New Synonymies and Combinations for New World Pselaphinae (Coleoptera: Staphylinidae)

The following new synonymies and new combinations for Pselaphinae of North and Central America are documented: Anarmodius aequinoctialis (Motschulsky) (Trichonyx), New Comb.; Anthylarthron cornutum (Brendel) (= Anthylarthron curtipenne Casey, New Syn.); Aporhexius robustus (Motschulsky) (Euplectus), New Comb.; Batrisodespunctlfrons Casey (= Batrisodes appalachianus Casey, New Syn.); Batrisodes ionae (LeConte) (= Batrisodes caseyt Blatchley, New Syn.); Batrisodes clypeonotus (Brendel) (= Batrisodes kahli Bowman, New Syn.); Batrisodes lineaticollis (Aube) (= Batrisus globosus LeConte, New Syn.); Brachygluta corniventris (Motschulsky) (Bryaxts), New Comb., (= Bryaxts illinoiensis Brendel, New Syn.); Cedius ziegleri LeConte (= Cedius robustus Casey, New Syn.); Conoplectus simplex (Motschulsky) (Rhexius), New Comb., jun. syn. of Conoplectus canaliculatus (LeConte), New Syn.; Ctenisodes Raffray (= Pilopius Casey, New Syn.); Cylindrarctus ludovicianus (Brendel) (= Cylindrarctus comes Casey, New Syn.; Dalmosanus Park (= Pygmactium Grigarick and Schuster, New Syn.); Decarthron consanguineum (Motschulsky) (Bryaxis), New Comb.; Decarthron formiceti (LeConte) (= Decarthron rayi Park, = Decarthron seriepunctatum Brendel, New Syns.); Decarthron velutinum (LeConte), New Status (= D. formiceti, Park, 1958); Decarthron marinum Brendel (= Decarthron diversum Park, New Syn.); Decarthron robustum (Motschulsky) (Metaxis), New Comb.; Euphalepsus Reitter (= Barada Raffray, = Tetrasemus Jeannel, New Syns.), in subtribe Baradina; Eupsentus dilatatus Motschulsky (= Eupsenius rufus LeConte, New Syn.); Eurhexius canaliculatus (Motschulsky) (Trichonyx), New Comb. (= Eurhexius zonalis Park, New Syn.); Harmophola adusta (Motschulsky) (Euplectus), New Comb.; Iteticus cylindricus (Motschulsky) (Batrisus), New Comb.; Nisaxis Casey (=Dranisaxa Park, New Syn.); Oropus strtatus (LeConte) (=Oropus keeni Casey and O. brevipennis Casey, New Syns.); Panaramecia tropicalis (Motschulsky) (Euplectus), New Comb. (= Panaramecia zvilliamsi Park, New Syn.); Phamisus Aube, (= Canthoderus Motschulsky, New Syn.); Pselaptus oedipus (Sharp) (Bryaxis, Cryptorhinula), New Comb.; Pselaphus bellax Casey (= Pselaphus ulkei Bowman, New Syn); Reichenbachia intacta (Sharp) (= Bryaxis sarcinaria Schaufuss, New Syn.); Reichenbachia pruinosa (Motschulsky) (Bryaxis), New Comb., (= Bryaxis macrura Motschulsky, = Reichenbachia bterigi Park, New Syns.); Reichenbachia rubricunda (Aube) (= Bryaxis gemmifer LeConte, New Syn.); Trimicerus Motschulsky, (= Batrybraxis Reitter, New Syn.); Trimicerus corn?gera (Motschulsky) (Bryaxis), New Comb. (= Batrybraxis panamensis Park, New Syn.); Trimicerus pacificus Motschulsky (= Batrybraxis bowmani Park, New Syn.); Trimiomelba dubia (LeConte) (= Trimium americanum Motschulsky, = Trimium convexulum LeConte, = Trimiomelba laevis Casey, New Syns.); Tyrus humeralis (Aube) (= Tyrus consimilis Casey, New Syn.); Tyrus semiruber Casey (= Tyrus humeralis of authors); Tyrus cortidnus Casey (= Tyrus carinifer Casey, New Syn.); Xybarida trimioides (Sharp) (Bryaxis, Cryptorhinula), New Comb. Lectotype designations: Batrisus ionae LeConte; Batrisus globosus LeConte; Bryaxis consangu?nea Motschulsky; Bryaxis corniventris Motschulsky; Bryaxis pruinosa Motschulsky; Metaxis robusta Motschulsky; Rhextus simplex Motschulsky; Trimium americanum LeConte; Tyrus consimilis Casey. New species and genera: Cylindrarctus semin?le Chandler, New Species (= Cylindrarctus comes, Chandler, 1988); Motschtyrus pilosus (Motschulsky) (Tychus), Panama, New Genus, New Comb

Active immunization against alpha-synuclein ameliorates the degenerative pathology and prevents demyelination in a model of multiple system atrophy.

BackgroundMultiple system atrophy (MSA) is a neurodegenerative disease characterized by parkinsonism, ataxia and dysautonomia. Histopathologically, the hallmark of MSA is the abnormal accumulation of alpha-synuclein (α-syn) within oligodendroglial cells, leading to neuroinflammation, demyelination and neuronal death. Currently, there is no disease-modifying treatment for MSA. In this sense, we have previously shown that next-generation active vaccination technology with short peptides, AFFITOPEs®, was effective in two transgenic models of synucleinopathies at reducing behavioral deficits, α-syn accumulation and inflammation.ResultsIn this manuscript, we used the most effective AFFITOPE® (AFF 1) for immunizing MBP-α-syn transgenic mice, a model of MSA that expresses α-syn in oligodendrocytes. Vaccination with AFF 1 resulted in the production of specific anti-α-syn antibodies that crossed into the central nervous system and recognized α-syn aggregates within glial cells. Active vaccination with AFF 1 resulted in decreased accumulation of α-syn, reduced demyelination in neocortex, striatum and corpus callosum, and reduced neurodegeneration. Clearance of α-syn involved activation of microglia and reduced spreading of α-syn to astroglial cells.ConclusionsThis study further validates the efficacy of vaccination with AFFITOPEs® for ameliorating the neurodegenerative pathology in synucleinopathies

On the spider species described by L. Koch in 1882 from the Balearic Islands (Araneae)

Examination of the L. Koch collection of the Zoological Museum in Berlin allows us to propose the following new synonyms and combinations: Erigone marina L. Koch, 1882 = Oedothorax fuscus (Blackwall, 1834) n. syn.; Theridion elimatum L. Koch, 1882 = Enoplognatha diversa (Blackwall, 1859) n. syn.; Liocranum variabilis Wunderlich, 2008 = Zora inornata L. Koch, 1882 n. syn. = Liocranum inornatum n. comb.; Lycosa perspicax L. Koch, 1882 = Arctosa fulvolineata (Lucas,1846) n. syn.; Alopecosella Roewer, 1960 = Arctosa C. L. Koch, 1847 n. syn.; Lycosa subhirsuta L. Koch, 1882 = Arctosa lacustris (Simon, 1876) n. syn.; Philodromus vegetus L. Koch, 1882 = Thanatus vulgaris Simon, 1870 n. syn.; Ozyptila bicuspis Simon, 1932 = Ozyptila furcula L. Koch, 1882 n. syn.; Haplodrassus maroccanus Denis, 1956 = Drassus parvulus L. Koch, 1882 n. syn. = Haplodrassus parvicorpus (Roewer, 1951) n. comb. (replacement name); Zelotes ruscinensis Simon, 1914 = Zelotes semirufa (L. Koch, 1882) n. syn.; Phlegra simoni L. Koch, 1882 = Phlegra bresnieri Lucas, 1846 n. syn.; Trochosula conspersa (L. Koch, 1882), Lycorma fraisnei (L. Koch, 1882), Lycorma insulana (L. Koch, 1882), Arctosa misella (L. Koch, 1992) and Pirata simplex (L. Koch, 1882) are all retransferred to their original genus Lycosa stat. rev. Cheiracanthium occidentale L. Koch, 1882, Ozyptila furcula L. Koch, 1882 and Zelotes callidus (Simon, 1878) are redescribed

Hippocampal neuronal cells that accumulate α-synuclein fragments are more vulnerable to Aβ oligomer toxicity via mGluR5--implications for dementia with Lewy bodies.

BackgroundIn dementia with Lewy bodies (DLB) abnormal interactions between α-synuclein (α-syn) and beta amyloid (Aβ) result in selective degeneration of neurons in the neocortex, limbic system and striatum. However, factors rendering these neurons selectively vulnerable have not been fully investigated. The metabotropic glutamate receptor 5 (mGluR5) has been shown to be up regulated in DLB and might play a role as a mediator of the neurotoxic effects of Aβ and α-syn in vulnerable neuronal populations. In this context, the main objective of the present study was to investigate the role of mGluR5 as a mediator of the neurotoxic effects of α-syn and Aβ in the hippocampus.ResultsWe generated double transgenic mice over-expressing amyloid precursor protein (APP) and α-syn under the mThy1 cassette and investigated the relationship between α-syn cleavage, Aβ, mGluR5 and neurodegeneration in the hippocampus. We found that compared to the single tg mice, the α-syn/APP tg mice displayed greater accumulation of α-syn and mGluR5 in the CA3 region of the hippocampus compared to the CA1 and other regions. This was accompanied by loss of CA3 (but not CA1) neurons in the single and α-syn/APP tg mice and greater loss of MAP 2 and synaptophysin in the CA3 in the α-syn/APP tg. mGluR5 gene transfer using a lentiviral vector into the hippocampus CA1 region resulted in greater α-syn accumulation and neurodegeneration in the single and α-syn/APP tg mice. In contrast, silencing mGluR5 with a lenti-shRNA protected neurons in the CA3 region of tg mice. In vitro, greater toxicity was observed in primary hippocampal neuronal cultures treated with Aβ oligomers and over-expressing α-syn; this effect was attenuated by down-regulating mGluR5 with an shRNA lentiviral vector. In α-syn-expressing neuronal cells lines, Aβ oligomers promoted increased intracellular calcium levels, calpain activation and α-syn cleavage resulting in caspase-3-dependent cell death. Treatment with pharmacological mGluR5 inhibitors such as 2-Methyl-6-(phenylethynyl)pyridine (MPEP) and 3-((2-Methyl-4-thiazolyl)ethynyl)pyridine (MTEP) attenuated the toxic effects of Aβ in α-syn-expressing neuronal cells.ConclusionsTogether, these results support the possibility that vulnerability of hippocampal neurons to α-syn and Aβ might be mediated via mGluR5. Moreover, therapeutical interventions targeting mGluR5 might have a role in DLB

Localization of α-synuclein in teleost central nervous system: immunohistochemical and Western blot evidence by 3D5 monoclonal antibody in the common carp, Cyprinus carpio

Alpha synuclein (α-syn) is a 140 amino acid vertebrate-specific protein, highly expressed in the human nervous system and abnormally accumulated in Parkinson's disease and other neurodegenerative disorders, known as synucleinopathies. The common occurrence of α-syn aggregates suggested a role for α-syn in these disorders, although its biological activity remains poorly understood. Given the high degree of sequence similarity between vertebrate α-syns, we investigated this proteins in the CNS of the common carp Cyprinus carpio, with the aim of comparing its anatomical and cellular distribution with that of mammalian α-syn. The distribution of α-syn was analyzed by semiquantitative Western blot, immunohistochemistry and immunofluorescence by a novel monoclonal antibody (3D5) against a fully conserved epitope between carp and human α-syn. The distribution of 3D5 immunoreactivity was also compared with that of ChAT, TH and 5HT by double immunolabelings. Results show that α-syn-like protein of about 17 kDa is expressed to different levels in several brain regions and in the spinal cord. Immunoreactive materials were localized in neuronal perikarya and varicose fibers but not in the nucleus. Present findings indicate that α-syn-like proteins may be expressed in few subpopulations of catecholaminergic and serotoninergic neurons in the carp brain. However, evidence of cellular colocalization 3D5/TH or 3D5/5HT was rare. Differently, the same proteins appear to be co-expressed with ChAT by cholinergic neurons in several motor and reticular nuclei. These results sustain the functional conservation of the α-syn expression in cholinergic systems and suggest that α-syn modulates similar molecular pathways in phylogenetically distant vertebrates. This article is protected by copyright. All rights reserved

Gut-seeded α-synuclein fibrils promote gut dysfunction and brain pathology specifically in aged mice

Parkinson’s disease is a synucleinopathy that is characterized by motor dysfunction, death of midbrain dopaminergic neurons and accumulation of α-synuclein (α-Syn) aggregates. Evidence suggests that α-Syn aggregation can originate in peripheral tissues and progress to the brain via autonomic fibers. We tested this by inoculating the duodenal wall of mice with α-Syn preformed fibrils. Following inoculation, we observed gastrointestinal deficits and physiological changes to the enteric nervous system. Using the AAV-PHP.S capsid to target the lysosomal enzyme glucocerebrosidase for peripheral gene transfer, we found that α-Syn pathology is reduced due to the increased expression of this protein. Lastly, inoculation of α-Syn fibrils in aged mice, but not younger mice, resulted in progression of α-Syn histopathology to the midbrain and subsequent motor defects. Our results characterize peripheral synucleinopathy in prodromal Parkinson’s disease and explore cellular mechanisms for the gut-to-brain progression of α-Syn pathology

[2.2](4,7)Isobenzofuranophanes - Synthesis, Characterisation and Reactivity

The isomeric Diels-Alder adducts 3, obtained by cycloaddition of tetraphenylcyclopentadienone to the 4,5:12,13-bis-(oxanorbornadieno)[2.2]paracyclophanes syn,syn- and anti,-syn-2[Note ][The stereochemical descriptors syn and anti refer to the orientation of the oxygen bridge in the oxabicyclo[2.2.1]heptadiene subunits with respect to the [2.2]paracyclophaneskeleton.], yield the unstable isobenzofuranophane 4 by consecutive extrusion of carbon monoxide and tetraphenylbenzene when heated to 180°C. The molecular ion of 4 was observed in the EI mass spectrum. The stable tetraphenyl-substituted analogue 10 was synthesized independently from the previously unknown 4,5,12,13-tetrabenzoyl[2.2]paracyclophane (9). UV/Vis as well as fluorescence spectra and an X-ray crystal structure analysis of 9 are reported