Clinical intake interviewing: proposing LGB affirmative recommendations

The initial impression a client formulates about the therapist is critical to establishing a deep and meaningful working alliance. The traditional intake interview protocol is fraught with heterocentric biases and heteronormative assumptions, thereby failing to provide an affirming experience for non-heterosexual clients or potentially overlooks issues relevant to competently serve the psychological needs of LGB clients. This dissertation endeavors to respond to the growing need for the clinical application of LGB affirmative approaches. An overview of the following bodies of literature is offered: (a) consequences of heterosexism on the lives of LGB individuals, (b) heterosexism and the field of psychology, (c) perceived competence of therapists treating LGB clients, (d) current practices in working clinically with LGB clients, and (e) intersection of multiple cultural considerations. Based on a synthesis of the literature, feedback from experts in the field, and a critical review of existing intake protocols, preliminary suggestions for engaging in an LGB affirming initial therapeutic experience is offered. 4 major areas of clinical considerations for engaging in an affirmative intake process are discussed: (a) creating an affirming environment, (b) the initial intake process, (c) important considerations specific to members of the LGB community; and (d) therapist competencies. Finally, intake questions for consideration in intake forms or during the course of an intake interview are presented

Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impact on in vitro gastro-duodenal proteolysis

Growing attempts are being made to rationally utilize foods for human health improvement and disease prevention. Milk proteins are well suited for this purpose, since they are widely consumed, offer nutritional benefits and have been shown to be potentially suitable carriers for bioactive ingredients, such as vitamins and nutraceuticals. This work characterizes the interactions between β-lactoglobulin (β-lg) and folic acid (FA) at different load ratio and their functional implications, in terms of colloidal behavior and digestibility. Dynamic light scattering, isothermal titration calorimetery and atomic force microscopy were used to investigate β-lg/FA nano-complexes (mean size < 10 nm) formed at protein:vitamin molar ratio 1:10, whereas three FA molecules were found to be bound to one protein molecule. Colloidal stability tests (3 < pH < 10) revealed that nano-complexes formation improved β-lg dissolution near its isoelectric point and at low pH-values. This was also found to be accompanied by a shift in zeta-potential values at pH = 5 for pure β-lg (0.95 ± 0.09 mV) versus β-lg/FA nano-complexes (−20.13 ± 1.29 mV). SDS-PAGE analysis of digesta, collected from gastric and duodenal in vitro digestion of β-lg and its nano-complexes, revealed no marked alterations in the proteolytic susceptibility of β-lg. The study findings show the interactions of FA and β-lg in the formation of nano-complexes may be harnessed for delivery of FA in clear beverages with minimal effects to the protein's sensitivity to proteolysis.Fil: Perez, Oscar Edgardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: David Birman, Tatyana. Technion - Israel Institute of Technology; IsraelFil: Kesselman, Ellina. Technion - Israel Institute of Technology; IsraelFil: Levi Tal, Sharon. Technion - Israel Institute of Technology; IsraelFil: Lesmes, Uri. Technion - Israel Institute of Technology; Israe

Axin-mediated CKI phosphorylation of β-catenin at Ser 45: a molecular switch for the Wnt pathway

The Wnt pathway controls numerous developmental processes via the β-catenin–TCF/LEF transcription complex. Deregulation of the pathway results in the aberrant accumulation of β-catenin in the nucleus, often leading to cancer. Normally, cytoplasmic β-catenin associates with APC and axin and is continuously phosphorylated by GSK-3β, marking it for proteasomal degradation. Wnt signaling is considered to prevent GSK-3β from phosphorylating β-catenin, thus causing its stabilization. However, the Wnt mechanism of action has not been resolved. Here we study the regulation of β-catenin phosphorylation and degradation by the Wnt pathway. Using mass spectrometry and phosphopeptide-specific antibodies, we show that a complex of axin and casein kinase I (CKI) induces β-catenin phosphorylation at a single site: serine 45 (S45). Immunopurified axin and recombinant CKI phosphorylate β-catenin in vitro at S45; CKI inhibition suppresses this phosphorylation in vivo. CKI phosphorylation creates a priming site for GSK-3β and is both necessary and sufficient to initiate the β-catenin phosphorylation–degradation cascade. Wnt3A signaling and Dvl overexpression suppress S45 phosphorylation, thereby precluding the initiation of the cascade. Thus, a single, CKI-dependent phosphorylation event serves as a molecular switch for the Wnt pathway