ABSTRACT
Recent evidence suggests potential associations between birthweight and disease in later life. For resource or other reasons recorded birthweight may be unavailable to researchers who have access to uniquely relevant outcome data. The present study examined the validity of parental recall of birthweight. Parents of 1015 males and females aged 12 and 15 years participating in the Young Hearts Study (a cluster random sample of 1015 males and females aged 12 and 15 years from post-primary schools in Northern Ireland) completed a questionnaire which included a question about their child's birthweight. The answer provided was compared with recorded birthweight obtained from archived computerised child health records with a cut-off point for inaccurate reporting set at +/- 227 g (1/2 lb). The influence of social class and weight at birth on accuracy of recall was also determined. A total of 84.8% of parents accurately recalled their child's birthweight to within 227 g. Parents from non-manual occupation social classes recalled birthweight more accurately than those from manual occupation social classes (88.0 vs. 82.6% accurate: chi2 = 4.81, p = 0.03). Parents of low birthweight infants tended to recall their birthweight less accurately than parents of normal weight infants: 76.1% accurate compared to 86.1% accurate: chi2 = 3.54, p = 0.06. Parents of high birthweight infants recalled their birthweight less accurately than parents of normal weight infants: 78.5% accurate: chi2 = 3.94, p = 0.05. In conclusion, parentally recalled birthweight may be a suitable proxy for recorded birthweight for population based research into disease in childhood and adolescence.
Subject(s)
Birth Weight , Mental Recall/classification , Parents/psychology , Adolescent , Cardiovascular Diseases/epidemiology , Child , Epidemiologic Studies , Female , Humans , Male , Northern Ireland/epidemiology , Occupations/classification , Risk Factors , Social Class , Surveys and Questionnaires , Time FactorsABSTRACT
Glutamine synthetase (E.C. 6.3.1.2) is expressed throughout the body and plays an important role in controlling body pH and in removing ammonia from the circulation. The enzyme clears L-glutamate, the major neurotransmitter in the central nervous system, from neuronal synapses. The enzyme is a very sensitive marker of many disease and aging processes, especially those involving reactive oxygen species. This report describes the localization of the enzyme to chromosome 1 by PCR analysis of a human/rodent somatic cell hybrid panel. We also describe the localization of a recently described pseudogene to chromosome 9. Further localization of the glutamine synthetase gene locus to 1q23 was accomplished by fluorescence in situ hybridization. The glutamine synthetase gene was mapped to five CEPH megaYACs between the polymorphic PCR markers D1S117 and D1S466 by analysis of the Whitehead Institute's recently described chromosome 1 contig map.
Subject(s)
Chromosomes, Human, Pair 1/genetics , Genes , Glutamate-Ammonia Ligase/genetics , Animals , Chromosome Mapping , Humans , Hybrid Cells , In Situ Hybridization, Fluorescence , Mice , Polymerase Chain Reaction , PseudogenesABSTRACT
5'-Phosphoribosyl N-formylglycinamide (FGAR) amidotransferase (EC 6.3.5.3) catalyzes the fourth reaction in the de novo synthesis of purines, that is, the conversion of FGAR to 5'-phosphoribosyl N-formylglycinamidine (FGAM). This is the only step of the pathway for which a vertebrate gene has not been cloned. FGAR amidotransferase has been highly purified from Chinese hamster ovary (CHO) cells, and this preparation has been used to generate monoclonal antibodies in mice. Two of these antibodies, designated BD4 and DD2, have been shown to recognize a 150-kDa protein in CHO-K1 cells that is of very low abundance in Ade-B cells, a CHO line in which FGAR amidotransferase activity is undetectable. Furthermore, the protein recognized by these antibodies is 5-10-fold more abundant in Azr cells. The CHO Azr cell line was made resistant to azaserine, a potent inhibitor of FGAR amidotransferase, and displays a 5-10-fold increase in FGAR amidotransferase activity over the parental K1 line. FGAR amidotransferase activity and the 150-kDa protein recognized by both monoclonal antibodies were found to immunoprecipitate concomitantly using antibody BD4. Monoclonal antibody DD2 cross-reacted with a human protein of identical molecular mass. A number of Ade-B/human hybrid cells were generated by somatic cell fusion and subsequent 5-bromo-2-deoxyuridine segregation. Analysis of these lines, together with two independently generated human/mouse hybrid cell lines, by both cytogenetics and immunoblotting with antibody DD2 revealed that the human FGAR amidotransferase gene is located on chromosome 17p.
