caa a22 4500 477100325 CHVBK 20180405111539.0 cr unu---uuuuu 170330e19961001xx s 000 0 eng 10.1007/BF00208314 doi (NATIONALLICENCE)springer-10.1007/BF00208314 The elicitor-induced oxidative burst in cultured chickpea cells drives the rapid insolubilization of two cell wall structural proteins [Elektronische Daten] [Oliver Otte, Wolfgang Barz] Elicitation of cultured chickpea cells caused rapid insolubilization of two cell wall structural proteins, p190, a putative hydroxyproline-rich glycoprotein and p80, a putative proline-rich protein. This process appeared to result from an H2O2-mediated oxidative cross-linking mechanism and was initiated within 5 min and complete within 20 min. Further, elicitation of cells induced a rapid, transient generation of H2O2 (oxidative burst), with an onset after 5 min and a maximum H2O2-release after 20 min, as measured by a luminol-dependent chemiluminescence assay. Both chemiluminescence and protein insolubilization were suppressed by exogenous application of catalase or diphenylene iodonium, an inhibitor of plasma-membrane NADPH oxidase, respectively. In contrast, exogenous H2O2 mimicked the effect of the elicitor, suggesting that the putative oxidative crosslinking of the proteins depends directly on H2O2 from the oxidative burst. The peroxidase inhibitor salicylhydroxamic acid blocked both the elicitor- and the exogenous-H2O2-stimulated insolubilization, indicating that a peroxidase activity downstream of H2O2-supply is required. The protein kinase inhibitor staurosporine blocked the elicitation of the oxidative burst and protein insolubilization. In contrast, the protein phosphatase 2A inhibitor cantharidin accelerated, potentiated and extended the elicited oxidative burst. Cantharidin even stimulated the responses in the absence of the elicitor. The competitive effect of both inhibitors confirms that a coordinated activation of (i) protein kinase(s) and (ii) counteracting protein phosphates(s) is a poised signal transduction step for the induction of an NADPH-oxidase-dependent oxidative burst, which drives the putative peroxidase-catalyzed cross-linking of the cell wall proteins. Springer-Verlag, 1996 Cell wall nationallicence Hydrogen peroxide nationallicence Hydroxypro-line-rich glycoprotein nationallicence Oxidative burst nationallicence Proline-rich protein nationallicence Protein phosphorylation nationallicence DPI : diphenylene iodonium nationallicence Ext-1 : extensin-1 nationallicence gE1 : anti-glycosylated extensin-1 antibodies nationallicence HRGP : hydroxyp-roline-rich glycoprotein nationallicence LDC : luminol-dependent chemiluminescence nationallicence POD : peroxidase nationallicence PA : polyacrylamide nationallicence PRP : proline-rich proteins nationallicence SHAM : salicylhydroxamic acid nationallicence Otte Oliver Institut für Biochemie und Biotechnologie der Pflanzen, Hindenburgplatz 55, D-48143, Münster, Germany aut Barz Wolfgang Institut für Biochemie und Biotechnologie der Pflanzen, Hindenburgplatz 55, D-48143, Münster, Germany aut Planta Springer-Verlag 200/2(1996-10-01), 238-246 0032-0935 200:2<238 1996 200 425 https://doi.org/10.1007/BF00208314 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00208314 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Otte Oliver Institut für Biochemie und Biotechnologie der Pflanzen, Hindenburgplatz 55, D-48143, Münster, Germany aut NATIONALLICENCE 700 1- Barz Wolfgang Institut für Biochemie und Biotechnologie der Pflanzen, Hindenburgplatz 55, D-48143, Münster, Germany aut NATIONALLICENCE 773 0- Planta Springer-Verlag 200/2(1996-10-01), 238-246 0032-0935 200:2<238 1996 200 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer