scholarly journals Biochemical basis of defense response in plant against Fusarium wilt through bio-agents as an inducers

2012 ◽  
Vol 7 (43) ◽  
pp. 5849-5857 ◽  
Author(s):  
Rajik Mohd ◽  
K Biswas S ◽  
Shakti Shiv
Keyword(s):  
Fusarium Wilt ◽  
Defense Response ◽  
Biochemical Basis

scholarly journals Biochemical basis of improvement of defense in tomato plant against Fusarium wilt by CaCl2

2017 ◽  
Vol 23 (3) ◽  
pp. 581-596 ◽  
Author(s):  
Nilanjan Chakraborty ◽  
Swarnendu Chandra ◽  
Krishnendu Acharya
Keyword(s):  
Fusarium Wilt ◽  
Tomato Plant ◽  
Biochemical Basis

scholarly journals Microbial and biochemical basis of a Fusarium wilt-suppressive soil

2015 ◽  
Vol 10 (1) ◽  
pp. 119-129 ◽  
Author(s):  
Jae-Yul Cha ◽  
Sangjo Han ◽  
Hee-Jeon Hong ◽  
Hyunji Cho ◽  
Daran Kim ◽  
...  
Keyword(s):  
Fusarium Wilt ◽  
Biochemical Basis ◽  
Suppressive Soil

scholarly journals A Methyl Esterase 1 (PvMES1) Promotes the Salicylic Acid Pathway and Enhances Fusarium Wilt Resistance in Common Beans

2021 ◽  
Author(s):  
Renfeng Xue ◽  
Ming Feng ◽  
Jian Chen ◽  
Weide Ge ◽  
Matthew W. Blair
Keyword(s):  
Salicylic Acid ◽  
Common Bean ◽  
Signaling Pathway ◽  
Fusarium Wilt ◽  
Defense Response ◽  
Sugar Metabolism ◽  
Common Beans ◽  
Wilt Resistance ◽  
Practical Applications ◽  
Fusarium Wilt Resistance

Abstract Common bean (Phaseolus vulgaris L.) is an important food legume. Fusarium wilt caused by Fusarium oxysporum f. sp. phaseoli is one of the most serious soil-born diseases of common bean found throughout the world and affects the yield and quality of the crop. Few sources of Fusarium wilt resistance exist in legumes and most are of quantitative inheritance. In this study, we have identified a methyl salicylate esterase (MES), PvMES1, that contributes to plant defense response by regulating the salicylic acid (SA) mediated signaling pathway in response to Fusarium wilt in common beans. The result showed the role of PvMES1 in regulating SA levels in common bean and thus the SA signaling pathway and defense response mechanism in the plant. Overexpression of the PvMES1 gene enhanced Fusarium wilt resistance; while silencing of the gene caused susceptibility to the diseases. RNA-seq analysis with these transiently modified plants showed that genes related to SA level changes included the following gene ontologies: a) interaction between host and pathogen; b) phenylpropanoid synthesis; and c) sugar metabolism as well as others. These key signal elements activated the defense response pathway in common bean to Fusarium wilt. Collectively, our findings indicate that PvMES1 plays a pivotal role in regulating SA biosynthesis and signaling, and increasing Fusarium wilt resistance in common bean, thus providing novel insight into the practical applications of both SA and MES genes and pathways they contribiute to for developing elite crop varieties with enhanced broad-spectrum resistance to this critical disease.

Autonomic mechanisms underlying the cardiac defense response in humans

1996 ◽  
Author(s):  
Jaime Vila ◽  
M. Carmen Fernandez ◽  
M. Nieves Perez ◽  
Gustavo Reyes
Keyword(s):  
Defense Response

Enhancement of Plasminogen Binding to U937 Cells and Fibrin by Complestatin

1997 ◽  
Vol 77 (01) ◽  
pp. 137-142 ◽  
Author(s):  
Kiyoshi Tachikawa ◽  
Keiji Hasurni ◽  
Akira Endo
Keyword(s):  
Binding Site ◽  
Binding Affinity ◽  
Blood Cells ◽  
Aminocaproic Acid ◽  
U937 Cells ◽  
Biochemical Basis ◽  
Equilibrium Binding ◽  
Pharmacological Stimulation ◽  
Endogenous Fibrinolysis ◽  
Stimulation Of

SummaryPlasminogen binds to endothelial and blood cells as well as to fibrin, where the zymogen is efficiently activated and protected from inhibition by α2-antiplasmin. In the present study we have found that complestatin, a peptide-like metabolite of a streptomyces, enhances binding of plasminogen to cells and fibrin. Complestatin, at concentrations ranging from 1 to 5 μM, doubled 125I-plasminogen binding to U937 cells both in the absence and presence of lipoprotein(a), a putative physiological competitor of plasminogen. The binding of 125I-plasminogen in the presence of complestatin was abolished by e-aminocaproic acid, suggesting that the lysine binding site(s) of the plasminogen molecule are involved in the binding. Equilibrium binding analyses indicated that complestatin increased the maximum binding of 125I-plasminogen to U937 cells without affecting the binding affinity. Complestatin was also effective in increasing 125I-plasminogen binding to fibrin, causing 2-fold elevation of the binding at ~1 μM. Along with the potentiation of plasminogen binding, complestatin enhanced plasmin formation, and thereby increased fibrinolysis. These results would provide a biochemical basis for a pharmacological stimulation of endogenous fibrinolysis through a promotion of plasminogen binding to cells and fibrin.

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