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Involvement of MAP‐kinases and ‐phosphatases in uptake and intracellular replication of Listeria monocytogenes in J774 macrophage cells
Author(s) -
Kügler Silke,
Schüller Stephanie,
Goebel Werner
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12763.x
Subject(s) - listeria monocytogenes , kinase , protein tyrosine phosphatase , phagocytosis , phosphatase , biology , microbiology and biotechnology , intracellular , mitogen activated protein kinase , macrophage , mapk/erk pathway , tyrosine kinase , phosphorylation , biochemistry , chemistry , signal transduction , in vitro , bacteria , genetics
In this study we show that protein tyrosine kinases and also protein tyrosine phosphatases are involved in the uptake of Listeria monocytogenes by J774 macrophages to a different extent than in the uptake of inert latex beads. In addition, protein tyrosine kinases are necessary for the intracellular growth and survival of L. monocytogenes . The expression of the MAP kinase phosphatase MKP‐1, a protein tyrosine phosphatase, is induced upon infection, and phagocytosis of L. monocytogenes by J774 cells overexpressing the MKP‐1 protein is reduced compared to control cells. The decreased phagocytosis of L. monocytogenes as a result of the MKP‐1 overexpression in J774 macrophages suggests that the activation of the MAP kinase(s) ERK‐1 and/or ERK‐2 is an essential requirement for the uptake of L. monocytogenes by J774 macrophages.

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