Decent Work and Burnout: A Profile Study With Academic Personnel.

This research explores the relationship between Decent Work (DW) and Burnout in Portuguese and Brazilian academic personnel. We focus on identifying profiles resulting from the relationship between these variables. Seven hundred twenty-seven participants composed the sample (Portuguese = 334; Brazilian = 393), and data were collected online using the Decent Work Questionnaire (DWQ) and the Personal Burnout subscale from the Copenhagen Burnout Inventory (CBI). Results of multiple linear regressions showed that two DW dimensions were significant and negatively related to Burnout: Fundamental Principles and Values at Work and Adequate Working Time and Workload. We found four profiles by performing a cluster analysis: Low Decent Work; High Decent Work; and two other profiles with DW deficit in at least one DW dimension: Low Fundamental Principles and Values at Work and Low Adequate working time and workload. Moreover, 71% of the total sample showed some decent work deficit. Differences between Burnout and the DW dimensions were analyzed through a MANOVA. In our sample, considering the broad dimensions of DW, Burnout seems to be mainly dependent on the deficit of aspects related to the quality of treatment and interpersonal relationships at work (e.g., perceptions of fairness, participation, non-discrimination) as well as the balance of the workload and the adequacy of the working hours. Interventions aiming at improvements must focus on those two dimensions.

Trabalho digno, satisfação com o trabalho e com a vida em administradores / Decent work, and satisfaction with work and life in managers / Trabajo decente, satisfacción con el trabajo y con la vida en administradores

O presente estudo objetivou avaliar interações entre a percepção do trabalho digno (TD) e a satisfação com o trabalho e com a vida, em uma amostra de administradores brasileiros (N = 292). Para isto, foram aplicados três instrumentos: o Questionário de Trabalho Digno, o Questionário de Satisfação com o Trabalho e a Escala de Satisfação com a Vida. Os resultados encontrados foram três correlações canônicas interpretáveis: a primeira mostra a associação de todas as dimensões do TD com todas as dimensões da satisfação com o trabalho e com a vida; a segunda, evidencia a interação entre a remuneração significativa para o exercício da cidadania e a satisfação com a vida; e a terceira, destaca a associação entre a saúde e segurança com a satisfação com o ambiente físico do trabalho. Os resultados sugerem a relevância do TD na promoção da satisfação com o trabalho e com a vida.

The present study aimed to explore interactions between decent work (DW) perception and satisfaction with work and life, in a sample of Brazilian managers (N = 292). For this, three instruments were applied: The Decent Work Questionnaire, the Work Satisfaction questionnaire and the Satisfaction With Life Scale. The results found were three interpretable canonical correlations: the first shows the association of all DW dimensions with all dimensions of satisfaction with work and life; the second shows the interaction between meaningful remuneration for the exercise of citizenship and satisfaction with life; and the third, highlights the association between health and safety with satisfaction with the physical work environment. The results suggest the relevance of DW in promoting satisfaction with work and life.

El presente estudio tuvo como objetivo evaluar las interacciones entre la percepción del trabajo decente (TD) y la satisfacción con el trabajo y con la vida, en una muestra de administradores brasileños (N = 292). Para eso, se aplicaron tres instrumentos: el Cuestionario de Trabajo Decente, el Cuestionario de Satisfacción Laboral y la Escala de Satisfacción con la Vida. Los resultados encontrados fueron tres correlaciones canónicas interpretables: la primera presenta la asociación de todas las dimensiones del TD con todas las dimensiones de satisfacción con el trabajo y con la vida; la segunda muestra la interacción entre la remuneración significativa para el ejercicio de la ciudadanía y la satisfacción con la vida; y la tercera, destaca la asociación entre salud y seguridad con la satisfacción con el ambiente físico de trabajo. Los resultados sugieren la importancia del TD en la promoción de la satisfacción con el trabajo y la vida.

Decent work, work motivation and psychological capital: An empirical research.

BACKGROUND: The Decent Work (DW) concept, proposed by the International Labour Organization, can be enriched by the contributions of a Work, Organizational and Personnel Psychology (WOPP) perspective. Namely, it would be important to relate DW perceptions to the main concepts in the WOPP realm. Understanding these relations would expand our knowledge of the nomological network of the DW concept and of its practical implications. OBJECTIVE: To analyze the relationships between DW, work motivation and psychological capital among knowledge workers in Portugal and Brazil. METHODS: The Decent Work Questionnaire (DWQ), a previously validated measure of 7 dimensions of DW from a WOPP perspective, the Multidimensional Work Motivation Scale (MWMS), and the Psychological Capital Questionnaire (PCQ) were administered to 2912 knowledge workers. Relations among concepts were analyzed by canonical correlation analyses and linear regression. RESULTS: The DW dimension Fulfilling and Productive Work was positively associated with intrinsic and identified work motivation, and negatively with amotivation. A second significant canonical variate related (negatively) Social Protection (DW dimension) to extrinsic material work motivation. Results from regression analysis support the idea that DW promotes psychological capital. CONCLUSIONS: Results suggest that DW is an important predictor of work motivation and psychological capital. Practical implications for human resources management are presented.

Decent work and work motivation in lawyers: an empirical research / Trabalho digno e motivação para o trabalho em advogados: uma pesquisa empírica / Trabajo decente y motivación para el trabajo de los abogados: una investigación empírica

This study aimed for better understanding of the effect of decent work on work motivation in lawyers in Portugal and Brazil (N = 611). The Decent Work Questionnaire (DWQ) and Multidimensional Work Motivation Scale (MWMS) were applied. The results of analysis of the canonical correlations showed the presence of two operating mechanisms (two significant canonical correlations). They suggest that fulfilling-and-productive-work is associated positively with intrinsic-and-identified-work-motivation and negatively with amotivation. It was also observed that an adequate working-time/workload is negatively associated with material-extrinsic-motivation (such as money). Summarizing, the results suggest that decent work, especially some of its dimensions, has an important role in promoting work motivation through two main mechanisms, the first one called 'worthy working life as part of being a citizen in society' and the second one called 'contextual life comfort and committed effort'. Limitations and practical implications conclude this article.

O presente estudo objetivou uma melhor compreensão dos efeitos do trabalho digno sobre a motivação para o trabalho em advogados de Portugal e do Brasil (N = 611). Foram aplicados o Questionário de Trabalho Digno e a Escala Multidimensional de Motivação para o Trabalho. Os resultados da análise das correlações canônicas evidenciaram dois mecanismos significativos atuantes. Elas sugerem que o trabalho realizante e produtivo está associado positivamente às motivações para o trabalho intrínseca e identificada e negativamente à desmotivação. Adicionalmente, observou-se que um adequado tempo/carga de trabalho se encontra negativamente associado à motivação extrínseca material (como dinheiro). Em resumo, os resultados sugerem que o trabalho digno, especialmente algumas de suas dimensões, tem um papel importante na promoção da motivação para o trabalho através de dois mecanismos principais, designados: 'vida de trabalho digna como parte de ser um cidadão na sociedade' e o segundo 'uma situação de vida confortável e esforços empenhados'. As limitações e implicações práticas concluem este artigo.

El presente estudio objetivó una mejor comprensión de los efectos del trabajo decente sobre la motivación para el trabajo de los abogados de Portugal y Brasil (N = 611). Se aplicaron el Cuestionario-del-Trabajo-Digno y la EscalaMultidimensional-de-Motivación-para-el-Trabajo. Los resultados del análisis de las correlaciones canónicas evidenció la presencia de dos mecanismos actuantes significativos. Estos sugieren que el trabajo-realizante-y-productivo está asociado positivamente a las motivaciones-intrínseca-e-identificada para el trabajo y negativamente a la desmotivación. Adicionalmente, se observó que un tiempo/carga-de-trabajo-adecuado se encuentra negativamente asociado a la motivación-extrínseca-material (como el dinero). En resumen, los resultados sugieren que el trabajo decente, especialmente algunas de sus dimensiones, tienen un papel importante en la promoción de la motivación para el trabajo a través de dos mecanismos principales, llamados: 'vida laboral digna, parte de ser un ciudadano en sociedad' y el segundo 'situación de vida confortable y esfuerzo empeñado'. Las limitaciones e implicaciones prácticas concluyen este artículo.

Design and development of analogues of dimers of insulin-like peptide 3 B-chain as high-affinity antagonists of the RXFP2 receptor.

Insulin-like peptide 3 (INSL3) is one of 10 members of the human relaxin-insulin superfamily of peptides. It is a peptide hormone that is expressed by fetal and postnatal testicular Leydig cells and postnatal ovarian thecal cells. It mediates testicular descent during fetal life and suppresses sperm apoptosis in adult males, whereas, in females, it causes oocyte maturation. INSL3 has also been shown to promote thyroid tumor growth and angiogenesis in human. These actions of INSL3 are mediated through its G protein-coupled receptor, RXFP2. INSL3, a two-chained peptide, binds to its receptor primarily via its B-chain, whereas elements of the A-chain are essential for receptor activation. In an attempt to design a high-affinity antagonist with potential clinical application as an anticancer agent as well as a contraceptive, we have previously prepared a synthetic parallel dimer of INSL3 B-chain and demonstrated that it binds to RXFP2 with high affinity. In this work, we undertook full pharmacological characterization of this peptide and show that it can antaogonize INSL3-mediated cAMP signaling through RXFP2. Further refinement by truncation of 18 residues yielded a minimized analogue that retained full binding affinity and INSL3 antagonism. It is an attractive lead peptide for in vivo evaluation as an inhibitor of male and female fertility and of INSL3-mediated carcinogenesis.

Resolving the unconventional mechanisms underlying RXFP1 and RXFP2 receptor function.

The receptors for relaxin and insulin-like peptide 3 (INSL3) are now well-characterized as the relaxin family peptide (RXFP) receptors RXFP1 and RXFP2, respectively. They are G-protein-coupled receptors (GPCRs) with closest similarity to the glycoprotein hormone receptors, with both containing large ectodomains with 10 leucine-rich repeats (LRRs). Additionally, RXFP1 and RXFP2 are unique in the LGR family in that they contain a low-density lipoprotein class A (LDL-A) module at their N-terminus. Ligand-mediated activation of RXFP1 and RXFP2 is a complex process involving various domains of the receptors. Primary ligand binding occurs via interactions between B-chain residues of the peptides with specific residues in the LRRs of the ectodomain. There is a secondary binding site in the transmembrane exoloops which may interact with the A chain of the peptides. Receptor signaling through cAMP then requires the unique LDL-A module, as receptors without this domain bind ligand normally but do not signal. This is an unconventional mode of activation for a GPCR, and the precise mode of action of the LDL-A module is currently unknown. The specific understanding of the mechanisms underlying ligand-mediated activation of RXFP1 and RXFP2 is crucial in terms of targeting these receptors for future drug development.

The A-chain of human relaxin family peptides has distinct roles in the binding and activation of the different relaxin family peptide receptors.

The relaxin peptides are a family of hormones that share a structural fold characterized by two chains, A and B, that are cross-braced by three disulfide bonds. Relaxins signal through two different classes of G-protein-coupled receptors (GPCRs), leucine-rich repeat-containing GPCRs LGR7 and LGR8 together with GPCR135 and GPCR142, now referred to as the relaxin family peptide (RXFP) receptors 1-4, respectively. Although key binding residues have been identified in the B-chain of the relaxin peptides, the role of the A-chain in their activity is currently unknown. A recent study showed that INSL3 can be truncated at the N terminus of its A-chain by up to 9 residues without affecting the binding affinity to its receptor RXFP2 while becoming a high affinity antagonist. This suggests that the N terminus of the INSL3 A-chain contains residues essential for RXFP2 activation. In this study, we have synthesized A-chain truncated human relaxin-2 and -3 (H2 and H3) relaxin peptides, characterized their structure by both CD and NMR spectroscopy, and tested their binding and cAMP activities on RXFP1, RXFP2, and RXFP3. In stark contrast to INSL3, A-chain-truncated H2 relaxin peptides lost RXFP1 and RXFP2 binding affinity and concurrently cAMP-stimulatory activity. H3 relaxin A-chain-truncated peptides displayed similar properties on RXFP1, highlighting a similar binding mechanism for H2 and H3 relaxin. In contrast, A-chain-truncated H3 relaxin peptides showed identical activity on RXFP3, highlighting that the B-chain is the sole determinant of the H3 relaxin-RXFP3 interaction. Our results provide new insights into the action of relaxins and demonstrate that the role of the A-chain for relaxin activity is both peptide- and receptor-dependent.

Defining the LGR8 residues involved in binding insulin-like peptide 3.

The peptide hormone insulin-like peptide 3 (INSL3) is essential for testicular descent and has been implicated in the control of adult fertility in both sexes. The human INSL3 receptor leucine-rich repeat-containing G protein-coupled receptor 8 (LGR8) binds INSL3 and relaxin with high affinity, whereas the relaxin receptor LGR7 only binds relaxin. LGR7 and LGR8 bind their ligands within the 10 leucine-rich repeats (LRRs) that comprise the majority of their ectodomains. To define the primary INSL3 binding site in LGR8, its LRRs were first modeled on the crystal structure of the Nogo receptor (NgR) and the most likely binding surface identified. Multiple sequence alignment of this surface revealed the presence of seven of the nine residues implicated in relaxin binding to LGR7. Replacement of these residues with alanine caused reduced [(125)I]INSL3 binding, and a specific peptide/receptor interaction point was revealed using competition binding assays with mutant INSL3 peptides. This point was used to crudely dock the solution structure of INSL3 onto the LRR model of LGR8, allowing the prediction of the INSL3 Trp-B27 binding site. This prediction was then validated using mutant INSL3 peptide competition binding assays on LGR8 mutants. Our results indicated that LGR8 Asp-227 was crucial for binding INSL3 Arg-B16, whereas LGR8 Phe-131 and Gln-133 were involved in INSL3 Trp-B27 binding. From these two defined interactions, we predicted the complete INSL3/LGR8 primary binding site, including interactions between INSL3 His-B12 and LGR8 Trp-177, INSL3 Val-B19 and LGR8 Ile-179, and INSL3 Arg-B20 with LGR8 Asp-181 and Glu-229.

Improved chemical synthesis and demonstration of the relaxin receptor binding affinity and biological activity of mouse relaxin.

The primary stored and circulating form of relaxin in humans, human gene-2 (H2) relaxin, has potent antifibrotic properties with rapidly occurring efficacy. However, when administered to experimental models of fibrosis, H2 relaxin can only be applied over short-term (2-4 week) periods, due to rodents mounting an antibody response to the exogenous human relaxin, resulting in delayed clearance and, hence, increased and variable circulating levels. To overcome this problem, the current study investigated the therapeutic potential of mouse relaxin over long-term exposure in vivo. Mouse relaxin is unique among the known relaxins in that it possesses an extra residue within the C-terminal region of its A-chain. To enable a detailed assessment of its receptor interaction and biological properties, it was chemically synthesized in good overall yield by the separate preparation of each of its A- and B-chains followed by regioselective formation of each of the intramolecular and two intermolecular disulfide bonds. Murine relaxin was shown to bind with high affinity to the human, mouse, and rat RXFP1 (primary relaxin) receptor but with a slightly lower affinity to that of H2 relaxin. When administered to relaxin-deficient mice (which undergo an age-dependent progression of organ fibrosis) over a 4 month treatment period, mouse relaxin was able to significantly inhibit the progression of collagen accumulation in several organs including the lung, kidney, testis, and skin (all p < 0.05 vs untreated group), consistent with the actions of H2 relaxin. These combined data demonstrate that mouse relaxin can effectively inhibit collagen deposition and accumulation (fibrosis) over long-term treatment periods.

The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation.

The receptors for the peptide hormones relaxin and insulin-like peptide 3 (INSL3) are the leucine-rich repeat-containing G-protein-coupled receptors LGR7 and LGR8 recently renamed as the relaxin family peptide (RXFP) receptors, RXFP1 and RXFP2, respectively. These receptors differ from other LGRs by the addition of an N-terminal low density lipoprotein receptor class A (LDLa) module and are the only human G-protein-coupled receptors to contain such a domain. Recently it was shown that the LDLa module of the RXFP1 and RXFP2 receptors is essential for ligand-stimulated cAMP signaling. The mechanism by which the LDLa module modulates receptor signaling is unknown; however, it represents a unique paradigm in understanding G-protein-coupled receptor signaling. Here we present the structure of the RXFP1 receptor LDLa module determined by solution NMR spectroscopy. The structure is similar to other LDLa modules but shows small differences in side chain orientations and inter-residue packing. Interchange of the module with the second ligand binding domain of the LDL receptor, LB2, results in a receptor that binds relaxin with full affinity but is unable to signal. Furthermore, we demonstrate via structural studies on mutated LDLa modules and functional studies on mutated full-length receptors that a hydrophobic surface within the N-terminal region of the module is essential for activation of RXFP1 receptor signal in response to relaxin stimulation. This study has highlighted the necessity to understand the structural effects of single amino acid mutations on the LDLa module to fully interpret the effects of these mutations on receptor activity.

Relaxin-3: improved synthesis strategy and demonstration of its high-affinity interaction with the relaxin receptor LGR7 both in vitro and in vivo.

Relaxin-3 is a member of the human relaxin peptide family, the gene for which, RLN3, is predominantly expressed in the brain. Mapping studies in the rodent indicate a highly developed network of RLN3, RLN1, and relaxin receptor-expressing cells in the brain, suggesting that relaxin peptides have important functional roles in the central nervous system. A regioselective disulfide-bond synthesis protocol was developed and used for the chemical synthesis of human (H3) relaxin-3. The selectively S-protected A and B chains were combined by stepwise formation of each of the three insulin-like disulfides via aeration, thioloysis, and iodolysis. Judicious positioning of the three sets of S-protecting groups was crucial for acquisition of synthetic H3 relaxin in a good overall yield. The activity of the peptide was tested against relaxin family peptide receptors. Although the highest activity was demonstrated on the human relaxin-3 receptor (GPCR135), the peptide also showed high activity on relaxin receptors (LGR7) from various species and variable activity on the INSL3 receptor (LGR8). Recombinant mouse prorelaxin-3 demonstrated similar activity to H3 relaxin, suggesting that the presence of the C peptide did not influence the conformation of the active site. H3 relaxin was also able to activate native LGR7 receptors. It stimulated increased MMP-2 expression in LGR7-expressing rat ventricular fibroblasts in a dose-dependent manner and, following infusion into the lateral ventricle of the brain, stimulated water drinking in rats, activating LGR7 receptors located in the subfornical organ. Thus, H3 relaxin is able to interact with the relaxin receptor LGR7 both in vitro and in vivo.

Splice variants of the relaxin and INSL3 receptors reveal unanticipated molecular complexity.

LGR7 and LGR8 are G protein-coupled receptors that belong to the leucine-rich repeat-containing G-protein coupled receptor (LGR) family, including the thyroid-stimulating hormone (TSH), LH and FSH receptors. LGR7 and LGR8 stimulate cAMP production upon binding of the cognate ligands, relaxin and insulin-like peptide 3 (INSL3), respectively. We cloned several novel splice variants of both LGR7 and LGR8 and analysed the function of four variants. LGR7.1 is a truncated receptor, including only the N-terminal region of the receptor and two leucine rich repeats. In contrast, LGR7.2, LGR7.10 and LGR 8.1 all contain an intact seven transmembrane domain and most of the extracellular region, lacking only one or two exons in the ectodomain. Our analysis demonstrates that although LGR7.10 and LGR8.1 are expressed at the cell surface, LGR7.2 is predominantly retained within cells and LGR7.1 is partially secreted. mRNA expression analysis revealed that several variants are co-expressed in various tissues. None of these variants were able to stimulate cAMP production following relaxin or INSL3 treatment. Unexpectedly, we did not detect any direct specific relaxin or INSL3 binding on any of the splice variants. The large number of receptor splice variants identified suggests an unforeseen complexity in the physiology of this novel hormone-receptor system.

Studies on soluble ectodomain proteins of relaxin (LGR7) and insulin 3 (LGR8) receptors.

The ectodomains of both the relaxin (LGR7) and the INSL3 (LGR8) receptors can be expressed on the cell surface using only a single transmembrane domain. These membrane-anchored proteins retain the ability to bind relaxin and can be cleaved from the cell surface. The subsequent LGR7 protein, 7BP, binds relaxin and can act as a functional relaxin antagonist. By contrast, the equivalent LGR8 protein 8BP does not bind relaxin or antagonize LGR8 activity. The 7BP protein has been successfully immobilized onto chemically derivatized surfaces for the capture of relaxin peptides and subsequent identification via SELDI-MS analysis.

The chemistry and biology of human relaxin-3.

A novel member of the human relaxin subclass of the insulin superfamily was recently discovered during a genomics database search and named relaxin-3. Like human relaxin-1 and relaxin-2, relaxin-3 is predicted to consist of a two-chain structure and three disulfide bonds in a disposition identical to that of insulin. To undertake detailed biophysical and biological characterization of the peptide, its chemical synthesis was undertaken. In contrast to human relaxin-1 and relaxin-2, however, relaxin-3 could not be successfully prepared by simple combination of the individual chains, thus necessitating recourse to the use of a regioselective disulfide bond formation strategy. Solid phase synthesis of the separate, selectively S-protected A and B chains followed by their purification and the subsequent stepwise formation of each of the three disulfides led to the successful acquisition of human relaxin-3. Comprehensive chemical characterization confirmed both the correct chain orientation and the integrity of the synthetic product. Relaxin-3 was found to bind to and activate native relaxin receptors in vitro and stimulate water drinking through central relaxin receptors in vivo. Recent studies have demonstrated that relaxin-3 will bind to and activate human LGR7, but not LGR8, in vitro. Secondary structural analysis showed it to adopt a less ordered confirmation than either relaxin-1 or relaxin-2, reflecting the presence in the former of a greater percentage of nonhelical forming amino acids. NMR spectroscopy and simulated annealing calculations were used to determine the three-dimensional structure of relaxin-3 and to identify key structural differences between the human relaxins.

Multiple binding sites revealed by interaction of relaxin family peptides with native and chimeric relaxin family peptide receptors 1 and 2 (LGR7 and LGR8).

Relaxin family peptide 1 (RXFP1) receptor (LGR7) and RXFP2 receptor (LGR8) were recently identified as the receptor targets for H2 relaxin and insulin-like peptide 3 (INSL3), respectively. In this study, we define the pharmacology of these two receptors by using a number of receptor chimeras and relaxin family peptides. We have identified two binding sites on these receptors: one primary, high-affinity site within the ectodomain and a secondary, lower affinity site within the transmembrane region. The primary site was found to dictate receptor binding characteristics, although the lower affinity site also exerts some influence and modulates ligand affinity for the primary site in a manner dependent upon the peptide in question. Not all relaxin peptides were able to bind to the RXFP2 receptor, indicating that the relaxin-RXFP2 receptor interaction is species-specific. INSL3 was found to exhibit characteristics of a partial agonist at the RXFP2 and chimeric RXFP1/2 receptors, with low maximal cAMP responses but high potency in coupling to this pathway. cAMP accumulation studies also revealed that the binding sites couple to cAMP signaling pathways with differing efficiency: the high-affinity site signals with high efficiency, whereas the lower affinity site signals with little to no efficiency. Comparisons between RXFP1, RXFP2, the chimeric receptors, and the truncated receptors revealed that the interaction between receptor sites is critical for optimal ligand binding and signal transduction and that the ectodomain is essential for signaling. Evidence obtained in this study supports a two-stage binding model of receptor activation: binding to the primary site allows a conformational change and interaction with the low-affinity transmembrane site.

H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2.

Leucine-rich repeat-containing, G protein-coupled receptors (LGRs) represent a unique subgroup of G protein-coupled receptors with a large ectodomain. Recent studies demonstrated that relaxin activates two orphan LGRs, LGR7 and LGR8, whereas INSL3/Leydig insulin-like peptide specifically activates LGR8. Human relaxin 3 (H3 relaxin) was recently discovered as a novel ligand for relaxin receptors. Here, we demonstrate that H3 relaxin activates LGR7 but not LGR8. Taking advantage of the overlapping specificity of these three ligands for the two related LGRs, chimeric receptors were generated to elucidate the mechanism of ligand activation of LGR7. Chimeric receptor LGR7/8 with the ectodomain from LGR7 but the transmembrane region from LGR8 maintains responsiveness to relaxin but was less responsive to H3 relaxin based on ligand stimulation of cAMP production. The decreased ligand signaling was accompanied by decreases in the ability of H3 relaxin to compete for (33)P-relaxin binding to the chimeric receptor. However, replacement of the exoloop 2, but not exoloop 1 or 3, of LGR7 to the chimeric LGR7/8 restored ligand binding and receptor-mediated cAMP production. These results suggested that activation of LGR7 by H3 relaxin involves specific binding of the ligand to both the ectodomain and the exoloop 2, thus providing a model with which to understand the molecular basis of ligand signaling for this unique subgroup of G protein-coupled receptors.

Desperticidade no contexto da invéxis / Petifreeness in the existential inversion context

O presente artigo visa expor alguns dados essenciais para a conscin inversora que ambiciona atingir a desperticidade na atual existência. Foram classificados três tipos básicos de condições existenciais: (1) robéxis; (2) pré-desperticidade; e (3) desperticidade. As autoras reúnem exemplos colhidos no cotidiano da comunidade conscienciológica ao longo desta primeira década de invéxis explícita (1992-2002), ressaltando as relações com a busca da desperticidade (AU)

Parapsiquismo no campo consciencioterápico / Parapsychism in the conscientiotherapeutic field

No presente trabalho, discute-se o parapsiquismo enquanto ferramenta imprescindível ao consciencioterapeuta, que possibilita a abordagem integral ao evoluciente, a interação entre as equipes intra e extrafísica e, portanto, o processo consciencioterapêutico. Observa-se que o parapsiquismo dos assistentes é potencializado no campo consciencioterápico em favor do assistido. Apresenta-se breve casuística relativa à questão da reeducação parapsíquica do evoluciente, trabalhada nos atendimentos. Constata-se que a qualificação do consciencioterapeuta passa não só pelo desenvolvimento do parapsiquismo, mas também pela qualificação cosmoética da intenção assistencial (AU)