scholarly journals Myosin Phosphatase Is Implicated in the Control of THP-1 Monocyte to Macrophage Differentiation

2021 ◽  
Vol 22 (5) ◽  
pp. 2516
Author(s):  
Emese Tóth ◽  
Ferenc Erdődi ◽  
Andrea Kiss
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Myosin Light Chain ◽  
Signal Transduction Pathways ◽  
Myosin Phosphatase ◽  
Pharmacological Interventions ◽  
Rock Inhibitor ◽  
Macrophage Differentiation ◽  
Disease States ◽  
The Impact

Monocyte to macrophage differentiation is characterized by the activation of various signal transduction pathways, which may be modulated by protein phosphorylation; however, the impact of protein kinases and phosphatases is not well understood yet. It has been demonstrated that actomyosin rearrangement during macrophage differentiation is dependent on Rho-associated protein kinase (ROCK). Myosin phosphatase (MP) target subunit-1 (MYPT1) is one of the major cellular substrates of ROCK, and MP is often a counter enzyme of ROCK; therefore, MP may also control macrophage differentiation. Changes in MP activity and the effects of MP activation were studied on PMA or l,25(OH)2D3-induced differentiation of monocytic THP-1 cells. During macrophage differentiation, phosphorylation of MYPT1 at Thr696 and Thr853 increased significantly, resulting in inhibition of MP. The ROCK inhibitor H1152 and the MP activator epigallocatechin-3-gallate (EGCG) attenuated MYPT1 phosphorylation and concomitantly decreased the extent of phosphorylation of 20 kDa myosin light chain. H1152 and EGCG pretreatment also suppressed the expression of CD11b and weakened the PMA-induced adherence of the cells. Our results indicate that MP activation/inhibition contributes to the efficacy of monocyte to macrophage differentiation, and this enzyme may be a target for pharmacological interventions in the control of disease states that are affected by excessive macrophage differentiation.

Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation

2001 ◽  
Vol 81 (2) ◽  
pp. 807-869 ◽  
Author(s):  
John M. Kyriakis ◽  
Joseph Avruch
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Treatment Strategies ◽  
Nuclear Factor Κb ◽  
Mitogen Activated Protein Kinase ◽  
Signal Transduction Pathways ◽  
Mitogen Activated Protein ◽  
Novel Treatment Strategies ◽  
Care Problems ◽  
The Impact

The molecular details of mammalian stress-activated signal transduction pathways have only begun to be dissected. This, despite the fact that the impact of these pathways on the pathology of chronic inflammation, heart disease, stroke, the debilitating effects of diabetes mellitus, and the side effects of cancer therapy, not to mention embryonic development, innate and acquired immunity, is profound. Cardiovascular disease and diabetes alone represent the most significant health care problems in the developed world. Thus it is not surprising that understanding these pathways has attracted wide interest, and in the past 10 years, dramatic progress has been made. Accordingly, it is now becoming possible to envisage the transition of these findings to the development of novel treatment strategies. This review focuses on the biochemical components and regulation of mammalian stress-regulated mitogen-activated protein kinase (MAPK) pathways. The nuclear factor-κB pathway, a second stress signaling paradigm, has been the subject of several excellent recent reviews (258, 260).

scholarly journals Distinct Nongenomic Signal Transduction Pathways Controlled by 17β-Estradiol Regulate DNA Synthesis and Cyclin D1 Gene Transcription in HepG2 Cells

2002 ◽  
Vol 13 (10) ◽  
pp. 3720-3729 ◽  
Author(s):  
Maria Marino ◽  
Filippo Acconcia ◽  
Francesco Bresciani ◽  
Alessandro Weisz ◽  
Anna Trentalance
Keyword(s):  
Gene Expression ◽  
Signal Transduction ◽  
Estrogen Receptor ◽  
Protein Kinase ◽  
Dna Synthesis ◽  
Gene Transcription ◽  
Hepg2 Cells ◽  
Signal Transduction Pathways ◽  
Cyclin D ◽  
17Β Estradiol

Estrogens induce cell proliferation in target tissues by stimulating progression through the G1 phase of the cell cycle. Activation of cyclin D1 gene expression is a critical feature of this hormonal action. The existence of rapid/nongenomic estradiol-regulated protein kinase C (PKC-α) and extracellular signal-regulated kinase (ERK) signal transduction pathways, their cross talk, and role played in DNA synthesis and cyclin D1 gene transcription have been studied herein in human hepatoma HepG2 cells. 17β-Estradiol was found to rapidly activate PKC-α translocation and ERK-2/mitogen-activated protein kinase phosphorylation in this cell line. These actions were independent of each other, preceding the increase of thymidine incorporation into DNA and cyclin D1expression, and did not involve DNA binding by estrogen receptor. The results obtained with specific inhibitors indicated that PKC-α pathway is necessary to mediate the estradiol-induced G1-S progression of HepG2 cells, but it does not exert any effect(s) on cyclin D1 gene expression. On the contrary, ERK-2 cascade was strongly involved in both G1-S progression and cyclin D1gene transcription. Deletion of its activating protein-1 responsive element motif resulted in attenuation of cyclin D1 promoter responsiveness to estrogen. These results indicate that estrogen-induced cyclin D1 transcription can occur in HepG2 cells independently of the transcriptional activity of estrogen receptor, sustaining the pivotal role played by nongenomic pathways of estrogen action in hormone-induced proliferation.

scholarly journals Protein Kinase A and Mitogen-Activated Protein Kinase Pathways Antagonistically Regulate Fission Yeast fbp1Transcription by Employing Different Modes of Action at Two Upstream Activation Sites

2000 ◽  
Vol 20 (17) ◽  
pp. 6426-6434 ◽  
Author(s):  
Lori A. Neely ◽  
Charles S. Hoffman
Keyword(s):  
Signal Transduction ◽  
Transcriptional Regulation ◽  
Protein Kinase ◽  
Mapk Pathway ◽  
Transcriptional Start Site ◽  
Mitogen Activated Protein Kinase ◽  
Signal Transduction Pathways ◽  
Start Site ◽  
Mitogen Activated Protein ◽  
Kinase A

ABSTRACT A significant challenge to our understanding of eukaryotic transcriptional regulation is to determine how multiple signal transduction pathways converge on a single promoter to regulate transcription in divergent fashions. To study this, we have investigated the transcriptional regulation of theSchizosaccharomyces pombe fbp1 gene that is repressed by a cyclic AMP (cAMP)-dependent protein kinase A (PKA) pathway and is activated by a stress-activated mitogen-activated protein kinase (MAPK) pathway. In this study, we identified and characterized twocis-acting elements in the fbp1 promoter required for activation of fbp1 transcription. Upstream activation site 1 (UAS1), located approximately 900 bp from the transcriptional start site, resembles a cAMP response element (CRE) that is the binding site for the atf1-pcr1 heterodimeric transcriptional activator. Binding of this activator to UAS1 is positively regulated by the MAPK pathway and negatively regulated by PKA. UAS2, located approximately 250 bp from the transcriptional start site, resembles a Saccharomyces cerevisiae stress response element. UAS2 is bound by transcriptional activators and repressors regulated by both the PKA and MAPK pathways, although atf1 itself is not present in these complexes. Transcriptional regulation offbp1 promoter constructs containing only UAS1 or UAS2 confirms that the PKA and MAPK regulation is targeted to both sites. We conclude that the PKA and MAPK signal transduction pathways regulatefbp1 transcription at UAS1 and UAS2, but that the antagonistic interactions between these pathways involve different mechanisms at each site.

Two Interacting Signal Transduction Pathways Regulate Collecting Duct Water Transport

Physiology ◽  
1988 ◽  
Vol 3 (6) ◽  
pp. 235-241 ◽  
Author(s):  
Y Ando ◽  
HR Jacobson ◽  
MD Breyer
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Cell Function ◽  
Collecting Duct ◽  
Signal Transduction Pathways ◽  
Phosphatidylinositol Bisphosphate ◽  
Kinase C ◽  
Arachidonate Metabolites

Receptor-mediated signal transduction occurs through phosphatidylinositol bisphosphate (PIP2) breakdown and activation of adenylate cyclase interacting to regulate cell function. Current studies suggest that hormone-stimulated PIP2 breakdown modulates the classic cyclic AMP-mediated hydrosmotic action of vasopressin through separate mechanisms attributable to activation of protein kinase C, elevation of intracellular Ca2+ concentration, and generation of arachidonate metabolites.

scholarly journals Protein Kinase G Induces an Immune Response in Cows Exposed toMycobacterium aviumSubsp.paratuberculosis

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Horacio Bach ◽  
Melissa Richard-Greenblatt ◽  
Eviatar Bach ◽  
Marcelo Chaffer ◽  
Wanika Lai ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Immune Response ◽  
Protein Kinase ◽  
Virulence Factors ◽  
Interferon Gamma ◽  
Host Cells ◽  
Protein Kinase G ◽  
Signal Transduction Pathways ◽  
Mycobacterial Species ◽  
Stimulation Of

To establish infection, pathogens secrete virulence factors, such as protein kinases and phosphatases, to modulate the signal transduction pathways used by host cells to initiate immune response. The protein MAP3893c is annotated in the genome sequence ofMycobacterium aviumsubspeciesparatuberculosis(MAP), the causative agent of Johne’s disease, as the serine/threonine protein kinase G (PknG). In this work, we report that PknG is a functional kinase that is secreted within macrophages at early stages of infection. The antigen is able to induce an immune response from cattle exposed to MAP in the form of interferon gamma production after stimulation of whole blood with PknG. These findings suggest that PknG may contribute to the pathogenesis of MAP by phosphorylating macrophage signalling and/or adaptor molecules as observed with other pathogenic mycobacterial species.

EXTRAOCULAR CELLULAR PHOTOTRANSDUCTION

2009 ◽  
Vol 02 (01) ◽  
pp. 93-100 ◽  
Author(s):  
LING ZHU ◽  
TIMON CHENG-YI LIU ◽  
MIN WU ◽  
JIAN-QIN YUAN ◽  
TONG-SHENG CHEN
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Monochromatic Light ◽  
Mitogen Activated Protein Kinase ◽  
Signal Transduction Pathways ◽  
Mitogen Activated Protein ◽  
Cellular Signal ◽  
Gs Protein ◽  
Almost All ◽  
Relationship Of

Photobiomodulation (PBM) is a modulation of monochromatic light or laser irradiation (LI) on biosystems. It is reviewed from the viewpoint of extraocular phototransduction in this paper. It was found that LI can induce extraocular phototransduction, and there may be an exact correspondence relationship of LI at different wavelengths and in different dose zones, and cellular signal transduction pathways. The signal transduction pathways can be classified into two types so that the Gs protein-mediated pathways belong to pathway 1, and the other pathways such as protein kinase Cs -mediated pathways and mitogen-activated protein kinase-mediated pathways belong to pathway 2. Almost all the present pathways found to mediate PBM belong to pathway 2, but there should be a pathway 1-mediated PBM. The previous studies were rather preliminary, and therefore further work should be done.

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