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  • It is known that changes in cGMP levels are

    2022-08-09

    It is known that changes in cGMP levels are positively correlated with plant adaptation to environmental stresses. It seems that a novel group of moonlighting kinases with GC activity is particularly involved in response to biotic stress. It was shown that danger-associated molecular pattern (DAMPs) molecules after binding with PepR1 receptor in Arabidopsis thaliana activate pathogen-defense signaling cascades including stimulation of guanylyl cyclase activity of AtPepR1 and cGMP biosynthesis (Qi et al., 2010). The existence of mechanism linking the pathogen perception on the cell surface and stimulation of intracellular cGMP and Ca2+ signaling in immune responses in plants was also observed (Ma et al., 2009 and Ryan et al., 2007). Furthermore, trancriptional analysis showed that AtWAKL10 gene is consistently co-expressed together with a group of pathogen defense related genes and it is induced as one of the first steps in response to a broad range of pathogens (biotrophic – P. syringae, P. infestans, E. cichoracearum, G. orontii and necrotrophic – B. cinerea) (Meier et al., 2010). Consequently, we made an effort to identify and characterize HpPepR1 gene and investigate the involvement of HpPepR1 in Hippestrum hybridum response to wounding and fungal infection. Here we demonstrate that recombinant HpPepR1 protein has 14 amino naloxone hcl long catalytic motif and it is able to catalyze in vitro cGMP biosynthesis, what proves that HpPepR1 acts as an active guanylyl cyclase. Transcriptional activity analysis suggest that HpPepR1 may be involved in early biotic stress responses in Hippeastrum hybridum bulbs making the gene one of the potential candidate elements responsible for pathogen-induced cGMP production.
    Material and methods
    Results and discussion
    Acknowledgements The authors thank PhD Anna Wojciechowska for help in statistical analysis. This project was supported by the National Science Centre, grant no. NN310 301839 and funds provided by Nicolaus Copernicus University (Toruń, Poland) for the research program of the Chair of Plant Physiology and Biotechnology.
    Introduction C-type natriuretic peptide (CNP) is a hormone that shares structural similarities to the cardiac hormones, atrial natriuretic peptide (ANP) and b-type natriuretic peptide (BNP) [1]. CNP is abundantly expressed in the endothelium [2,3] and kidneys [[4], [5], [6]] as well as the heart [[7], [8], [9]], but to lesser extent than ANP and BNP. CNP selectively binds with high affinity to the particulate guanylyl cyclase B (pGC-B) receptor and has fairly low affinity for the particulate guanylyl cyclase A (pGC-A) receptor [10,11]. Through the generation of its second messenger cGMP, CNP mediates potent anti-fibrotic actions [[12], [13], [14], [15]], while lacking comparable renal enhancing or blood pressure (BP) lowering properties compared to ANP or BNP. Despite these beneficial anti-fibrotic actions, CNP's therapeutic potential is limited because of its short circulating half-life [16] predominantly due to rapid degradation by neprilysin (NEP) [[17], [18], [19]] as well as high affinity for the clearance receptor, NPRC [20,21]. Currently, there is no selective pGC-B activator approved for clinical use. Given the anti-fibrotic actions assigned to pGC-B activation in models of organ fibrosis including cardiac and renal fibrosis [12,13,22], the engineering of a selective pGC-B activator with a longer half-life may represent a breakthrough in drug discovery and therapeutics. Indeed, elegant studies by Pankow et al., have demonstrated that NPs with longer amino- and/or carboxyl- terminal amino acid (AA) extensions are resistant to NEP degradation [18], which in turn may contribute to enhanced biological actions. Studies have established that CNP is produced as a prohormone that is cleaved intracellularly by the enzyme, furin, to yield a 53-AA intermediate form (C53) [23]. C53 is subsequently cleaved by an unknown enzyme to generate the 22-AA biologically active form CNP [1,24,25]. However, the biological and cGMP generation actions of C53 are undefined and may represent a therapeutic opportunity targeting pGC-B/cGMP pathway and multiorgan fibrosis.