The philosophical anthropology of Interculturality: a vehicle for creating inclusive identities and positive peace

This chapter illustrates how a philosophical anthropology of interculturality can be the vehicle of higher level social, political, and ethical identities. It explores interculturality as a dynamic and inclusive model for the encounter with cultural, ethnic, national, and religious difference. Anthropology offers cross-cultural perspectives on social behavior and moral learning regarding the management of conflict. Anthropology, with its vast documentation of indigenous societies, past and present, including descriptions of nonviolent modes of conflict resolution, approaches to peacemaking, and creation of peace systems, provides a pool of knowledge about successful approaches to creating and maintaining interculturality, for example, with propeace values and inclusive identities.Este capítulo refleja cómo una filosofía antropológica de la interculturalidad puede ser la herramienta de identidades de un mayor nivel social, político y ético. El texto explora la interculturalidad como modelo dinámico y participativo en su encuentro con diferencias culturales, étnicas, nacionales y religiosas. La Antropología ofrece perspectivas interculturales sobre comportamiento social y aprendizaje moral con respecto al manejo del conflicto. Así mismo, con su amplia información sobre sociedades indígenas, pasadas y presentes, la antropología incluye descripciones de modalidades no violentas de resolución de conflictos, acercamientos a la Paz y a la creación de sistemas de paz, y proporciona un acervo de conocimientos sobre métodos eficaces a la hora de crear y mantener la interculturalidad, por ejemplo, con valores pro-paz e identidades participativas

The Original Partnership Societies: Evolved Propensities for Equality, Prosociality, and Peace

This article focuses on what nomadic forager research suggests about human nature and examines how this ancestral form of human social organization is fundamentally partnership-oriented. Taking mobile forager social organization into consideration is important to partnership studies because all humanity lived as mobile foragers until very recently. The material considered in this article stems from 1) individual forager ethnographies, 2) qualitative comparative forager studies, and 3) research based on systematically sampled forager traits. The findings show the pervasiveness of egalitarianism (including gender equality), socialization and social control mechanism geared toward promoting prosocial behaviors such as sharing and the caring for others, conflict avoidance and resolution mechanisms, and no inclination toward warfare in values or practice. Such patterns that cut across nomadic forager societies from around the world call into question a familiar narrative about the supposedly self-centered, warlike, and hording nature of humanity. Mobile forager studies support an alternative narrative that challenges assumptions about the ‘'primitive versus civilized,’ normative progress and modernity, and biased projections of innate depravity onto all humanity. The article concludes by proposing that our nomadic forager forbearers solved the challenges of survival over evolutionary time not by making war, developing slavery, or ranking people into domination hierarchies of ‘haves’” and ‘have nots’—social institutions with which we are all too familiar today—but rather, our mobile forager ancestors promoted egalitarianism, cooperation, caring and sharing as they developed ways to resolve disputes with a minimum of bloodshed and sidestepped the development of war

Biochemical and aggregation analysis of Bence Jones proteins from different light chain diseases

Deposition of immunoglobulin light chains is a result of clonal proliferation of monoclonal plasma cells that secrete free immunoglobulin light chains, also called Bence Jones proteins (Bence Jones proteins). These Bence Jones proteins are present in circulation in large amounts and excreted in urine in various light chain diseases such as light chain amyloidosis (AL), light chain deposition disease (LCDD) and multiple myeloma (MM). BJP from patients with AL, LCDD and MM were purified from their urine and studies were performed to determine their secondary structure, thermodynamic stability and aggregate formation kinetics. Our results show that LCDD and MM proteins have the lowest free energy of folding while all proteins show similar melting temperatures. Incubation of the BJP at their melting temperature produced morphologically different aggregates: amyloid fibrils from the AL proteins, amorphous aggregates from the LCDD proteins and large spherical species from the MM proteins. The aggregates formed under in vitro conditions suggested that the various proteins derived from patients with different light chain diseases might follow different aggregation pathways

Association between psoas abscess and prosthetic hip infection: a case-control study

Background and purpose The relationship between prosthetic hip infection and a psoas abscess is poorly documented. We determined the frequency of prosthetic hip infections associated with psoas abscesses and identified their determinants

In Vitro Aggregation Behavior of a Non-Amyloidogenic λ Light Chain Dimer Deriving from U266 Multiple Myeloma Cells

Excessive production of monoclonal light chains due to multiple myeloma can induce aggregation-related disorders, such as light chain amyloidosis (AL) and light chain deposition diseases (LCDD). In this work, we produce a non-amyloidogenic IgE λ light chain dimer from human mammalian cells U266, which originated from a patient suffering from multiple myeloma, and we investigate the effect of several physicochemical parameters on the in vitro stability of this protein. The dimer is stable in physiological conditions and aggregation is observed only when strong denaturating conditions are applied (acidic pH with salt at large concentration or heating at melting temperature Tm at pH 7.4). The produced aggregates are spherical, amorphous oligomers. Despite the larger β-sheet content of such oligomers with respect to the native state, they do not bind Congo Red or ThT. The impossibility to obtain fibrils from the light chain dimer suggests that the occurrence of amyloidosis in patients requires the presence of the light chain fragment in the monomer form, while dimer can form only amorphous oligomers or amorphous deposits. No aggregation is observed after denaturant addition at pH 7.4 or at pH 2.0 with low salt concentration, indicating that not a generic unfolding but specific conformational changes are necessary to trigger aggregation. A specific anion effect in increasing the aggregation rate at pH 2.0 is observed according to the following order: SO4−≫Cl−>H2PO4−, confirming the peculiar role of sulfate in promoting protein aggregation. It is found that, at least for the investigated case, the mechanism of the sulfate effect is related to protein secondary structure changes induced by anion binding

An in vivo study of the host response to starch-based polymers and composites subcutaneously implanted in rats

Implant failure is one of the major concerns in the biomaterials field. Several factors have been related to the fail but in general these biomaterials do not exhibit comparable physical, chemical or biological properties to natural tissues and ultimately, these devices can lead to chronic inflammation and foreign-body reactions. Starch-based biodegradable materials and composites have shown promising properties for a wide range of biomedical applications as well as a reduced capacity to elicit a strong reaction from immune system cells in vitro. In this work, blends of corn starch with ethylene vinyl alcohol (SEVA-C), cellulose acetate (SCA) and polycaprolactone (SPCL), as well as hydroxyapatite (HA) reinforced starch-based composites, were investigated in vivo. The aim of the work was to assess the host response evoked for starch-based biomaterials, identifying the presence of key cell types. The tissues surrounding the implant were harvested together with the material and processed histologically for evaluation using immunohistochemistry. At implant retrieval there was no cellular exudate around the implants and no macroscopic signs of an inflammatory reaction in any of the animals. The histological analysis of the sectioned interface tissue after immunohistochemical staining using ED1, ED2, CD54, MHC class II and a/b antibodies showed positively stained cells for all antibodies, except for a/b for all the implantation periods, where it was different for the various polymers and for the period of implantation. SPCL and SCA composites were the materials that stimulated the greatest cellular tissue responses, but generally biodegradable starch-based materials did not induce a severe reaction for the studied implantation times, which contrasts with other types of degradable polymeric biomaterials.Fundação para a Ciência e a Tecnologia (FCT

Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils

The assembly of soluble proteins into ordered fibrillar aggregates with cross-β structure is an essential event of many human diseases. The polypeptides undergoing aggregation are generally small in size. To explore if the small size is a primary determinant for the formation of amyloids under pathological conditions we have created two databases of proteins, forming amyloid-related and non-amyloid deposits in human diseases, respectively. The size distributions of the two protein populations are well separated, with the systems forming non-amyloid deposits appearing significantly larger. We have then investigated the propensity of the 486-residue hexokinase-B from Saccharomyces cerevisiae (YHKB) to form amyloid-like fibrils in vitro. This size is intermediate between the size distributions of amyloid and non-amyloid forming proteins. Aggregation was induced under conditions known to be most effective for amyloid formation by normally globular proteins: (i) low pH with salts, (ii) pH 5.5 with trifluoroethanol. In both situations YHKB aggregated very rapidly into species with significant β-sheet structure, as detected using circular dichroism and X-ray diffraction, but a weak Thioflavin T and Congo red binding. Moreover, atomic force microscopy indicated a morphology distinct from typical amyloid fibrils. Both types of aggregates were cytotoxic to human neuroblastoma cells, as indicated by the MTT assay. This analysis indicates that large proteins have a high tendency to form toxic aggregates, but low propensity to form regular amyloid in vivo and that such a behavior is intrinsically determined by the size of the protein, as suggested by the in vitro analysis of our sample protein

Molecular Structure of Amyloid Fibrils Controls the Relationship between Fibrillar Size and Toxicity

According to the prevailing view, soluble oligomers or small fibrillar fragments are considered to be the most toxic species in prion diseases. To test this hypothesis, two conformationally different amyloid states were produced from the same highly pure recombinant full-length prion protein (rPrP). The cytotoxic potential of intact fibrils and fibrillar fragments generated by sonication from these two states was tested using cultured cells.For one amyloid state, fibril fragmentation was found to enhance its cytotoxic potential, whereas for another amyloid state formed within the same amino acid sequence, the fragmented fibrils were found to be substantially less toxic than the intact fibrils. Consistent with the previous studies, the toxic effects were more pronounced for cell cultures expressing normal isoform of the prion protein (PrP(C)) at high levels confirming that cytotoxicity was in part PrP(C)-dependent. Silencing of PrP(C) expression by small hairpin RNAs designed to silence expression of human PrP(C) (shRNA-PrP(C)) diminished the deleterious effects of the two amyloid states to a different extent, suggesting that the role of PrP(C)-mediated and PrP(C)-independent mechanisms depends on the structure of the aggregates.This work provides a direct illustration that the relationship between an amyloid's physical dimension and its toxic potential is not unidirectional but is controlled by the molecular structure of prion protein (PrP) molecules within aggregated states. Depending on the structure, a decrease in size of amyloid fibrils can either enhance or abolish their cytotoxic effect. Regardless of the molecular structure or size of PrP aggregates, silencing of PrP(C) expression can be exploited to reduce their deleterious effects