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J Biol Chem, Vol. 274, Issue 11, 7095-7102, March 12, 1999

Murine p38- Mitogen-activated Protein Kinase, a Developmentally Regulated Protein Kinase That Is Activated by Stress and Proinflammatory Cytokines

Mickey C.-T. Hu, You-ping Wang, Adel Mikhail^¶, Wan Rong Qiu, and Tse-Hua Tan

From the  Department of Cell Biology, Amgen, Inc., Thousand Oaks, California 91320, ^¶ Phylogeny, Inc., Columbus, Ohio 43212, and the  Department of Microbiology and Immunology, Baylor College of Medicine, Houston, Texas 77030

The p38 mitogen-activated protein kinases (MAPK) play a crucial role in stress and inflammatory responses and are also involved in activation of the human immunodeficiency virus gene expression. We have isolated the murine cDNA clones encoding p38- MAPK, and we have localized the p38- gene to mouse chromosome 17A3-B and human chromosome 6p21.3. By using Northern and in situ hybridization, we have examined the expression of p38- in the mouse adult tissues and embryos. p38- was expressed primarily in the lung, testis, kidney, and gut epithelium in the adult tissues. Although p38- was expressed predominantly in the developing gut and the septum transversum in the mouse embryo at 9.5 days, its expression began to be expanded to many specific tissues in the 12.5-day embryo. At 15.5 days, p38- was expressed virtually in most developing epithelia in embryos, suggesting that p38- is a developmentally regulated MAPK. Interestingly, p38- and p38- were similar serine/threonine kinases but differed in substrate specificity. Overall, p38- resembles p38-, whereas p38- resembles p38-. Moreover, p38- is activated by environmental stress, extracellular stimulants, and MAPK kinase-3, -4, -6, and -7, suggesting that p38- is a unique stress-responsive protein kinase.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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