A5017178156- Protein Tyrosine Phosphatases
- Cell Adhesion Molecules Research
- Blood Coagulation and Thrombosis Mechanisms
- Melanoma and MAPK Pathways
- Bioactive Compounds and Antitumor Agents
- Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Biochemical and Molecular Research
- Research on Leishmaniasis Studies
- Protein Kinase Regulation and GTPase Signaling
- Knee injuries and reconstruction techniques
- Signaling Pathways in Disease
- Cellular Mechanics and Interactions
- Osteoarthritis Treatment and Mechanisms
- Muscle Physiology and Disorders
- Ubiquitin and proteasome pathways
- NF-κB Signaling Pathways
- Cancer-related Molecular Pathways
- Skin and Cellular Biology Research
- Cell death mechanisms and regulation
- Chromosomal and Genetic Variations
- DNA Repair Mechanisms
- Mitochondrial Function and Pathology
- Trypanosoma species research and implications
Cancer Research UK
2015
Cancer Research UK Scotland Institute
2015
University of Strathclyde
2004-2011
Friedrich-Alexander-Universität Erlangen-Nürnberg
2000
Inserm
1996
Centre National de la Recherche Scientifique
1996
Institut de génétique et de biologie moléculaire et cellulaire
1996
In this study we generated a novel dual specific phosphatase 4 (DUSP4) deletion mouse using targeted strategy in order to examine the role of MAP kinase phosphatase-2 (MKP-2) immune responses. Lipopolysaccharide (LPS) induced rapid, time and concentration-dependent increase MKP-2 protein expression bone marrow-derived macrophages from MKP-2+/+ but not MKP-2−/− mice. LPS-induced JNK p38 phosphorylation was significantly increased prolonged whilst ERK unaffected. also potentiated...
Mitogen-activated protein kinase phosphatase-2 (MKP-2) is a type 1 nuclear dual specific phosphatase (DUSP) implicated in number of cancers. We examined the role MKP-2 regulation MAP phosphorylation, cell proliferation, and survival responses mouse embryonic fibroblasts (MEFs) derived from novel (DUSP-4) deletion mouse. show that serum PDGF induced ERK-dependent expression wild MEFs but not MKP-2(-/-) MEFs. stimulation sustained ERK phosphorylation was enhanced MEFs, whereas...
BACKGROUND AND PURPOSE We assessed the effects of over‐expressing dual‐specific phosphatase, mitogen‐activated protein (MAP) kinase phosphatase‐2 (MKP‐2), in human umbilical vein endothelial cells (HUVECs) on inflammatory expression and apoptosis, two key features dysfunction disease. EXPERIMENTAL APPROACHES infected HUVECs for 40 h with an adenoviral version MKP‐2 (Adv.MKP‐2). Tumour necrosis factor (TNF)‐α‐stimulated phosphorylation MAP was measured by Western blotting. Cellular apoptosis...
Barth syndrome is an X-linked mitochondrial disease, symptoms of which include neutropenia and cardiac myopathy. These are the most significant clinical consequences a increasingly recognised to have variable presentation. Mutation in Taz gene Xq28 thought be responsible for condition, by altering lipid content function. Male chimeras carrying targeted mutation on their X-chromosome were infertile. Testes from knockout smaller than control counterparts this was associated with disruption...
In this study we examined the potential for PAR(2) and TNFalpha to synergise at level of MAP kinase signalling in expressing NCTC2544 cells. However, our surprise found that activation by trypsin or specific activating peptide SLIGKV-OH strongly inhibited both phosphorylation activity JNK. contrast neither p38 nor ERK was affected although stimulated IkappaBalpha loss partially reversed. The inhibitory effect not observed parental cells PAR(4), however inhibition reversed pre-incubation with...