MAP Kinases: From Intracellular Signals to Physiology and Disease

Physiology ◽  
2002 ◽  
Vol 17 (2) ◽  
pp. 62-67 ◽  
Author(s):  
Herbert Schramek
Keyword(s):  
Cell Differentiation ◽  
Protein Kinases ◽  
Map Kinases ◽  
Reparative Regeneration ◽  
Mitogen Activated Protein Kinases ◽  
Differentiated Cells ◽  
Pathological Conditions ◽  
Intracellular Signals ◽  
Mitogen Activated Protein

Although differentiated cells will usually maintain their specialized character, conversion of cellular specificities can be observed during adaptation or reparative regeneration. In pathological conditions, such as inflammation and carcinogenesis, even highly specialized cells can alter their properties, leading to a deranged control of cell differentiation and/or proliferation. Mitogen-activated protein kinases are central regulators of these processes.

scholarly journals Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun.

1994 ◽  
Vol 14 (11) ◽  
pp. 7352-7362 ◽  
Author(s):  
E Cano ◽  
C A Hazzalin ◽  
L C Mahadevan
Keyword(s):  
Protein Kinases ◽  
Map Kinases ◽  
Early Gene ◽  
Intracellular Signals ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Serine Kinases ◽  
Translational Arrest ◽  
Epidermal Growth ◽  
Nuclear Responses

Independent of its ability to block translation, anisomycin intrinsically initiates intracellular signals and immediate-early gene induction [L. C. Mahadevan and D. R. Edwards, Nature (London) 349:747-749, 1991]. Here, we characterize further its action as a potent, selective signalling agonist. In-gel kinase assays show that epidermal growth factor (EGF) transiently activates five kinases: the mitogen-activated protein (MAP) kinases ERK-1 and -2, and three others, p45, p55, and p80. Anisomycin, at inhibitory and subinhibitory concentrations, does not activate ERK-1 and -2 but elicits strong sustained activation of p45 and p55, which are unique in being serine kinases whose detection is enhanced with poly-Glu/Tyr or poly-Glu/Phe copolymerized in these gels. Translational arrest using emetine or puromycin does not activate p45 and p55 but does prolong EGF-stimulated ERK-1 and -2 activation. Rapamycin, which blocks anisomycin-stimulated p70/85S6k activation without affecting nuclear responses, has no effect on p45 or p55 kinase. p45 and p55 are activable by okadaic acid or UV irradiation, and both kinases phosphorylate the c-Jun NH2-terminal peptide 1-79, putatively placing them within c-Jun NH2-terminal kinase/stress-activated protein kinase (JNK/SAPK) subfamily of MAP kinases. Thus, the EGF- and anisomycin-activated kinases p45 and p55 are strongly implicated in signalling to c-fos and c-jun, whereas the MAP kinases ERK-1 and -2 are not essential for this process.

Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun

1994 ◽  
Vol 14 (11) ◽  
pp. 7352-7362 ◽  
Author(s):  
E Cano ◽  
C A Hazzalin ◽  
L C Mahadevan
Keyword(s):  
Protein Kinases ◽  
Map Kinases ◽  
Early Gene ◽  
Intracellular Signals ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Serine Kinases ◽  
Translational Arrest ◽  
Epidermal Growth ◽  
Nuclear Responses

Independent of its ability to block translation, anisomycin intrinsically initiates intracellular signals and immediate-early gene induction [L. C. Mahadevan and D. R. Edwards, Nature (London) 349:747-749, 1991]. Here, we characterize further its action as a potent, selective signalling agonist. In-gel kinase assays show that epidermal growth factor (EGF) transiently activates five kinases: the mitogen-activated protein (MAP) kinases ERK-1 and -2, and three others, p45, p55, and p80. Anisomycin, at inhibitory and subinhibitory concentrations, does not activate ERK-1 and -2 but elicits strong sustained activation of p45 and p55, which are unique in being serine kinases whose detection is enhanced with poly-Glu/Tyr or poly-Glu/Phe copolymerized in these gels. Translational arrest using emetine or puromycin does not activate p45 and p55 but does prolong EGF-stimulated ERK-1 and -2 activation. Rapamycin, which blocks anisomycin-stimulated p70/85S6k activation without affecting nuclear responses, has no effect on p45 or p55 kinase. p45 and p55 are activable by okadaic acid or UV irradiation, and both kinases phosphorylate the c-Jun NH2-terminal peptide 1-79, putatively placing them within c-Jun NH2-terminal kinase/stress-activated protein kinase (JNK/SAPK) subfamily of MAP kinases. Thus, the EGF- and anisomycin-activated kinases p45 and p55 are strongly implicated in signalling to c-fos and c-jun, whereas the MAP kinases ERK-1 and -2 are not essential for this process.

scholarly journals High-fat diet increases O-GlcNAc levels in cerebral arteries: a link to vascular dysfunction associated with hyperlipidaemia/obesity?

2016 ◽  
Vol 130 (11) ◽  
pp. 871-880 ◽  
Author(s):  
Victor V. Lima ◽  
Fernanda R. Giachini ◽  
Takayuki Matsumoto ◽  
Weiguo Li ◽  
Alecsander F.M. Bressan ◽  
...  
Keyword(s):  
Protein Kinases ◽  
High Fat Diet ◽  
Vascular Dysfunction ◽  
Cerebral Arteries ◽  
Cerebral Vasculature ◽  
High Fat ◽  
Mitogen Activated Protein Kinases ◽  
Pathological Conditions ◽  
Mitogen Activated Protein

Increased O-GlcNAcylation (O-GlcNAc) in cerebral arteries, as a result of a high-fat diet (HFD), augments reactivity to constrictor stimuli as well as increases mitogen-activated protein kinases (MAPKs) activity. Increased O-GlcNAc levels may represent a new mechanism to cerebral vasculature dysfunction under pathological conditions.

scholarly journals Src Family Kinases and p38 Mitogen-Activated Protein Kinases Regulate Pluripotent Cell Differentiation in Culture

PLoS ONE ◽  
2016 ◽  
Vol 11 (10) ◽  
pp. e0163244 ◽  
Author(s):  
Boon Siang Nicholas Tan ◽  
Joly Kwek ◽  
Chong Kum Edwin Wong ◽  
Nicholas J. Saner ◽  
Charlotte Yap ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Protein Kinases ◽  
Src Family Kinases ◽  
Pluripotent Cell ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

scholarly journals Mitogen-activated protein kinases mediate changes in gene expression, but not cytoskeletal organization associated with cardiac muscle cell hypertrophy.

1994 ◽  
Vol 126 (6) ◽  
pp. 1565-1572 ◽  
Author(s):  
J Thorburn ◽  
J A Frost ◽  
A Thorburn
Keyword(s):  
Protein Kinases ◽  
Map Kinases ◽  
Individual Cell ◽  
Treatment Results ◽  
Mitogen Activated Protein Kinases ◽  
Cytoskeletal Organization ◽  
Hypertrophic Response ◽  
Ras Protein ◽  
Cellular Hypertrophy ◽  
Mitogen Activated Protein

Shortly after birth, cardiac myocytes lose the ability to divide, and, in adult animals, heart muscle grows by a process of cellular hypertrophy where each individual cell gets larger. We have previously shown that activated Ras protein can induce markers of the hypertrophic phenotype, including atrial natriuretic factor (ANF) expression and organization of contractile proteins, and that Ras is at least partially required for the hypertrophic effect of phenylephrine. In the present study, we examine the requirement for the mitogen-activated protein kinases (MAP kinases) in the hypertrophic response induced by phenylephrine. We find that phenylephrine treatment results in the activation of the MAP kinases and that this activity is required for transactivation of the fos, ANF, and MLH promoters. However, inhibition of MAP kinases does not prevent phenylephrine-induced organization of actin. These results suggest that the signal transduction pathways leading to different hypertrophic responses diverge upstream of the MAP kinases but possibly downstream of Ras.

scholarly journals New Insights into the p38γ and p38δ MAPK Pathways

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Ana Risco ◽  
Ana Cuenda
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Kinases ◽  
Expression Patterns ◽  
Cellular Functions ◽  
Mitogen Activated Protein Kinases ◽  
Pathological Conditions ◽  
Mitogen Activated Protein ◽  
Distinct Role ◽  
Made In

The mammalian p38 mitogen-activated protein kinases (MAPKs) family is composed of four members (p38α, p38β, p38γ, and p38δ), which are very similar in amino acid sequence but differ in their expression patterns. This suggests that they may have specific functions in different organs. In the last years most of the effort has been centred on the study of the function of the p38α isoform, which is widely referred to as p38 in the literature. However, the role that other p38 isoforms play in cellular functions and their implication in some of the pathological conditions have not been precisely defined so far. In this paper we highlight recent advances made in defining the functions of the two less studied alternative p38MAPKs, p38γ and p38δ. We describe that these p38MAPKs show similarities to the classical p38α isoform, although they may play central and distinct role in certain physiological and pathological processes.

scholarly journals MAP kinases nomenclature: Time for curation

2018 ◽  
Author(s):  
Khaled Moustafa
Keyword(s):  
Map Kinase ◽  
Protein Kinases ◽  
Map Kinases ◽  
Protein Families ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

The nomenclature of Mitogen Activated Protein Kinases (MAPKs) takes different formats composed of symbols, prefixes, suffixes, or descriptive acronyms of their functions that sometimes lead to confusion and make the indexed information redundant and inconsistent. To avoid such redundancy and reduce confusion, a curation of the terminology of MAP kinase families, and that of other protein families that present similar nomenclature issues, is required. Some arguable suggestions are presented here toward this goal.

325 ACTIVITY OF MATURATION-PROMOTING FACTOR (MPF) AND MITOGEN-ACTIVATED PROTEIN KINASES DURING IN VITRO MATURATION OF BUFFALO OOCYTES (BUBALUS BUBALIS)

2006 ◽  
Vol 18 (2) ◽  
pp. 270
Author(s):  
B. Gasparrini ◽  
G. Leoni ◽  
L. Boccia ◽  
M. Galiotto ◽  
S. Ledda ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinases ◽  
In Vitro Maturation ◽  
Map Kinases ◽  
Kinase Activity ◽  
Buffer System ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Maturation Promoting Factor

The maturation promoting factor (MPF) and mitogen-activated protein kinases (MAPK) are the key regulators of both meiotic and mitotic cell cycles. The absence of data on the activity of the major cell cycle kinases in buffalo oocytes during meiotic progression provided the bases for this study. More specifically we assayed the MPF and MAP kinase activity of buffalo oocytes during meiosis. Abattoir-derived cumulus-oocyte complexes (COCs) with a compact, non-atretic cumulus and a homogeneous cytoplasm were utilized for the study. The COCs (n = 293, over four replicates) were matured in vitro in TCM-199 supplemented with 10% fetal calf serum (FCS), 0.2 mM sodium pyruvate, 0.5 �g/mL FSH, 5 �g/mL LH, 1 �g/mL 17�-estradiol, 50 �M of cysteamine, and 50 �g/mL kanamycin (B199). In vitro maturation (IVM) was carried out at 38.5�C under a controlled gas atmosphere of 5% CO2 in humidified air. At scale times during the culture (0, 3, 6, 9, 12, 15, 18, 21, 24 h) groups of oocytes were stained with Hoechst 33342 to assess chromatin configuration and stored according to the maturation stage (GV, GVDB, MI, and MII) at -80�C pending protein analysis. SDS-polyacrylamide gel electrophoresis wase performed using Laemmli discontinuous buffer system (Laemmli 1970 Nature 227, 680) with a 12% running gel. Groups of oocytes were analyzed for MPF activity (n = 65) by histone H1 kinase activity (Naito and Toyoda 1991 J. Reprod. Fertil. 93, 467-473) and for MAPK activity (n = 48) by myelin basic protein assays (Chesnel et al. 1995 Biol. Reprod. 52, 895-902). The activity of both MPF and MAP kinases was quantified by measuring the density of the bands on the autoradiographic film with a densitometer. Differences in the levels of the kinases among groups were analyzed by ANOVA. It was assumed that the value of MPF and MAPK was 100% in metaphase II (MII) stage oocytes. The lowest levels of MPF and MAPK activities were found in the oocytes at the GV (0-6 h post-IVM: 40% and 17.2%, respectively) and at the GVBD (6-9 h post-IVM: 41.2% and 18%) stages. The activities increased at metaphase I (MI) stage (9-15 h post-IVM) and at MII (21-24 post-IVM). Interestingly, although similar levels of MAP kinases were found at MI and MII stages (95.1% vs. 100%), MPF levels were significantly lower (P < 0.01) at the MI stage compared to those detected at MII (82.8% vs. 100%). The fluctuations of the MPF levels in buffalo appear different compared to those observed in other species; in particular, no differences were recorded between the GV and the GVBD stages whereas a significant increase of the MPF levels was found at MII compared to the MI stage. It seems that MPF and MAPK could differently guide meiotic resumption and progression to the MII arrest in this species. To our knowledge, this is the first report on biochemical analysis of the cell cycle regulation in buffalo oocytes.

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