Modulation of mts1 expression in mouse and human normal and tumor cells
- 1 January 1994
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 15 (1) , 463-468
- https://doi.org/10.1002/elps.1150150163
Abstract
The mts1 gene, encoding small Ca2+‐binding protein of the S100‐family, is considered as a gene whose activity correlates with the manifestation of a metastatic phenotype of tumor cells. It was shown before that the mts1 is expressed not only in metastatic tumor cells but also in some normal tissues, namely in so‐called “lymphoid” organs: spleen, thymus; bone marrow. In this work we analyzed in more detail the expression of mts1 in human and mouse hematopoietic cells and cell lines. A high level of mts1 RNA was observed in T‐lymphocytes, neutrophils, monocytes/macrophages and in corresponding cell lines. Controversially, the mts1 gene was silent in B‐lymphocytes as well as in myeloma and erythroleukemia cell lines. The possibility of modulating the mts1 gene expression by the action of different agents was demonstrated. Mitogens, such as lipopolysaccharides (LPS), interferon (IFNγ), and concanavalin A (Con A), modulate the level of the mts1 gene expression in hematopoietic cells differently. Calcium ionophore, A23187, can also be regarded as a modulator of the mts1 gene expression, since its addition to the cells results in a substantial decrease of the mts1 RNA level. It was shown that the mts1 RNA's half‐life is relatively long, more than 24 h. We therefore believe that calcium ionophore can activate some ribonucleases which degrade the mts1 RNA. Cycloheximide prevents the effect of A23187 and stabilizes the mts1 RNA, probably by blocking the synthesis of these nucleases. Thus, the obtained data indicate that the agents which are capable of changing the physiological status of the cells also modulate the mts1 gene expression.Keywords
This publication has 11 references indexed in Scilit:
- Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E.Proceedings of the National Academy of Sciences, 1993
- Calvasculin, an encoded protein from mRNA termed pEL-98, 18A2, 42A, or p9Ka, is secreted by smooth muscle cells in culture and exhibits Ca(2+)-dependent binding to 36-kDa microfibril-associated glycoprotein.Journal of Biological Chemistry, 1992
- Transcriptional analysis of the mts1 gene with specific reference to 5' flanking sequences.Proceedings of the National Academy of Sciences, 1992
- Regulation of c-fos and c-jun protooncogene expression by the Ca(2+)-ATPase inhibitor thapsigargin.Proceedings of the National Academy of Sciences, 1991
- CREB: a Ca 2+ -Regulated Transcription Factor Phosphorylated by Calmodulin-Dependent KinasesScience, 1991
- cAMP response element-binding protein is activated by Ca2+/calmodulin- as well as cAMP-dependent protein kinase.Proceedings of the National Academy of Sciences, 1991
- Isolation and characterization of a gene specifically expressed in different metastatic cells and whose deduced gene product has a high degree of homology to a Ca2+-binding protein family.Genes & Development, 1989
- Effects of simultaneous and sequential exposure to granulocytic and monocytic inducers on the choice of differentiation pathway in HL-60 promyelocytic leukemia cellsLeukemia Research, 1988
- Increased abundance of a normal cell mRNA sequence accompanies the conversion of rat mammary cuboidal epithelial cells to elongated myoepithellal-llke cells in cultureNucleic Acids Research, 1984
- Growth-related changes in specific mRNAs of cultured mouse cells.Proceedings of the National Academy of Sciences, 1983