Corticosterone‐induced rapid phosphorylation of p38 and JNK mitogen‐activated protein kinases in PC12 cells [PDF]
The present study showed that corticosterone (B) could induce a rapid activation of p38 and c‐Jun NH2‐terminal protein kinase (JNK) in PC12 cells. The dose–response and time–response curves were bell‐shaped with maximal activation at 10−9 M and at 15 min. RU38486 had no effect, and bovine serum albumin‐coupled B could induce the activation.
Xiaoyu Li+5 more
semanticscholar +6 more sources
Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium [PDF]
Cadmium (Cd), a human carcinogen, can induce apoptosis in various cell types. Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis.
Show‐Mei Chuang+2 more
semanticscholar +5 more sources
Stress-responsive JNK mitogen-activated protein kinase mediates aspirin-induced suppression of B16 melanoma cellular proliferation [PDF]
Available anticancer drugs do not seem to modify the prognosis of metastatic melanoma. Salicylate and acetyl salicylic acid (aspirin) were found to suppress growth in a number of transformed cells, that is, prostate and colon. Therefore, we studied the direct effects of aspirin on metastatic B16 melanoma cells.
Orly Ordan+3 more
semanticscholar +8 more sources
Raf-independent Deregulation of p38 and JNK Mitogen-activated Protein Kinases Are Critical for Ras Transformation [PDF]
Activated Ras, but not Raf, causes transformation of RIE-1 epithelial cells, supporting the importance of Raf-independent pathways in mediating Ras transformation. The p38 and JNK mitogen-activated protein kinase cascades are activated by Ras via Raf-independent effector function.
Kevin Pruitt+4 more
semanticscholar +8 more sources
Interacting JNK-docking Sites in MKK7 Promote Binding and Activation of JNK Mitogen-activated Protein Kinases [PDF]
D-sites are a class of MAPK-docking sites that have been found in many MAPK regulators and substrates. A single functional, high affinity D-site has been identified near the N terminus of each of the MAPK kinases (MKKs or MEKs) MEK1, MEK2, MKK3, MKK4, and MKK6.
David Ho+4 more
semanticscholar +6 more sources
c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases. [PDF]
c-Jun transcriptional activity is stimulated by phosphorylation at two N-terminal sites: Ser-63 and -73. Phosphorylation of these sites is enhanced in response to a variety of extracellular stimuli, including growth factors, cytokines, and UV irradiation.
Audrey Minden+6 more
semanticscholar +4 more sources
Role of p38 and JNK Mitogen-Activated Protein Kinases in the Activation of Ternary Complex Factors [PDF]
The transcription factors Elk-1 and SAP-1 bind together with serum response factor to the serum response element present in the c-fos promoter and mediate increased gene expression. The ERK, JNK, and p38 groups of mitogen-activated protein (MAP) kinases phosphorylate and activate Elk-1 in response to a variety of extracellular stimuli. In contrast, SAP-
Whitmarsh, Alan J.+4 more
openaire +6 more sources
Octacalcium phosphate crystals directly stimulate expression of inducible nitric oxide synthase through p38 and JNK mitogen-activated protein kinases in articular chondrocytes. [PDF]
Basic calcium phosphate (BCP) crystals, including hydroxyapatite, octacalcium phosphate (OCP) and carbonate-apatite, have been associated with severe osteoarthritis and several degenerative arthropathies.
Hang‐Korng Ea+3 more
semanticscholar +4 more sources
Activation of Mitogen-Activated Protein Kinases (ERK/JNK) and AP-1 Transcription Factor in Rat Carotid Arteries After Balloon Injury [PDF]
Smooth muscle cell proliferation is a key event in neointimal formation after balloon angioplasty. The molecular signals that mediate this process have yet to be identified.
Yanhua Hu+3 more
openalex +2 more sources
Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver [PDF]
The stress-activated protein kinases JNK and p38 mediate increased gene expression and are activated by environmental stresses and proinflammatory cytokines. Using an in vivo model in which oxidative stress is generated in the liver by intracellular metabolism, rapid protein–DNA complex formation on stress ...
Paulson Ke+4 more
openaire +4 more sources