Entre la política y la academia: una tesis sobre productores tabacaleros

Trataré de presentar una imagen de tus primeros años en la Universidad de Oslo, principalmente en lo concerniente a tu tesis de Magistergrad en Antropología Social, que presentaste en 1978. No recuerdo exactamente cuándo fue que te encontré por primera vez, pero debió ser varios años antes, probablemente a principios de los 1970s. En ese entonces me acababan de tomar como University Lecturer en el Departamento, y tú acababas de regresar después de varios años en el exterior y habías empezado tus estudios en Antropología Social. No me acuerdo en qué momento de la Carrera estabas cuando nos conocimos, y si ya habías empezado tus estudios de posgrado. Esto se me fue por completo, probablemente porque fue en los 70s, una época oportuna para el compromiso político profundo y para la crítica del programa tradicional y de los cursos del Departamento. Era un tiempo en que los estudios y la política y la sociabilidad general estaban estrechamente unidas, y nosotros, que por aquella época pertenecíamos a la extrema izquierda, pasábamos el tiempo en continuos debates acerca de absolutamente todo, y el tema de quién se recibía cuándo y con qué exámenes eran cuestiones totalmente subordinadas a todas esas cosas que nos involucraban

The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families

AbstractThree of the original Norwegian lecithin:cholesterol acyltransferase (LCAT) deficiency families have been investigated for mutations in the gene for lecithin:cholesterol acyltransferase by DNA sequencing of the exons amplified by the polymerase chain reaction. A single T→A transversion in codon 252 in exon 6 converting Met(ATG) to Lys(AAG) was observed in all homozygotes. In spite of the identical mutation, the disease phenotypes differed in severity. This was not reflected in the expression of LCAT in the heterozygotes

New Family Cultures: Gendered Intimacy Forms and Life Project in Reshaping, 2013

The project addresses the challenges and opportunities of the meeting between the equality project of the Nordic welfare model and new and more culturally complex, family and lifestyles in Norway today. This is done by examining how gendered relationships are formed and transformed into two new groups - both of which can be regarded as central norm carriers and agents of change within the current gender discourse: i) Families who represent a growing and culturally influential cosmopolitan middle class and ii) the descendants of first generation immigrants with higher education who thus can be considered as part of an emerging middle class among minority groups. The empirical study will be based on narrative in-depth interviews in combination with participant observation. For further information about ”New Family Cultures: Gendered Intimacy Forms and Life Project in Reshaping, 2013”, please contact the principal investigator

PSKH1, a novel splice factor compartment-associated serine kinase

Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP splicing factors containing a serine/arginine-rich domain (SR proteins) concentrate in splicing factor compartments (SFCs) within the nucleus of interphase cells. Nuclear SFCs are considered mainly as storage sites for splicing factors, supplying splicing factors to active genes. The mechanisms controlling the interaction of the various spliceosome constituents, and the dynamic nature of the SFCs, are still poorly understood. We show here that endogenous PSKH1, a previously cloned kinase, is located in SFCs. Migration of PSKH1-FLAG into SFCs is enhanced during co-expression of T7-tagged ASF/SF2 as well as other members of the SR protein family, but not by two other non-SR nuclear proteins serving as controls. Similar to the SR protein kinase family, overexpression of PSKH1 led to reorganization of co-expressed T7-SC35 and T7-ASF/SF2 into a more diffuse nuclear pattern. This redistribution was not dependent on PSKH1 kinase activity. Different from the SR protein kinases, the SFC-associating features of PSKH1 were located within its catalytic kinase domain and within its C-terminus. Although no direct interaction was observed between PSKH1 and any of the SR proteins tested in pull-down or yeast two-hybrid assays, forced expression of PSKH1-FLAG was shown to stimulate distal splicing of an E1A minigene in HeLa cells. Moreover, a GST-ASF/SF2 fusion was not phosphorylated by PSKH1, suggesting an indirect mechanism of action on SR proteins. Our data suggest a mutual relationship between PSKH1 and SR proteins, as they are able to target PSKH1 into SFCs, while forced PSKH1 expression modulates nuclear dynamics and the function of co-expressed splicing factors