scholarly journals Selenoproteins Protect Against Avian Liver Necrosis by Metabolizing Peroxides and Regulating Receptor Interacting Serine Threonine Kinase 1/Receptor Interacting Serine Threonine Kinase 3/Mixed Lineage Kinase Domain-Like and Mitogen-Activated Protein Kinase Signaling

2021 ◽  
Vol 12 ◽  
Author(s):  
Tong Li ◽  
Jing Zhang ◽  
Peng-Jie Wang ◽  
Zi-Wei Zhang ◽  
Jia-Qiang Huang
Keyword(s):  
Protein Kinase ◽  
Basal Diet ◽  
Kinase Domain ◽  
Mitogen Activated Protein Kinase ◽  
Liver Necrosis ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Mitogen Activated Protein ◽  
Se Deficiency ◽  
Protein Kinase Signaling

Liver necroptosis of chicks is induced by selenium (Se)/vitamin E (VE) deficiencies and may be associated with oxidative cell damage. To reveal the underlying mechanisms of liver necrosis, a pool of the corn–soy basal diet (10 μg Se/kg; no VE added), a basal diet plus all-rac-α-tocopheryl acetate (50 mg/kg), Se (sodium selenite at 0.3 mg/kg), or both of these nutrients were provided to day-old broiler chicks (n = 40/group) for 6 weeks. High incidences of liver necrosis (30%) of chicks were induced by –SE–VE, starting at day 16. The Se concentration in liver and glutathione peroxidase (GPX) activity were decreased (P < 0.05) by dietary Se deficiency. Meanwhile, Se deficiency elevated malondialdehyde content and decreased superoxide dismutase (SOD) activity in the liver at weeks 2 and 4. Chicks fed with the two Se-deficient diets showed lower (P < 0.05) hepatic mRNA expression of Gpx1, Gpx3, Gpx4, Selenof, Selenoh, Selenok, Selenom, Selenon, Selenoo, Selenop, Selenot, Selenou, Selenow, and Dio1 than those fed with the two Se-supplemented diets. Dietary Se deficiency had elevated (P < 0.05) the expression of SELENOP, but decreased the downregulation (P < 0.05) of GPX1, GPX4, SELENON, and SELENOW in the liver of chicks at two time points. Meanwhile, dietary Se deficiency upregulated (P < 0.05) the abundance of hepatic proteins of p38 mitogen-activated protein kinase, phospho-p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, phospho-c-Jun N-terminal kinase, extracellular signal-regulated kinase, phospho-mitogen-activated protein kinase, receptor-interacting serine-threonine kinase 1 (RIPK1), receptor-interacting serine-threonine kinase 3 (RIPK3), and mixed lineage kinase domain-like (MLKL) at two time points. In conclusion, our data confirmed the differential regulation of dietary Se deficiency on several key selenoproteins, the RIPK1/RIPK3/MLKL, and mitogen-activated protein kinase signaling pathway in chicks and identified new molecular clues for understanding the etiology of nutritional liver necrosis.

scholarly journals Multiple Mitogen-Activated Protein Kinase Signaling Pathways Connect the Cot Oncoprotein to the c-junPromoter and to Cellular Transformation

2000 ◽  
Vol 20 (5) ◽  
pp. 1747-1758 ◽  
Author(s):  
Mario Chiariello ◽  
Maria Julia Marinissen ◽  
J. Silvio Gutkind
Keyword(s):  
Protein Kinase ◽  
Molecular Mechanisms ◽  
Cellular Transformation ◽  
Mitogen Activated Protein Kinase ◽  
Serine Threonine Kinase ◽  
Activated T Cells ◽  
Mapk Kinase ◽  
Threonine Kinase ◽  
Mitogen Activated Protein

ABSTRACT The serine/threonine kinase Cot is a member of the mitogen-activated protein kinase (MAPK) kinase kinase family implicated in cellular transformation. Enhanced expression of this protein has been shown to activate both the MAPK and the c-Jun N-terminal kinase (JNK) pathways and to stimulate the nuclear factor of activated T cells and NF-κB-dependent transcription. However, the nature of the normal functions of the Cot protein and the molecular mechanisms responsible for its oncogenic potential are still largely unknown. Here, we show that overexpression of the cot proto-oncogene is sufficient to stimulate the expression of c-jun and that, in turn, the activity of c-Jun is required for Cot-induced transformation. These observations prompted us to explore the molecular events by which Cot regulates c-jun expression. We found that Cot potently stimulates the activity of the c-jun promoter utilizing JNK-dependent and -independent pathways, the latter involving two novel members of the MAPK family, p38γ (ERK6) and ERK5. Molecularly, this activity was found to be dependent on the ability of Cot to activate, in vivo, members of each class of the MAPK kinase superfamily, including MEK, SEK, MKK6, and MEK5. Furthermore, the use of dominant interfering molecules revealed that Cot requires JNK, p38s, and ERK5 to stimulate the c-jun promoter fully and to induce neoplastic transformation. These findings indicate that Cot represents the first example of a serine/threonine kinase acting simultaneously on all known MAPK cascades. Moreover, these observations strongly suggest that the transforming ability of Cot results from the coordinated activation of these pathways, which ultimately converge on the regulation of the expression and activity of the product of the c-junproto-oncogene.

Mammalian Sterile20-like kinase 1 and the regulation of apoptosis

2004 ◽  
Vol 32 (3) ◽  
pp. 485-488 ◽  
Author(s):  
P.M. de Souza ◽  
M.A. Lindsay
Keyword(s):  
Protein Kinase ◽  
Physiological Function ◽  
Mitogen Activated Protein Kinase ◽  
Serine Threonine Kinase ◽  
Mapk Kinase ◽  
Threonine Kinase ◽  
Abundant Evidence ◽  
Mitogen Activated Protein ◽  
Kinase Pathway

Mammalian Sterile20-like kinase 1 (Mst1) is a ubiquitously expressed serine/threonine kinase which represents a member of the rapidly expanding family of enzymes related to the yeast Sterile20 kinase. Although the physiological function of Mst1 and its role in intracellular signalling is still unclear, reports to date suggest that Mst1, similar to its yeast homologue, operates in the MAPK (mitogen-activated protein kinase) pathway and, in this capacity, may represent a putative MAPK kinase kinase kinase. Moreover, there is abundant evidence for a role of this enzyme in apoptosis, where not only is it a target for caspases, but may also serve as an activator of these proteases to amplify the apoptotic signalling pathway. This paper reviews the investigations that have led to our current understanding of the mechanisms by which Mst1 may be activated and thereby contribute to apoptosis.

scholarly journals Expression and Characterization of the Mycobacterium tuberculosis Serine/Threonine Protein Kinase PknB

1999 ◽  
Vol 67 (11) ◽  
pp. 5676-5682 ◽  
Author(s):  
Yossef Av-Gay ◽  
Sarwat Jamil ◽  
Steven J. Drews
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Infection Model ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Mitogen Activated Protein

ABSTRACT PknB is a member of the newly discovered eukaryotic-like protein serine/threonine kinase (PSTK) family of proteins. The pknBgene was cloned and expressed in Escherichia coli. The active recombinant protein was purified and shown to be reactive with antiphosphoserine antibodies, as well as with antibodies to the phosphorylated eukaryotic Ser/Thr kinases mitogen-activated protein kinase kinase 3 and 6, P38, and Creb. In vitro kinase assays demonstrated that PknB is a functional kinase that is autophosphorylated on serine/threonine residues and is also able to phosphorylate the peptide substrate myelin basic protein. Analysis ofpknB expression in Mycobacterium tuberculosisindicates the presence of pknB mRNA in (i) organisms grown in vitro in bacteriological media, (ii) a murine macrophage in vitro infection model, and (iii) in vivo alveolar macrophages from a patient with tuberculosis.

scholarly journals Novel Functions of Death-Associated Protein Kinases through Mitogen-Activated Protein Kinase-Related Signals

2018 ◽  
Vol 19 (10) ◽  
pp. 3031 ◽  
Author(s):  
Mohamed Elbadawy ◽  
Tatsuya Usui ◽  
Hideyuki Yamawaki ◽  
Kazuaki Sasaki
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Family Members ◽  
Mitogen Activated Protein Kinase ◽  
Special Focus ◽  
Main Function ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Death Associated Protein Kinase ◽  
Mitogen Activated Protein

Death associated protein kinase (DAPK) is a calcium/calmodulin-regulated serine/threonine kinase; its main function is to regulate cell death. DAPK family proteins consist of DAPK1, DAPK2, DAPK3, DAPK-related apoptosis-inducing protein kinases (DRAK)-1 and DRAK-2. In this review, we discuss the roles and regulatory mechanisms of DAPK family members and their relevance to diseases. Furthermore, a special focus is given to several reports describing cross-talks between DAPKs and mitogen-activated protein kinases (MAPK) family members in various pathologies. We also discuss small molecule inhibitors of DAPKs and their potential as therapeutic targets against human diseases.

scholarly journals 3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region.

1996 ◽  
Vol 16 (3) ◽  
pp. 868-876 ◽  
Author(s):  
G Sithanandam ◽  
F Latif ◽  
F M Duh ◽  
R Bernal ◽  
U Smola ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Protein Kinase ◽  
Small Cell Lung Cancer ◽  
Suppressor Gene ◽  
Small Cell ◽  
Mitogen Activated Protein Kinase ◽  
Small Cell Lung ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Mitogen Activated Protein

NotI linking clones, localized to the human chromosome 3p21.3 region and homozygously deleted in small cell lung cancer cell lines NCI-H740 and NCI-H1450, were used to search for a putative tumor suppressor gene(s). One of these clones, NL1G210, detected a 2.5-kb mRNA in all examined human tissues, expression being especially high in the heart and skeletal muscle. Two overlapping cDNA clones containing the entire open reading frame were isolated from a human heart cDNA library and fully characterized. Computer analysis and a search of the GenBank database to reveal high sequence identity of the product of this gene to serine-threonine kinases, especially to mitogen-activated protein kinase-activated protein kinase 2, a recently described substrate of mitogen-activated kinases. Sequence identitiy was 72% at the nucleotide level and 75% at the amino acid level, strongly suggesting that this protein is a serine-threonine kinase. Here we demonstrate that the new gene, referred to as 3pK (for chromosome 3p kinase), in fact encodes a mitogen-activated protein kinase-regulated protein serine-threonine kinase with a novel substrate specificity.

scholarly journals Raf-1 is a potential substrate for mitogen-activated protein kinase in vivo

1991 ◽  
Vol 277 (2) ◽  
pp. 573-576 ◽  
Author(s):  
N G Anderson ◽  
P Li ◽  
L A Marsden ◽  
N Williams ◽  
T M Roberts ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Mitogen Activated Protein ◽  
Insulin Dependent ◽  
Potential Substrate

MAP (mitogen-activated protein) kinase is shown to phosphorylate baculovirally expressed Raf-1 in vitro, generating one major tryptic phosphopeptide which co-migrated with a peptide from Raf-1 32P-labelled in situ. This peptide also undergoes an insulin-dependent increase in labelling. Thus the serine/threonine kinase Raf-1 may be a substrate for MAP kinase in vivo.

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