scholarly journals cAMP activates calcium signalling via phospholipase C to regulate cellulase production in the filamentous fungus Trichoderma reesei

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Yumeng Chen ◽  
Xingjia Fan ◽  
Xinqing Zhao ◽  
Yaling Shen ◽  
Xiangyang Xu ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Phospholipase C ◽  
Trichoderma Reesei ◽  
Filamentous Fungus ◽  
Calcium Signalling ◽  
Signal Transduction Pathway ◽  
Cellulase Production ◽  
Signalling Pathway ◽  
Dependent Manner ◽  
Transduction Pathway

Abstract Background The filamentous fungus Trichoderma reesei is one of the best producers of cellulase and has been widely studied for the production of cellulosic ethanol and bio-based products. We previously reported that Mn2+ and N,N-dimethylformamide (DMF) can stimulate cellulase overexpression via Ca2+ bursts and calcium signalling in T. reesei under cellulase-inducing conditions. To further understand the regulatory networks involved in cellulase overexpression in T. reesei, we characterised the Mn2+/DMF-induced calcium signalling pathway involved in the stimulation of cellulase overexpression. Results We found that Mn2+/DMF stimulation significantly increased the intracellular levels of cAMP in an adenylate cyclase (ACY1)-dependent manner. Deletion of acy1 confirmed that cAMP is crucial for the Mn2+/DMF-stimulated cellulase overexpression in T. reesei. We further revealed that cAMP elevation induces a cytosolic Ca2+ burst, thereby initiating the Ca2+ signal transduction pathway in T. reesei, and that cAMP signalling causes the Ca2+ signalling pathway to regulate cellulase production in T. reesei. Furthermore, using a phospholipase C encoding gene plc-e deletion strain, we showed that the plc-e gene is vital for cellulase overexpression in response to stimulation by both Mn2+ and DMF, and that cAMP induces a Ca2+ burst through PLC-E. Conclusions The findings of this study reveal the presence of a signal transduction pathway in which Mn2+/DMF stimulation produces cAMP. Increase in the levels of cAMP activates the calcium signalling pathway via phospholipase C to regulate cellulase overexpression under cellulase-inducing conditions. These findings provide insights into the molecular mechanism of the cAMP–PLC–calcium signalling pathway underlying cellulase expression in T. reesei and highlight the potential applications of signal transduction in the regulation of gene expression in fungi.

scholarly journals Characterization of phosphoinositide-specific phospholipase C in rat colonocyte membranes

1993 ◽  
Vol 292 (1) ◽  
pp. 271-276 ◽  
Author(s):  
M J G Bolt ◽  
B M Bissonnette ◽  
R K Wali ◽  
S C Hartmann ◽  
T A Brasitus ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Monoclonal Antibodies ◽  
Phospholipase C ◽  
Plasma Membranes ◽  
Signal Transduction Pathway ◽  
Protein S ◽  
Transduction Pathway ◽  
Intestinal Physiology ◽  
Key Enzyme

The phosphoinositide signal transduction pathway mediates important processes in intestinal physiology, yet the key enzyme, phosphoinositide-specific phospholipase C (PI-PLC), is not well-characterized in the colon. PI-PLC activity was examined in rat colonic membranes using exogenous [3H]phosphatidylinositol 4,5-bisphosphate (PIP2) as substrate, and beta-glycerophosphate to suppress degradation of substrate or product. The activity of membrane PI-PLC increased 6-fold with the addition of alamethicin, and a further 2-3-fold enhancement was observed with 10 microM guanosine 5′-[gamma-thio]triphosphate (GTP[S]), suggesting the involvement of G-protein(s). The effect of GTP[S] appeared to be specific, as up to 100 microM adenosine 5′-[gamma-thio]-triphosphate failed to stimulate PI-PLC activity, and guanosine 5′-[beta-thio]diphosphate inhibited activity. The response of membrane PI-PLC to Ca2+ was biphasic, while > 0.5 mM Mg2+ was inhibitory with or without GTP[S]. Comparable total PI-PLC activities and responses to GTP[S] and Ca2+ were observed in purified brush-border and basolateral membranes. Western immunoblots probed with monoclonal antibodies to PLC isoenzymes PLC-beta 1, -gamma 1 and -delta 1 demonstrated that these antipodal plasma membranes contain predominantly the PLC-delta 1 isoform, with small amounts of PLC-gamma 1 present but no detectable PLC-beta 1. PLC-gamma 1 was the major isoform detected in cytosol.

scholarly journals PI3 kinase directly phosphorylates Akt1/2 at Ser473/474 in the insulin signal transduction pathway

2013 ◽  
Vol 220 (1) ◽  
pp. 49-59 ◽  
Author(s):  
A Tsuchiya ◽  
T Kanno ◽  
T Nishizaki
Keyword(s):  
Signal Transduction ◽  
Glucose Transporter ◽  
Signal Transduction Pathway ◽  
Significant Inhibition ◽  
Dependent Manner ◽  
Transduction Pathway ◽  
Glut4 Translocation ◽  
Insulin Signal Transduction ◽  
Insulin Signal ◽  
Insulin Signal Transduction Pathway

Insulin stimulated translocation of the glucose transporter GLUT4 from the cytosol to the plasma membrane in a concentration (1 nM–1 μM)-dependent manner and increased glucose uptake in 3T3-L1 adipocytes. Insulin-induced GLUT4 translocation to the cell surface was prevented by the phosphoinositide 3 kinase (PI3K) inhibitor wortmannin, the 3-phosphoinositide-dependent protein kinase 1 (PDK1) inhibitor BX912 or the Akt1/2 inhibitor MK2206, and by knocking-down PI3K, PDK1 or Akt1/2. Insulin increased phosphorylation of Akt1/2 at Thr308/309 and Ser473/474, to activate Akt1/2, in the adipocytes. Insulin-induced phosphorylation of Akt1/2 was suppressed by wortmannin and knocking-down PI3K, while no significant inhibition of the phosphorylation was obtained with BX912 or knocking-down PDK1. In the cell-free Akt assay, PI3K phosphorylated Akt1 both at Thr308 and Ser473 and Akt2 at Ser474 alone. In contrast, PDK1 phosphorylates Akt1 at Thr308 and Akt2 at Thr309. The results of this study indicate that PI3K activates Akt1, independently of PDK1, and Akt2 by cooperating with PDK1 in the insulin signal transduction pathway linked to GLUT4 translocation.

scholarly journals The overlooked background of gastric MMC III: the signalling pathways of motilin receptors inducing canine left gastric artery relaxation

2020 ◽  
Author(s):  
Hongyu Li ◽  
Lanlan Yang ◽  
Ying Jin ◽  
Chunxiang Jin
Keyword(s):  
Nitric Oxide ◽  
Signal Transduction ◽  
Endothelial Cells ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Left Gastric Artery ◽  
Phase Iii ◽  
Dependent Manner ◽  
Transduction Pathway ◽  
Gastric Artery

Abstract Background: In diabetic patients with gastroparesis, the gastric blood supply is often decreased and delayed gastric emptying associating MMCIII absence is the main symptom. Under physiological conditions, motilin has been shown to induce a sustained increase in left gastric artery (LGA) blood flow and initiate MMC phase III simultaneously. The study aimed to elucidating the signal transduction pathways of motilin receptors (MLNRs) in the relaxation of LGA.Methods: MLNR expression in the LGA was analysed by immunohistochemistry. Motilin-induced relaxation of the LGA was tested in a multi-wire myograph system. Effects of inhibitors or blockers in the signal transduction pathway were observed.Results: Immunohistochemical and immunofluorescence staining showed that the MLNRs were on the membranes of endothelial cells. Motilin relaxed U46619 pre-contracted canine LGA rings in a concentration-dependent manner, with an EC50 value of 9.010 ± 0.789 × 10−8 M. Motilin’s effect was inhibited by denuded endothelium but not by muscarinic receptor inhibitors. The effect was selectively and competitively inhibited by Phe-cyclo[Lys-Tyr(3-tBu)-Ala-]•trifluoroacetate (GM-109; MLNR antagonist) and completely or partially inhibited by inhibitors of the G protein–phospholipase C–inositol trisphosphate (G pr–PLC–IP3) and nitric oxide synthase–nitric oxide–soluble guanylyl cyclase (NOS–NO–sGC) signal transduction pathway, inhibitors of cyclooxygenase and myoendothelial gap junction, blockers of the potassium channel and low/free Ca2+ Krebs solutions, but not by inhibitors of protein kinase C, protein kinase A or L-type voltage-operated Ca2+ channel.Conclusions: MLNRs were on the membranes of endothelial cells of canine LGA. The main intracellular signal transduction pathway was motilin–MLNR–G pr–PLC–IP3–NOS–NO–sGC–cGMP. These results may provide a new theoretical basis for research on diabetic gastroparesis.

Interaction of spermine with a signal transduction pathway involving phospholipase C, during the growth of Catharanthus roseus transformed roots

2004 ◽  
Vol 120 (1) ◽  
pp. 140-151 ◽  
Author(s):  
Ileana Echevarria-Machado ◽  
Angela Ku-Gonzalez ◽  
Victor M. Loyola-Vargas ◽  
S. M. Teresa Hernandez-Sotomayor
Keyword(s):  
Signal Transduction ◽  
Phospholipase C ◽  
Catharanthus Roseus ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Transformed Roots

scholarly journals Calcium Signaling through Phospholipase C Activates Dendritic Cells To Mature and Is Necessary for the Activation and Maturation of Dendritic Cells Induced by Diverse Agonists

2004 ◽  
Vol 11 (1) ◽  
pp. 77-82 ◽  
Author(s):  
Kenneth C. Bagley ◽  
Sayed F. Abdelwahab ◽  
Robert G. Tuskan ◽  
George K. Lewis
Keyword(s):  
Signal Transduction ◽  
Dendritic Cells ◽  
Calcium Signaling ◽  
Phospholipase C ◽  
Cellular Proliferation ◽  
Signal Transduction Pathway ◽  
Calcium Ionophore ◽  
Prostaglandin E ◽  
Ionophore A23187 ◽  
Transduction Pathway

ABSTRACT Calcium is an important second messenger in the phospholipase C (PLC) signal transduction pathway. Calcium signaling is involved in many biological processes, including muscle contraction, cellular activation, and cellular proliferation. Dendritic cell (DC) maturation is induced by many different stimuli, including bacterial lipopolysaccharide (LPS), bacterial toxins, inflammatory cytokines, prostaglandins, as well as calcium mobilization. In the present study, we determined the role of the PLC signal transduction pathway in the activation and maturation of human monocyte-derived DCs (MDDCs) induced by diverse agonists. We found that signaling through PLC activates MDDCs to mature and is necessary for LPS, cholera toxin, dibutyryl-cyclic AMP, prostaglandin E2, and the calcium ionophore A23187 to induce MDDC maturation. The results of the present study along with the results of other studies indicate that multiple signaling pathways are involved in the activation of DCs and that inhibition of any of these pathways inhibits the maturation of DCs.

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