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1.
Salud colect ; 10(3): 313-323, sep.-dic. 2014.
Article in Spanish | LILACS | ID: lil-733292

ABSTRACT

El objetivo de este trabajo es estudiar, desde una perspectiva feminista, la diversidad y homogeneidad en las trayectorias profesionales de las médicas de familia que ejercían en Andalucía a comienzos del siglo XXI, a través del análisis de los significados que ellas mismas confieren a su desarrollo profesional y de la influencia de los factores personales, familiares y laborales. Realizamos un estudio cualitativo con seis grupos de discusión. Participaron 32 médicas de familia que se encontraban trabajando en los centros de salud urbanos de la red sanitaria pública de Andalucía. El análisis del discurso revela que la mayoría de las médicas no planifican sus metas profesionales y que, cuando lo hacen, las van entrelazando con las necesidades familiares. Esto se traduce en que sus trayectorias profesionales sean discontinuas. Por el contrario, las trayectorias orientadas al desarrollo profesional y a la planificación consciente de metas son más frecuentes entre las médicas que ocupan cargos de dirección en centros de salud.


The purpose of this article was to study, from a feminist perspective, the diversity and homogeneity in the career paths of female primary care physicians from Andalusia, Spain in the early 21st century, by analyzing the meanings they give to their careers and the influence of personal, family and professional factors. We conducted a qualitative study with six discussion groups. Thirty-two female primary care physicians working in urban health centers of the public health system of Andalusia participated in the study. The discourse analysis revealed that most of the female physicians did not plan for professional goals and, when they did plan for them, the goals were intertwined with family needs. Consequently, their career paths were discontinuous. In contrast, career paths oriented towards professional development and the conscious planning of goals were more common among the female doctors acting as directors of health care centers.


Subject(s)
Humans , Ferric Compounds/chemistry , Ferrous Compounds/chemistry , Iron/chemistry , Sarcosine/analogs & derivatives , tau Proteins/chemistry , Aluminum/chemistry , Brain Chemistry , Chlorides , Immunoblotting , Macromolecular Substances , Phosphates/chemistry , Phosphorylation , Protein Binding/physiology , Reducing Agents/chemistry , Sarcosine/chemistry
2.
Experimental & Molecular Medicine ; : e29-2013.
Article in English | WPRIM | ID: wpr-74491

ABSTRACT

O-linked N-acetylglucosamine (O-GlcNAc) represents a key regulatory post-translational modification (PTM) that is reversible and often reciprocal with phosphorylation of serine and threonine at the same or nearby residues. Although recent technical advances in O-GlcNAc site-mapping methods combined with mass spectrometry (MS) techniques have facilitated study of the fundamental roles of O-GlcNAcylation in cellular processes, an efficient technique for examining the dynamic, reciprocal relationships between O-GlcNAcylation and phosphorylation is needed to provide greater insights into the regulatory functions of O-GlcNAcylation. Here, we describe a strategy for selectively identifying both O-GlcNAc- and phospho-modified sites. This strategy involves metal affinity separation of O-GlcNAcylated and phosphorylated peptides, beta-elimination of O-GlcNAcyl or phosphoryl functional groups from the separated peptides followed by dithiothreitol (DTT) conjugation (BEMAD), affinity purification of DTT-conjugated peptides using thiol affinity chromatography, and identification of formerly O-GlcNAcylated or phosphorylated peptides by MS. The combined metal affinity separation and BEMAD approach allows selective enrichment of O-GlcNAcylated peptides over phosphorylated counterparts. Using this approach with mouse brain synaptosomes, we identified the serine residue at 605 of the synapsin-1 peptide, 603QASQAGPGPR612, and the serine residue at 692 of the tau peptide, 688SPVVSGDTSPR698, which were found to be potential reciprocal O-GlcNAcylation and phosphorylation sites. These results demonstrate that our strategy enables mapping of the reciprocal site occupancy of O-GlcNAcylation and phosphorylation of proteins, which permits the assessment of cross-talk between these two PTMs and their regulatory roles.


Subject(s)
Animals , Mice , Acetylglucosamine/metabolism , Amino Acid Sequence , Brain/metabolism , Chromatography, Affinity , Glycosylation , Molecular Sequence Data , Peptides/isolation & purification , Phosphorylation , Synapsins/chemistry , Synaptosomes/metabolism , Tandem Mass Spectrometry , tau Proteins/chemistry
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