S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes.
S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes.
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S100C/A11 是 Ca(2+) 诱导的人表皮角质形成细胞生长抑制的关键介质。
DOI：
10.1083/jcb.200304017
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发表时间：
2003-11-24
影响因子：
7.8
通讯作者：
Huh, NH
中科院分区：
文献类型：
--
作者：
Sakaguchi, M;Miyazaki, M;Takaishi, M;Sakaguchi, Y;Makino, E;Kataoka, N;Yamada, H;Namba, M;Huh, NH
细胞外Ca2+的增加诱导人角质形成细胞在培养中生长停滞和分化。我们研究了S100C/A11可能参与这种生长调节。当细胞暴露于高Ca2+时，S100C/A11在10Thr和94Ser位点特异性磷酸化。磷酸化促进了S100C/A11与核仁蛋白的结合，导致S100C/A11的核易位。在细胞核中，S100C/A11从核蛋白中释放出Sp1/3。由此产生的游离Sp1/3转录激活p21CIP1/WAF1，这是细胞生长的代表性负调节因子。将抗s100c /A11抗体引入细胞后，Ca2+诱导的生长抑制和p21CIP1/WAF1的诱导作用在很大程度上被消除。在人表皮上基底层分化细胞的细胞核中检测到S100C/A11，而在基底层增殖细胞的细胞核中检测不到。这些结果表明，S100C/A11是Ca2+诱导的人角质形成细胞生长抑制的关键介质，并可能参与体内的生长调节。
An increase in extracellular Ca2+ induces growth arrest and differentiation of human keratinocytes in culture. We examined possible involvement of S100C/A11 in this growth regulation. On exposure of the cells to high Ca2+, S100C/A11 was specifically phosphorylated at 10Thr and 94Ser. Phosphorylation facilitated the binding of S100C/A11 to nucleolin, resulting in nuclear translocation of S100C/A11. In nuclei, S100C/A11 liberated Sp1/3 from nucleolin. The resulting free Sp1/3 transcriptionally activated p21CIP1/WAF1, a representative negative regulator of cell growth. Introduction of anti-S100C/A11 antibody into the cells largely abolished the growth inhibition induced by Ca2+ and the induction of p21CIP1/WAF1. In the human epidermis, S100C/A11 was detected in nuclei of differentiating cells in the suprabasal layers, but not in nuclei of proliferating cells in the basal layer. These results indicate that S100C/A11 is a key mediator of the Ca2+-induced growth inhibition of human keratinocytes in culture, and that it may be possibly involved in the growth regulation in vivo as well.
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影响因子：
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