Carisma e poder no discurso religioso: um estudo do legado de Masaharu Taniguchi A Seicho-No-Ie no Brasil

A inserção das novas religiões japonesas no Brasil, entre elas a Seicho-No-Ie, está diretamente ligada à imigração japonesa, iniciada em 1908. Esses imigrantes trouxeram com eles cosmovisões e práticas religiosas, que faziam parte de um antigo e rico legado cultural. No Japão, o surgimento dessas novas religiões se deu, principalmente, em decorrência da Restauração Meiji (1868-1912), um período de modernização daquele país. Nessa época apareceram a Oomoto, Tenrikyô, Soka Gakkai, Igreja Messiânica Mundial e a Seicho-No-Ie. Masaharu Taniguchi (1893-1985) fundou a Seicho-No-Ie em 1930, um movimento filosófico-religioso, cujo nome significa lar do progredir infinito . A sua base doutrinária está fundamentada nas tradições budistas e xintoístas mescladas, posteriormente, com preceitos do cristianismo. O fato fundante dessa nova religião são as revelações que Taniguchi afirma ter recebido de uma divindade xintoísta. Foi, no entanto, a divulgação de seus ensinamentos, por meio de uma revista, que deu início à sua expansão no Japão e depois em várias partes do mundo. Taniguchi foi um líder profético e carismático, que instaurou um sistema de dominação simbólica peculiar, mas passível de ser analisada à luz das teorias de Max Weber e Pierre Bourdieu. O processo de institucionalização tomou a família Taniguchi como o modelo ideal, articulando-se a partir dela um sistema de dominação misto de patriarcal, carismático e burocrático. Assim se formou um legado, inicialmente inspirado na tradição imperial japonesa, em que o papel feminino está subordinado à ordem androcêntrica. Esse fator privilegiou a sucessão do Mestre Taniguchi por seu genro, Seicho Arachi, que adotou o sobrenome do sogro e, anos mais tarde, se reproduziu na ascensão do primogênito do casal Seicho e Emiko, Masanobu Taniguchi. No Brasil, os imigrantes japoneses, já no início dos anos 30, descobriram a Seicho-No-Ie, graças ao recebimento do mensário editado no Japão por Taniguchi. Foi, entretanto, o trabalho missionário dos irmãos Daijiro e Miyoshi Matsuda, imigrantes japoneses no Brasil, que a Seicho-No-Ie aqui se estabeleceu e se desenvolveu, obtendo o seu reconhecimento oficial como filial da sede japonesa, em 30/05/51. Inicialmente a Seicho-No-Ie se restringiu às fronteiras étnicas e culturais da colônia japonesa, porém, a partir de 1960, passou a atrair brasileiros, enquanto buscava aculturar as suas atividades doutrinárias. Busca-se neste estudo descrever a organização assumida no Brasil pela Seicho-No-Ie, a sua estrutura doutrinária e administrativa, apresentando-as como uma reprodução da Sede Internacional situada no Japão. Procuramos valorizar o discurso religioso da Seicho-No-Ie contido nos livros e revistas publicados, e atualmente, em programas de televisão. Acreditamos serem esses meios, ao lado dos ensinamentos transmitidos por um seleto corpo de preletores, as principais formas de reprodução desse legado que Masaharu Taniguchi deixou aos seus seguidores, japoneses, brasileiros e de outras nacionalidades.

Carisma e poder no discurso religioso: um estudo do legado de Masaharu Taniguchi A Seicho-No-Ie no Brasil

A inserção das novas religiões japonesas no Brasil, entre elas a Seicho-No-Ie, está diretamente ligada à imigração japonesa, iniciada em 1908. Esses imigrantes trouxeram com eles cosmovisões e práticas religiosas, que faziam parte de um antigo e rico legado cultural. No Japão, o surgimento dessas novas religiões se deu, principalmente, em decorrência da Restauração Meiji (1868-1912), um período de modernização daquele país. Nessa época apareceram a Oomoto, Tenrikyô, Soka Gakkai, Igreja Messiânica Mundial e a Seicho-No-Ie. Masaharu Taniguchi (1893-1985) fundou a Seicho-No-Ie em 1930, um movimento filosófico-religioso, cujo nome significa lar do progredir infinito . A sua base doutrinária está fundamentada nas tradições budistas e xintoístas mescladas, posteriormente, com preceitos do cristianismo. O fato fundante dessa nova religião são as revelações que Taniguchi afirma ter recebido de uma divindade xintoísta. Foi, no entanto, a divulgação de seus ensinamentos, por meio de uma revista, que deu início à sua expansão no Japão e depois em várias partes do mundo. Taniguchi foi um líder profético e carismático, que instaurou um sistema de dominação simbólica peculiar, mas passível de ser analisada à luz das teorias de Max Weber e Pierre Bourdieu. O processo de institucionalização tomou a família Taniguchi como o modelo ideal, articulando-se a partir dela um sistema de dominação misto de patriarcal, carismático e burocrático. Assim se formou um legado, inicialmente inspirado na tradição imperial japonesa, em que o papel feminino está subordinado à ordem androcêntrica. Esse fator privilegiou a sucessão do Mestre Taniguchi por seu genro, Seicho Arachi, que adotou o sobrenome do sogro e, anos mais tarde, se reproduziu na ascensão do primogênito do casal Seicho e Emiko, Masanobu Taniguchi. No Brasil, os imigrantes japoneses, já no início dos anos 30, descobriram a Seicho-No-Ie, graças ao recebimento do mensário editado no Japão por Taniguchi. Foi, entretanto, o trabalho missionário dos irmãos Daijiro e Miyoshi Matsuda, imigrantes japoneses no Brasil, que a Seicho-No-Ie aqui se estabeleceu e se desenvolveu, obtendo o seu reconhecimento oficial como filial da sede japonesa, em 30/05/51. Inicialmente a Seicho-No-Ie se restringiu às fronteiras étnicas e culturais da colônia japonesa, porém, a partir de 1960, passou a atrair brasileiros, enquanto buscava aculturar as suas atividades doutrinárias. Busca-se neste estudo descrever a organização assumida no Brasil pela Seicho-No-Ie, a sua estrutura doutrinária e administrativa, apresentando-as como uma reprodução da Sede Internacional situada no Japão. Procuramos valorizar o discurso religioso da Seicho-No-Ie contido nos livros e revistas publicados, e atualmente, em programas de televisão. Acreditamos serem esses meios, ao lado dos ensinamentos transmitidos por um seleto corpo de preletores, as principais formas de reprodução desse legado que Masaharu Taniguchi deixou aos seus seguidores, japoneses, brasileiros e de outras nacionalidades.

Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the β1-adrenergic receptor

Several G-protein coupled receptors, such as the β1-adrenergic receptor (β1-AR), contain polyproline motifs within their intracellular domains. Such motifs in other proteins are known to mediate protein–protein interactions such as with Src homology (SH)3 domains. Accordingly, we used the proline-rich third intracellular loop of the β1-AR either as a glutathione S-transferase fusion protein in biochemical “pull-down” assays or as bait in the yeast two-hybrid system to search for interacting proteins. Both approaches identified SH3p4/p8/p13 (also referred to as endophilin 1/2/3), a SH3 domain-containing protein family, as binding partners for the β1-AR. In vitro and in human embryonic kidney (HEK) 293 cells, SH3p4 specifically binds to the third intracellular loop of the β1-AR but not to that of the β2-AR. Moreover, this interaction is mediated by the C-terminal SH3 domain of SH3p4. Functionally, overexpression of SH3p4 promotes agonist-induced internalization and modestly decreases the Gs coupling efficacy of β1-ARs in HEK293 cells while having no effect on β2-ARs. Thus, our studies demonstrate a role of the SH3p4/p8/p13 protein family in β1-AR signaling and suggest that interaction between proline-rich motifs and SH3-containing proteins may represent a previously underappreciated aspect of G-protein coupled receptor signaling.

CP12 provides a new mode of light regulation of Calvin cycle activity in higher plants

CP12 is a small nuclear encoded chloroplast protein of higher plants, which was recently shown to interact with NAD(P)H–glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC 1.2.1.13), one of the key enzymes of the reductive pentosephosphate cycle (Calvin cycle). Screening of a pea cDNA library in the yeast two-hybrid system for proteins that interact with CP12, led to the identification of a second member of the Calvin cycle, phosphoribulokinase (PRK; EC 2.7.1.19), as a further specific binding partner for CP12. The exchange of cysteines for serines in CP12 demonstrate that interaction with PRK occurs at the N-terminal peptide loop of CP12. Size exclusion chromatography and immunoprecipitation assays reveal the existence of a stable 600-kDa PRK/CP12/GAPDH complex in the stroma of higher plant chloroplasts. Its stoichiometry is proposed to be of two N-terminally dimerized CP12 molecules, each carrying one PRK dimer on its N terminus and one A2B2 complex of GAPDH subunits on the C-terminal peptide loop. Incubation of the complex with NADP or NADPH, in contrast to NAD or NADH, causes its dissociation. Assays with the stromal 600-kDa fractions in the presence of the four different nicotinamide-adenine dinucleotides indicate that PRK activity depends on complex dissociation and might be further regulated by the accessible ratio of NADP/NADPH. From these results, we conclude that light regulation of the Calvin cycle in higher plants is not only via reductive activation of different proteins by the well-established ferredoxin/thioredoxin system, but in addition, by reversible dissociation of the PRK/CP12/GAPDH complex, mediated by NADP(H).

Myozenin: An α-actinin- and γ-filamin-binding protein of skeletal muscle Z lines

To better understand the structure and function of Z lines, we used sarcomeric isoforms of α-actinin and γ-filamin to screen a human skeletal muscle cDNA library for interacting proteins by using the yeast two-hybrid system. Here we describe myozenin (MYOZ), an α-actinin- and γ-filamin-binding Z line protein expressed predominantly in skeletal muscle. Myozenin is predicted to be a 32-kDa, globular protein with a central glycine-rich domain flanked by α-helical regions with no strong homologies to any known genes. The MYOZ gene has six exons and maps to human chromosome 10q22.1-q22.2. Northern blot analysis demonstrated that this transcript is expressed primarily in skeletal muscle with significantly lower levels of expression in several other tissues. Antimyozenin antisera stain skeletal muscle in a sarcomeric pattern indistinguishable from that seen by using antibodies for α-actinin, and immunogold electron microscopy confirms localization specifically to Z lines. Thus, myozenin is a skeletal muscle Z line protein that may be a good candidate gene for limb-girdle muscular dystrophy or other neuromuscular disorders.

Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase ζ/β by the yeast substrate-trapping system

We used a genetic method, the yeast substrate-trapping system, to identify substrates for protein tyrosine phosphatases ζ (PTPζ/RPTPβ). This method is based on the yeast two-hybrid system, with two essential modifications: conditional expression of protein tyrosine kinase v-src (active src) to tyrosine-phosphorylate the prey proteins and screening by using a substrate-trap mutant of PTPζ (PTPζ-D1902A) as bait. By using this system, several substrate candidates for PTPζ were isolated. Among them, GIT1/Cat-1 (G protein-coupled receptor kinase-interactor 1/Cool-associated, tyrosine-phosphorylated 1) was examined further. GIT1/Cat-1 bound to PTPζ-D1902A dependent on the substrate tyrosine phosphorylation. Tyrosine-phosphorylated GIT1/Cat-1 was dephosphorylated by PTPζ in vitro. Immunoprecipitation experiments indicated that PTPζ-D1902A and GIT1/Cat-1 form a stable complex also in mammalian cells. Immunohistochemical analyses revealed that PTPζ and GIT1/Cat-1 were colocalized in the processes of pyramidal cells in the hippocampus and neocortex in rat brain. Subcellular colocalization was further verified in the growth cones of mossy fibers from pontine explants and in the ruffling membranes and processes of B103 neuroblastoma cells. Moreover, pleiotrophin, a ligand for PTPζ, increased tyrosine phosphorylation of GIT1/Cat-1 in B103 cells. All these results indicate that GIT1/Cat-1 is a substrate molecule of PTPζ.

Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions.

Macromolecular interactions define many biological phenomena. Although genetic methods are available to identify novel protein-protein and DNA-protein interactions, no genetic system has thus far been described to identify molecules or mutations that dissociate known interactions. Herein, we describe genetic systems that detect such events in the yeast Saccharomyces cerevisiae. We have engineered yeast strains in which the interaction of two proteins expressed in the context of the two-hybrid system or the interaction between a DNA-binding protein and its binding site in the context of the one-hybrid system is deleterious to growth. Under these conditions, dissociation of the interaction provides a selective growth advantage, thereby facilitating detection. These methods referred to as the "reverse two-hybrid system" and "reverse one-hybrid system" facilitate the study of the structure-function relationships and regulation of protein-protein and DNA-protein interactions. They should also facilitate the selection of dissociator molecules that could be used as therapeutic agents.

TRAF5, a novel tumor necrosis factor receptor-associated factor family protein, mediates CD40 signaling.

Signals emanating from CD40 play crucial roles in B-cell function. To identify molecules that transduce CD40 signalings, we have used the yeast two-hybrid system to done cDNAs encoding proteins that bind the cytoplasmic tail of CD40. A cDNA encoding a putative signal transducer protein, designated TRAF5, has been molecularly cloned. TRAF5 has a tumor necrosis factor receptor-associated factor (TRAF) domain in its carboxyl terminus and is most homologous to TRAF3, also known as CRAF1, CD40bp, or LAP-1, a previously identified CD40-associated factor. The amino terminus has a RING finger domain, a cluster of zinc fingers and a coiled-coil domain, which are also present in other members of the TRAF family protein except for TRAF1. In vitro binding assays revealed that TRAF5 associates with the cytoplasmic tail of CD40, but not with the cytoplasmic tail of tumor receptor factor receptor type 2, which associates with TRAF2. Based on analysis of the association between TRAF5 and various CD40 mutants, residues 230-269 of CD40 are required for the association with TRAF5. In contrast to TRAF3, overexpression of TRAF5 activates transcription factor nuclear factor kappa B. Furthermore, amino-terminally truncated forms of TRAF5 suppress the CD40-mediated induction of CD23 expression, as is the case with TRAF3. These results suggest that TRAF5 and TRAF3 could be involved in both common and distinct signaling pathways emanating from CD40.

Interaction of cyclooxygenases with an apoptosis- and autoimmunity-associated protein.

Cyclooxygenases (COXs) 1 and 2 are 72-kDa, intralumenal residents of the endoplasmic reticulum (ER) and nuclear envelope, where they catalyze the rate-limiting steps in the conversion of arachidonate to the physiologically dynamic prostanoids. Recent studies, including the generation of knockout mice, show COX-1 and COX-2 to have biologically distinct roles within cells and organisms. Also apparent is that arachidonate substrate is selectably metabolized by COX-2 after mitogen stimulation in many cells that contain both isoforms. Because COX-1 and COX-2 are highly conserved in all residues needed for catalysis and in their purified forms have almost identical kinetic properties, we have searched for COX-interacting ER proteins that might mediate these unique isoenzymic properties. Using COXs as bait in the yeast two-hybrid system, we identified autoimmunity- and apoptosis-associated nucleobindin (Nuc) as a protein that specifically interacts with both isoenzymes. COX-Nuc binding was substantiated by immunoprecipitation experiments, which showed that COX-1 and, to a lesser extent, COX-2 form complexes with Nuc in vitro. When overexpressed in COS-1 cells, Nuc was found to be extracellularly released. However, when Nuc was co-overexpressed with COX-1 or COX-2, its release was reduced by >80%. This finding suggests that COX isoenzymes participate in the retention of Nuc within the lumen of the ER, where COX may regulate the release of Nuc from the cell. It also identifies Nuc as a potential regulator of COXs through this interaction.

GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain.

Using the yeast two-hybrid system we have identified a human protein, GAIP (G Alpha Interacting Protein), that specifically interacts with the heterotrimeric GTP-binding protein G alpha i3. Interaction was verified by specific binding of in vitro-translated G alpha i3 with a GAIP-glutathione S-transferase fusion protein. GAIP is a small protein (217 amino acids, 24 kDa) that contains two potential phosphorylation sites for protein kinase C and seven for casein kinase 2. GAIP shows high homology to two previously identified human proteins, GOS8 and 1R20, two Caenorhabditis elegans proteins, CO5B5.7 and C29H12.3, and the FLBA gene product in Aspergillus nidulans--all of unknown function. Significant homology was also found to the SST2 gene product in Saccharomyces cerevisiae that is known to interact with a yeast G alpha subunit (Gpa1). A highly conserved core domain of 125 amino acids characterizes this family of proteins. Analysis of deletion mutants demonstrated that the core domain is the site of GAIP's interaction with G alpha i3. GAIP is likely to be an early inducible phosphoprotein, as its cDNA contains the TTTTGT sequence characteristic of early response genes in its 3'-untranslated region. By Northern analysis GAIP's 1.6-kb mRNA is most abundant in lung, heart, placenta, and liver and is very low in brain, skeletal muscle, pancreas, and kidney. GAIP appears to interact exclusively with G alpha i3, as it did not interact with G alpha i2 and G alpha q. The fact that GAIP and Sst2 interact with G alpha subunits and share a common domain suggests that other members of the GAIP family also interact with G alpha subunits through the 125-amino-acid core domain.

MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase.

A constitutively active fragment of rat MEK kinase 1 (MEKK1) consisting of only its catalytic domain (MEKK-C) expressed in bacteria quantitatively activates recombinant mitogen-activated protein (MAP) kinase/extracellular signal-regulated protein kinase (ERK) kinases 1 and 2 (MEK1 and MEK2) in vitro. Activation of MEK1 by MEKK-C is accompanied by phosphorylation of S218 and S222, which are also phosphorylated by the protein kinases c-Mos and Raf-1. MEKK1 has been implicated in regulation of a parallel but distinct cascade that leads to phosphorylation of N-terminal sites on c-Jun; thus, its role in the MAP kinase pathway has been questioned. However, in addition to its capacity to phosphorylate MEK1 in vitro, MEKK-C interacts with MEK1 in the two-hybrid system, and expression of mouse MEKK1 or MEKK-C in mammalian cells causes constitutive activation of both MEK1 and MEK2. Neither cotransfected nor endogenous ERK2 is highly activated by MEKK1 compared to its stimulation by epidermal growth factor in spite of significant activation of endogenous MEK. Thus, other as yet undefined mechanisms may be involved in determining information flow through the MAP kinase and related pathways.

Identificação e caracterização de RNA mensageiros candidatos a alvo das proteínas PUMILHO de Arabidopsis através do sistema triplo-híbrido de levedura

Proteínas PUF regulam a estabilidade e a tradução através da ligação a seqüências específicas nas regiões 3\' não traduzidas (3\' UTR) dos mensageiros. A ligação é mediada por um domínio de ligação conservado constituído por 8 repetições de aproximadamente 36 aminoácidos cada. Experimentos realizados no sistema triplo-híbrido de levedura mostraram que os homólogos PUF de Arabidopsis APUM-1, APUM-2 e APUM-3 são capazes de ligar especificamente à seqüência chamada de Elemento de Resposta a NANOS (NRE) reconhecida pelo homólogo PUF de Drosophila. A utilização de bibliotecas de expressão de RNA em ensaios no sistema triplo-híbrido permitiu a identificação de seqüências de ligação consenso para as três proteínas APUM. Análises computacionais identificaram elementos de ligação a APUM em regiões 3\' UTR de importantes transcritos relacionados ao controle do meristema do caule e à manutenção das células totipotentes. Nós mostramos que os homólogos APUM-l, APUM-2 e APUM-3 reconhecem elementos de ligação a APUM nas regiões 3\' UTR dos transcritos WUSCHEL, CLAVATA-1, ZWILLE e FASCIATA-2. Ensaios de RT-PCR e Western blot semiquantitativos mostraram que a quantidade dos transcritos WUSHEL e CLAVATA-1 é alterada em plantas antisenso induzíveis para APUM-l, APUM-2 e APUM-3. A relevância biológica dessas interações foi observada através de ensaios de coimunoprecipitação, confirmando, portanto, o primeiro caso de regulação traducional descrito para os mensageiros WUSCHEL e CLAVATA-1. Análises computacionais adicionais para a identificação de outros homólogos PUF em Arabidopsis encontraram vinte e cinco proteínas possuindo repetições PUF. Entre elas, os homólogos APUM-4, APUM-S e APUM-6 apresentam alta similaridade com as proteínas APUM-l, APUM-2 e APUM-3, sendo capazes de ligar especificamente à seqüência NRE e aos elementos de ligação a APUM presentes nas regiões 3\' UTR dos transcritos WUSCHEL, CLAVATA-1, ZWILLE e FASCIATA-ts resultados indicam que vários homólogos PUF podem agir como reguladores traducionais em Arabidopsis através de um mecanismo molecular conservado entre as espécies, podendo abrir uma nova área de investigação da regulação de mRNA em plantas.

Fragm. lat. II 95 - Biblia glossata (Ps 2), mit zusätzlichen Marginalglossen

Vorbesitzer: Stadtarchiv Frankfurt am Main

Fragm. lat. II 10 - Expositio in Cantica canticorum (Ct 1,10 - 2,17)

Trägerband: Ms. Barth. 66; Vorbesitzer: St. Peter Urach; Bartholomaeusstift Frankfurt am Main

Fragm. lat. II 9 - 1. Expositio in Cantica canticorum 2. Theologische Notate

Trägerband: Ms. Barth. 54; Vorbesitzer: Johannes Mushunt de Fulda; Bartholomaeusstift Frankfurt am Main