些激活剂促使酶从可溶性部分转移至颗粒部分的情况。受到刺激后，我们分析了转移至B细胞膜的同工酶形式，结果显示LPS和抗IgM抗体之间存在不同的同工酶转移模式。这些数据，连同转移的蛋白激酶C同工酶激活所需的不同Ca2+条件，可能有助于阐明这两种配体诱导B淋巴细胞克隆扩增和分化的机制。
