Primer registro de Syncharina lineiceps (Hemiptera: Cicadellidae) en la Argentina: clave para el reconocimiento de las especies del género

We report for the first time in Argentina the presence of Syncharina lineiceps (Spinola) and it is cited as new record for blueberries crops. For each species of the genus Syncharina Young we provide updated information referred to geographic distribution and plants hosts. A key to identify the species of the genus is presented.Se cita por primera vez para la Argentina la especie Syncharina lineiceps (Spinola) y se da a conocer como nuevo registro para los cultivos de arándanos. Para cada especie del género Syncharina Young, se proporciona información actualizada referida a la distribución geográfica y las plantas huéspedes. Se propone una clave para identificar las especies del género

Genus Plesiommata Provancher (Hemiptera: Cicadellidae) in Argentina: first detailed description of the female genitalia and comparisons with its neotropical congeners

Plesiommata Provancher is a sharpshooter genus with six species described, three present in the Neotropics. The morphology of the female genitalia of this genus is still poorly known. In this contribution, the female genitalia of P. mollicella (Fowler) and P. corniculata Young are described and illustrated for the first time. The vector species P. corniculata Young is recorded as new for Argentina. A key to Neotropical species including new female genital characters is presented along with updated information as new distribution records, host plant records and phytosanitary importance.Fil: Defea, Bárbara Soledad. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. División Entomología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Paradell, Susana Liria. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. División Entomología; ArgentinaFil: Marino, Ana Maria. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. División Entomología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentin

Descriptions of immatures of the South American plant hopper, Taosa (C.) longula

Descriptions of the immature stages of Taosa (Cuernavaca) longula Remes Lenicov (Hemiptera: Fulgoroidea: Dictyopharidae) and a key for their identification is provided for specimens collected on the water hyacinth, Eichhornia crassipes (Martius) Solms-Laubach (Commelinales: Pontederiaceae), in northeastern Argentina and Peru. Newly emerged nymphs from eggs collected in the field were reared in rearing chambers, and each stage was fixed to microscopic examination and illustration. Fifth nymphal instars can be easily recognized from congeners by the brown marked pattern coloration, shorter vertex, and the distinguishable median carina along the frons. Information on behavior and developmental time is also included.Fil: Marino, Ana Maria. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. División Entomología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Hernández, María Cristina. Fundación para el Estudio de Especies Invasivas; ArgentinaFil: Brentassi, Maria Eugenia. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. División Entomología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Defea, Bárbara Soledad. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. División Entomología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentin

Beta-arrestin inhibits CAMKKbeta-dependent AMPK activation downstream of protease-activated-receptor-2

<p>Abstract</p> <p>Background</p> <p>Proteinase-activated-receptor-2 (PAR₂) is a seven transmembrane receptor that can activate two separate signaling arms: one through Gαq and Ca²⁺mobilization, and a second through recruitment of β-arrestin scaffolds. In some cases downstream targets of the Gαq/Ca²⁺signaling arm are directly inhibited by β-arrestins, while in other cases the two pathways are synergistic; thus β-arrestins act as molecular switches capable of modifying the signal generated by the receptor.</p> <p>Results</p> <p>Here we demonstrate that PAR₂can activate adenosine monophosphate-activated protein kinase (AMPK), a key regulator of cellular energy balance, through Ca²⁺-dependent Kinase Kinase β (CAMKKβ), while inhibiting AMPK through interaction with β-arrestins. The ultimate outcome of PAR₂activation depended on the cell type studied; in cultured fibroblasts with low endogenous β-arrestins, PAR₂activated AMPK; however, in primary fat and liver, PAR₂only activated AMPK in β-arrestin-2^-/-mice. β-arrestin-2 could be co-immunoprecipitated with AMPK and CAMKKβ under baseline conditions from both cultured fibroblasts and primary fat, and its association with both proteins was increased by PAR₂activation. Addition of recombinant β-arrestin-2 to in vitro kinase assays directly inhibited phosphorylation of AMPK by CAMKKβ on Thr172.</p> <p>Conclusions</p> <p>Studies have shown that decreased AMPK activity is associated with obesity and Type II Diabetes, while AMPK activity is increased with metabolically favorable conditions and cholesterol lowering drugs. These results suggest a role for β-arrestin in the inhibition of AMPK signaling, raising the possibility that β-arrestin-dependent PAR₂signaling may act as a molecular switch turning a positive signal to AMPK into an inhibitory one.</p

Proteinase-activated receptors in GtoPdb v.2023.1

Proteinase-activated receptors (PARs, nomenclature as agreed by the NC-IUPHAR Subcommittee on Proteinase-activated Receptors [39]) are unique members of the GPCR superfamily activated by proteolytic cleavage of their amino terminal exodomains. Agonist proteinase-induced hydrolysis unmasks a tethered ligand (TL) at the exposed amino terminus, which acts intramolecularly at the binding site in the body of the receptor to effect transmembrane signalling. TL sequences at human PAR1-4 are SFLLRN-NH2, SLIGKV-NH2, TFRGAP-NH2 and GYPGQV-NH2, respectively. With the exception of PAR3, synthetic peptides with these sequences (as carboxyl terminal amides) are able to act as agonists at their respective receptors. Several proteinases, including neutrophil elastase, cathepsin G and chymotrypsin can have inhibitory effects at PAR1 and PAR2 such that they cleave the exodomain of the receptor without inducing activation of G&#945;q-coupled calcium signalling, thereby preventing activation by activating proteinases but not by agonist peptides. Neutrophil elastase (NE) cleavage of PAR1 and PAR2 can however activate MAP kinase signaling by exposing a TL that is different from the one revealed by trypsin [87]. PAR2 activation by NE regulates inflammation and pain responses [115, 76] and triggers mucin secretion from airway epithelial cells [116]

β-Arrestin–Dependent Endocytosis of Proteinase-Activated Receptor 2 Is Required for Intracellular Targeting of Activated Erk1/2

Recently, a requirement for β-arrestin–mediated endocytosis in the activation of extracellular signal–regulated kinases 1 and 2 (ERK1/2) by several G protein–coupled receptors (GPCRs) has been proposed. However, the importance of this requirement for function of ERK1/2 is unknown. We report that agonists of Gαq-coupled proteinase–activated receptor 2 (PAR2) stimulate formation of a multiprotein signaling complex, as detected by gel filtration, immunoprecipitation and immunofluorescence. The complex, which contains internalized receptor, β-arrestin, raf-1, and activated ERK, is required for ERK1/2 activation. However, ERK1/2 activity is retained in the cytosol and neither translocates to the nucleus nor causes proliferation. In contrast, a mutant PAR2 (PAR2δST363/6A), which is unable to interact with β-arrestin and, thus, does not desensitize or internalize, activates ERK1/2 by a distinct pathway, and fails to promote both complex formation and cytosolic retention of the activated ERK1/2. Whereas wild-type PAR2 activates ERK1/2 by a PKC-dependent and probably a ras-independent pathway, PAR2(δST363/6A) appears to activate ERK1/2 by a ras-dependent pathway, resulting in increased cell proliferation. Thus, formation of a signaling complex comprising PAR2, β-arrestin, raf-1, and activated ERK1/2 might ensure appropriate subcellular localization of PAR2-mediated ERK activity, and thereby determine the mitogenic potential of receptor agonists

Proteinase-activated receptors in GtoPdb v.2021.3

Proteinase-activated receptors (PARs, nomenclature as agreed by the NC-IUPHAR Subcommittee on Proteinase-activated Receptors [39]) are unique members of the GPCR superfamily activated by proteolytic cleavage of their amino terminal exodomains. Agonist proteinase-induced hydrolysis unmasks a tethered ligand (TL) at the exposed amino terminus, which acts intramolecularly at the binding site in the body of the receptor to effect transmembrane signalling. TL sequences at human PAR1-4 are SFLLRN-NH2, SLIGKV-NH2, TFRGAP-NH2 and GYPGQV-NH2, respectively. With the exception of PAR3, synthetic peptides with these sequences (as carboxyl terminal amides) are able to act as agonists at their respective receptors. Several proteinases, including neutrophil elastase, cathepsin G and chymotrypsin can have inhibitory effects at PAR1 and PAR2 such that they cleave the exodomain of the receptor without inducing activation of G&#945;q-coupled calcium signalling, thereby preventing activation by activating proteinases but not by agonist peptides. Neutrophil elastase (NE) cleavage of PAR1 and PAR2 can however activate MAP kinase signaling by exposing a TL that is different from the one revealed by trypsin [82]. PAR2 activation by NE regulates inflammation and pain responses [111, 72] and triggers mucin secretion from airway epithelial cells [112]

Proteinase-activated receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

Proteinase-activated receptors (PARs, nomenclature as agreed by the NC-IUPHAR Subcommittee on Proteinase-activated Receptors [35]) are unique members of the GPCR superfamily activated by proteolytic cleavage of their amino terminal exodomains. Agonist proteinase-induced hydrolysis unmasks a tethered ligand (TL) at the exposed amino terminus, which acts intramolecularly at the binding site in the body of the receptor to effect transmembrane signalling. TL sequences at human PAR1-4 are SFLLRN-NH2, SLIGKV-NH2, TFRGAP-NH2 and GYPGQV-NH2, respectively. With the exception of PAR3, synthetic peptides with these sequences (as carboxyl terminal amides) are able to act as agonists at their respective receptors. Several proteinases, including neutrophil elastase, cathepsin G and chymotrypsin can have inhibitory effects at PAR1 and PAR2 such that they cleave the exodomain of the receptor without inducing activation of G&#945;q-coupled calcium signalling, thereby preventing activation by activating proteinases but not by agonist peptides. Neutrophil elastase (NE) cleavage of PAR1 and PAR2 can however activate MAP kinase signaling by exposing a TL that is different from the one revealed by trypsin [73]. PAR2 ectivation by NE regulates inflammation and pain responses [101, 65] and triggers mucin secretion from airway epithelial cells [102]

Biodiversity indicators in scientific collections: Diagnosis of the cicadellidae collection (insecta: Hemiptera) of museo de la plata, Argentina

Se caracterizó la diversidad de la colección de Hemiptera Cicadellidae del Museo de La Plata utilizando los siguientes indicadores: 1) Identificación taxonómica, grado de resolución taxonómica de la colección, 2) Representatividad taxonómica y geográfica de los especímenes montados, 3) Porcentaje de especímenes con asociaciones biológicas con plantas o parasitoides. Estos indicadores fueron comparados con los del Neotrópico y con la escala del Índice de Salud de Colecciones (escalas 6, 7 y 8). Se registraron 74 géneros, 119 especies y 2796 ejemplares de Cicadellinae, Coelidiinae, Deltocephalinae, Idiocerinae, Ledrinae y Xestocephalinae para Argentina más 110 especímenes del extranjero. Para la identificación taxonómica, el material se agrupó en cuatro categorías: A- Tipo etiquetado, fichado, catalogado y publicado, B- Identificado a especie, etiquetado, fichado, con datos biológicos (escalas 6 y 7), C- Identificado a género, etiquetado, fichado y D- Identificado a subfamilia, etiquetado, fichado (escala 8). Del grupo A se encontraron 166 especímenes, el grupo B representa el 94,95% de los ejemplares (2655) (escalas 6 y 7), del grupo C el porcentaje fue de 2,18% (61 ejemplares) y del grupo D el 2,86% (80 ejemplares) (8). La representatividad taxonómica de la colección es del 40,9% a subfamilia respecto al Neotrópico. A nivel genérico, las mejor representadas fueron Xestocephalinae, Ledrinae (33,3%), Cicadellinae (18,7%) y Deltocephalinae (17,7%). A nivel específico Ledrinae (12%), Deltocephalinae (6,5%) y Cicadellinae (4,2%). Cicadellinae y Deltocephalinae representan el 96% de los ejemplares. La representatividad geográfica respecto a la Argentina fue alta 86,95 %; sólo el 12,53% de los ejemplares presentó plantas asociadas.The diversity of Cicadellidae (Hemiptera) housed in the collection of Museo de La Plata was characterized using the following indicators: 1) Taxonomic identification, degree of taxonomic resolution; 2) Taxonomic and geographic representativeness of the pinned specimens 3) Percentage of specimens associated with plants or parasitoids. These indicators were compared with available data for the Neotropical region and with The Collections Health Index (scales 6, 7 and 8). Seventy-four genera, 119 species and 2796 specimens of Cicadellinae, Coelidiinae, Deltocephalinae, Idiocerinae, Ledrinae and Xestocephalinae were recorded. To assess taxonomic identification, the specimens were grouped into four categories: A-Type material, labeled, databased, catalogued and published, B-Identified to species level, labeled and databased (scale 6 and 7 of the Collections Health Index), C-Identified to genus level, labeled and databased and, D-Identified to subfamily level, labeled and databased (8). From group A, 166 specimens were recorded, group B represented 94.95% of the total specimens studied (2655) (scales 6, 7), group C represented 2.18% (61 specimens) and D, 2.86% (80 specimens) (8). Taxonomic representativeness to subfamily level was 40.9% with respect to the Neotropics. At generic level, the subfamilies best represented were Xestocephalinae, Ledrinae (33.3%), Cicadellinae (18.7%) and Deltocephalinae (17.7%) and, to specific level, Ledrinae (12%), Deltocephalinae (6.5%) and Cicadellinae (4.2%). Cicadellinae and Deltocephalinae represent 96% of the total recorded specimens. The geographic representativeness was high 86.95% with respect to Argentina; only 12.53% of the specimens presented host plant data.Facultad de Ciencias Naturales y Muse