[Prevalence of anorexia nervosa, bulimia nervosa and other eating disorders in adolescent girls in Reus (Spain)]. / Prevalencia de anorexia nerviosa, bulimia nerviosa y otros TCA en adolescentes femeninas de Reus.

INTRODUCTION: Eating disorders are characterized by changes in eating patterns associated with a series of psychosocial conflicts, low self-esteem and poor empathy, and an obsession with slimming. OBJECTIVES: The aims of the present study were: 1. To determinate the prevalence of anorexia nervosa, bulimia nervosa and other eating disorders in a representative sample of adolescent girls between the ages of 12 and 21 living in the city of Reus (Spain). 2. To evaluate the association between eating disorders and alterations on the Eating Attitudes Test-40 (EAT-40), Body Attitudes Test (BAT), and the Aesthetic Body Shape Questionnaire (CIMEC). MATERIAL AND METHOD: We performed a cross-sectional observational study in a random sample of adolescent girls aged between 12 and 21 years old. Information was gathered from a structured questionnaire on demographic and anthropometric factors (age, place of birth, education, etc.), clinical examination, clinical interview, DMS-IV diagnostic criteria, and three self-administered tests: EAT-40, BAT and CIMEC. RESULTS: A total of 551 adolescents were analyzed. The mean age was 17.6+/-2.5 years. Diagnostic criteria of anorexia nervosa were found in 0.9% (95% CI: 0.4-2.4), bulimia nervosa in 2.9% (95% CI: 1.7-4.7), and other eating disorders in 5.3% (95% CI: 3.6-7.5). The test showing the greatest alterations was the CIMEC (38%), followed by the BAT (27.1%) and EAT-40 (23.1%). All the adolescents that met the diagnostic criteria of anorexia nervosa showed alterations in all three tests. CONCLUSIONS: The high prevalence of eating disorders indicates the need for greater direct involvement among health professionals. The EAT-40, BAT and CIMEC are effective screening instruments for these disorders.

CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes.

Evidence is presented showing that a protein tyrosine phosphatase different from CD45 is present on the membrane of human hematopoietic cells. The molecule recognized by the monoclonal antibody 143-41, which has been classified as CD148 in the VI International Workshop on Leukocyte Differentiation Antigens, was immunopurified and sequenced. The sequence obtained from N-terminus as well as from two different CNBr-digested peptides showed a close identity with a previously described tyrosine phosphatase named HPTP-eta/DEP-1. CD148 is present on all hematopoietic lineages, being expressed with higher intensity on granulocytes than on monocytes and lymphocytes. Interestingly, whereas it is clearly present on peripheral blood lymphocytes, it is poorly expressed on different lymphoid cell lines of T and B origin. When this protein tyrosine phosphatase was cocrosslinked with CD3, an inhibition of the normally observed calcium mobilization was observed. This inhibition correlates with a decrease in phospholipase C-gamma (PLC-gamma) phosphorylation and is similar to the one observed with CD45. In addition, it is shown that the crosslinking of the CD148 alone is also able to induce an increase in [Ca2+]i. This increase is abolished in the presence of genistein and by cocrosslinking with CD45. These data, together with the induction of tyrosine phosphorylation on several substrates, including PLC-gamma, after CD148 crosslinking, suggest the involvement of a tyrosine kinase-based signaling pathway in this process. In conclusion, the data presented show that CD148 corresponds to a previously described protein tyrosine phosphatase HPTP-eta/DEP-1 and that this molecule is involved in signal transduction in lymphocytes.

CD148, a membrane protein tyrosine phosphatase, is able to induce tyrosine phosphorylation on human lymphocytes.

CD148 is a new cluster of differentiation defined in the VI International Workshop on Leucocyte Differentiation Antigens. It has been identified as the hematopoietic form of a formerly described membrane protein tyrosine phosphatase called HPTP eta/ DEP-1. Previous data have demonstrated that this molecule is able to give rise to [Ca2+]i increase. In the present work we show its capability to induce protein tyrosine phosphorylation in human lymphocytes in spite of its intrinsic protein tyrosine phosphatase activity. The induction of kinase activity suggests the involvement of some protein tyrosine kinase based signaling pathway. The activation of this postulated kinase could be carried out through a direct association or via an adapter molecule.