Unknown

Dataset Information

0

S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes.


ABSTRACT: 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 Ca(2+)-induced growth inhibition of human keratinocytes in culture, and that it may be possibly involved in the growth regulation in vivo as well.

SUBMITTER: Sakaguchi M 

PROVIDER: S-EPMC2173690 | biostudies-literature | 2003 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes.

Sakaguchi Masakiyo M   Miyazaki Masahiro M   Takaishi Mikiro M   Sakaguchi Yoshihiko Y   Makino Eiichi E   Kataoka Noriyuki N   Yamada Hidenori H   Namba Masayoshi M   Huh Nam-ho NH  

The Journal of cell biology 20031117 4


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 act  ...[more]

Similar Datasets

| S-EPMC2174196 | biostudies-literature
2016-07-31 | E-GEOD-74407 | biostudies-arrayexpress
2016-07-31 | GSE74407 | GEO
| S-EPMC3738260 | biostudies-literature
| S-EPMC3608085 | biostudies-literature
| S-EPMC1216828 | biostudies-literature
| S-EPMC3423538 | biostudies-literature
| S-EPMC6496262 | biostudies-literature
| S-EPMC5568930 | biostudies-literature
| S-EPMC5376294 | biostudies-literature