title: Plant natriuretic peptides are apoplastic and paracrine stress response molecules.
abstract: Higher plants contain biologically active proteins that are recognized by antibodies against human atrial natriuretic peptide (ANP). We identified and isolated two Arabidopsis thaliana immunoreactive plant natriuretic peptide (PNP)-encoding genes, AtPNP-A and AtPNP-B, which are distantly related members of the expansin superfamily and have a role in the regulation of homeostasis in abiotic and biotic stresses, and have shown that AtPNP-A modulates the effects of ABA on stomata. Arabidopsis PNP (PNP-A) is mainly expressed in leaf mesophyll cells, and in protoplast assays we demonstrate that it is secreted using AtPNP-A:green fluorescent protein (GFP) reporter constructs and flow cytometry. Transient reporter assays provide evidence that AtPNP-A expression is enhanced by heat, osmotica and salt, and that AtPNP-A itself can enhance its own expression, thereby generating a response signature diagnostic for paracrine action and potentially also autocrine effects. Expression of native AtPNP-A is enhanced by osmotica and transiently by salt. Although AtPNP-A expression is induced by salt and osmotica, ABA does not significantly modulate AtPNP-A levels nor does recombinant AtPNP-A affect reporter expression of the ABA-responsive RD29A gene. Together, these results provide experimental evidence that AtPNP-A is stress responsive, secreted into the apoplastic space and can enhance its own expression. Furthermore, our findings support the idea that AtPNP-A, together with ABA, is an important component in complex plant stress responses and that, much like in animals, peptide signaling molecules can create diverse and modular signals essential for growth, development and defense under rapidly changing environmental conditions.
authors.affiliation: Monash Institute of Pharmaceutical Sciences, Monash University 381 Royal Parade, Parkville, Vic 3052, Australia.
authors.forename: Yu Hua
authors.initials: YH
authors.lastname: Wang
authors.forename: Chris
authors.initials: C
authors.lastname: Gehring
authors.forename: Helen R
authors.initials: HR
authors.lastname: Irving
mesh_terms: D000040:Abscisic Acid / Q000494:pharmacology; D017360:Arabidopsis / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D006152:Cyclic GMP / Q000494:pharmacology; D005434:Flow Cytometry; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D005966:Glucuronidase / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000378:metabolism; D008954:Models, Biological; D045265:Natriuretic Peptides / Q000378:metabolism*; D019899:Paracrine Communication / Q000187:drug effects; D019441:Plant Epidermis / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D018515:Plant Leaves / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D030821:Plants, Genetically Modified; D011523:Protoplasts / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013312:Stress, Physiological / Q000187:drug effects; D014158:Transcription, Genetic / Q000187:drug effects
chemical_list: D029681:Arabidopsis Proteins; D045265:Natriuretic Peptides; C464762:PNP-A protein, Arabidopsis; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D000040:Abscisic Acid; D005966:Glucuronidase; D006152:Cyclic GMP