932 resultados para INTERPERSONAL RELATIONSHIPS


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The vocalizations of Hypsiboas ericae (Caramaschi & Cruz, 2000) are described and new information on the external morphology and osteology of the species are presented. H. ericae presents a bony spine in the prepolex and the individuals can present green or brown dorsal color, as other species of the Hypsiboas pulchellus (Duméril & Bibron, 1841) species group. The vocalizations of H. ericae are similar to the vocalizations of Hypsiboas bischoffi (Boulenger, 1887), Hypsiboas guentheri (Boulenger, 1886), and other species in the H. polytaenius (Cope, 1870 "1869") clade of the H. pulchellus species group, but some osteological aspects are different to those found in the majority of the species of this group.

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The diet and trophic relationships between the macroinvertebrates Phyllogomphoides joaquini Rodrigues Capítulo, 1992 and Coenagrionidae (Odonata), Chironomidae (Diptera), Diplodon delodontus (Lamarck, 1919) (Bivalvia: Hyriidae), and Pomacea canaliculata (Lamarck, 1822) (Gastropoda: Ampulariidae) and the fishes Pimelodella laticeps Eigenmann, 1917 (Heptapteridae) and Bryconamericus iheringii (Boulenger, 1887) (Characidae) in a temperate lowland lotic system in Argentina were assessed on the basis of gut contents and stable-isotope analyses. The feeding strategies were analyzed by the AMUNDSEN method. Relative food items contribution for the taxa studied indicated a generalist-type trophic strategy. In macroinvertebrates, in general, the values of stable isotope confirmed the result of the analysis of gut contents. With the fish, stable-isotope analysis demonstrated that both species are predators, although B. iheringii exhibited a more omnivorous behaviour. These feeding studies allowed us to determine the trophic relationships among taxa studied. Detritus and diatoms were a principal source of food for all the macroinvertebrates studied. In La Choza stream the particulate organic matter is a major no limited food resource, has a significant influence upon the community.

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The alpha1b-adrenergic receptor (AR) is a member of the large superfamily of seven transmembrane domain (TMD) G protein-coupled receptors (GPCR). Combining site-directed mutagenesis of the alpha1b-AR with computational simulations of receptor dynamics, we have explored the conformational changes underlying the process of receptor activation, i.e. the transition between the inactive and active states. Our findings suggest that the structural constraint stabilizing the alpha1b-AR in the inactive form is a network of H-bonding interactions amongst conserved residues forming a polar pocket and R143 of the DRY sequence at the end of TMDIII. We have recently reported that point mutations of D142, of the DRY sequence and of A293 in the distal portion of the third intracellular loop resulted in ligand-independent (constitutive) activation of the alpha1b-AR. These constitutively activating mutations could induce perturbations resulting in the shift of R143 out of the polar pocket. The main role of R143 may be to mediate receptor activation by triggering the exposure of several basic amino acids of the intracellular loops towards the G protein. Our investigation has been extended also to the biochemical events involved in the desensitization process of alpha1b-AR. Our results indicate that immediately following agonist-induced activation, the alpha1b-AR can undergo rapid agonist-induced phosphorylation and desensitization. Different members of the G protein coupled receptor kinase family can play a role in agonist-induced regulation of the alpha1b-AR. In addition, constitutively active alpha1b-AR mutants display different phosphorylation and internalization features. The future goal is to further elucidate the molecular mechanism underlying the complex equilibrium between activation and inactivation of the alpha1b-AR and its regulation by pharmacological substances. These findings can help to elucidate the mechanism of action of various agents displaying properties of agonists or inverse agonists at the adrenergic system.

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Receptors for interleukin 2 (IL-2) esit in at least three forms which differ in their subunit compositio, their affinity for ligand and their ability to mediate a cellular reponse. Type I receptors occur following cellular acitivation and consist of the 55,000 m. w. glycoprotein Tac. These receptors bind IL-2 with a low affinity, do not internalize ligand and have not been definitively associated with any response. Type II receptors, on the other hand, conssit of one or more glycoproteins of 70,000 m. w. which have been termed "beta ([beta]) chains." They bind IL-2 with an intermediate affinity and rapidly internalize the ligand. [Beta] proteins mediate many cellular IL-2-dependent reponses, including the short-term activation of natural killer cells and the induction of Tac protein expression. Type III receptors consist of a ternary complex of the Tac protein, the [beta] chain(s) and IL-2. They are characterized by a paricularly high affinity for ligand association. Type III receptors also internalize ligand and mediate IL-2-dependent responses at low factor concentrations. The identification of two independent IL-2-binding molecules, Tac and [beta], thus provides the elusive molecular explanation for the differences in IL-2 receptor affinity and suggests the potential for selective therapeutic manipulation of IL-2 reponses.