Immunocytochemical Localization of Anion Exchanger-2 (AE-2) in the Dorsal Root Ganglion of Adult Rats
Immunocytochemical Localization of Anion Exchanger-2 (AE-2) in the Dorsal Root Ganglion of Adult Rats
复制标题
成年大鼠背根神经节中阴离子交换器 2 (AE-2) 的免疫细胞化学定位
DOI:
10.2220/biomedres.23.213
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发表时间:
2002
影响因子:
1.2
通讯作者:
Y. Ogawa
中科院分区:
文献类型:
--
作者:
S. Wakisaka;S. Honma;T. Onishi;S. Toyosawa;Y. Ogawa
Nearly a century ago, Otto Warburg made the seminal observation that tumors metabolize glucose more rapidly than normal tissue and do so even in the presence of ox-ygen [1,2]. Since this observation, numerous studies have addressed how cancer cells enhance glucose uptake and the mechanisms by which this additional glucose is utilized [3,4]. Several lines of evidence suggest that can-cer cells reprogram their metabolic networks through coordinated regulation of enzyme expression and activi-ty to enhance anabolic processes. One process that influ-ences expression of metabolic enzymes important in cancer is alternative splicing. Among the alternatively spliced genes expressed in cancer cells is the embryonic isoform of pyruvate kinase, PKM2 [5]. This observation was pioneered by Erich Eigenbrodt and is now consid-ered as a major node in the regulation of cancer metabo-lism [6,7]. In the following commentary, we describe the mechanisms by which the activity of PKM2 is controlled in tumors to facilitate cell growth, work that has stemmed from Eigenbrodt’s efforts exploring the onco-genic role of this glycolytic isozyme. Pyruvate kinase (PK) is a glycolytic enzyme that converts phosphoenolpyruvate (PEP) and ADP into pyruvate and ATP. This reaction is both a rate-limiting step and the final step in glycolysis [6]. In mammals, there are two genes that encode four PK isozymes [8]. Alternative pro-moter utilization of the
影响因子:
8.8
作者:
Snell, K;Natsumeda, Y;Eble, J N;Glover, J L;Weber, G
通讯作者:
Weber, G