Parental bonding and mental health in adolescence

Attachment between parent and child plays a crucial role in the healthy development of the child. Accordingly disturbances in parental bonding will be linked with the development of mental disorders later in life. The present study examines the relationship between parental bonding and mental health in healthy adolescents. Participants were 847 Israeli high school students who completed the Parental Bonding Instrument (PBI), the Brief Symptom Inventory (BSI), the General Well-Being (GWB), the Perceived Social Support (PSS), and the Social Desirability scale (SDS). In general, Israeli adolescents reported more parental care and less control than did Australian adolescents and adults. Female subjects reported more maternal care than did males. Subjects who reported high care and low control (optimal bonding) reported less distress, better general well-being and better social support that did all other groups. In contrast, those who reported low care and high control (affectionless control bonding) had the highest BSI scores and the lowest GWB and PSS scores. These results are in line with Bowlby's theory of attachment. They also show that specific configuration of parental bonding are linked with distress and isolation in adolescents.     

High density lipoprotein conversion mediated by human plasma phospholipid transfer protein

Phospholipid transfer protein (PLTP) was purified from lipoprotein-free human plasma, obtained upon treatment of plasma with dextran sulfate and Ca2+, by employing a series of column chromatography. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified PLTP showed a single main band, corresponding to the molecular mass of 78 kDa. However, isoelectric focusing of the purified preparation gave multiple bands with pI ranging from 4.3 to 5.1, indicative of microheterogeneity. Purified PLTP was shown to possess not only phospholipid transfer activity, but also high density lipoprotein (HDL) conversion activity (Tu, A.-Y., Nishida, H. I., and Nishida, T. (1990), FASEB J. 4, A2148; Jauhiainen, M., Metso, J., Pahlman, R., Blomqvist, S., van Tol, A., and Ehnholm, C. (1993) J. Biol. Chem. 268, 4032-4036). Isolated HDL3 was enlarged to the size of HDL2b upon incubation with purified PLTP for 6 h at 37 degrees C at the PLTP/HDL3 molar ratio of approximately 1:45. Both the HDL conversion and the phosphatidylcholine transfer activities of purified PLTP were effectively inhibited by rabbit anti-PLTP immunoglobulin G. The primary importance of PLTP in the HDL enlargement that occurs in human plasma upon incubation at 37 degrees C was shown by the strong inhibitory effect of the anti-PLTP immunoglobulin G. The process of PLTP-mediated HDL enlargement was accompanied by the release of apoproteins, primarily apoA-I. HDL3 enlargement mediated by PLTP was effectively inhibited by the addition of free fatty acids.     

Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins

Enteropathogenic Escherichia coli (EPEC) secretes at least five proteins. Two of these proteins, EspA and EspB (previously called EaeB), activate signal transduction pathways in host epithelial cells. While the role of the other three proteins (39, 40, and 110 kDa) remains undetermined, secretion of all five proteins is under the control of perA, a known positive regulator of several EPEC virulence factors. On the basis of amino-terminal protein sequence data, we cloned and sequenced the gene which encodes the 110-kDa secreted protein and examined its possible role in EPEC signaling and interaction with epithelial cells. In accordance with the terminology used for espA and espB, we called this gene espC, for EPEC-secreted protein C. We found significant homology between the predicted EspC protein sequence and a family of immunoglobulin A (IgA) protease-like proteins which are widespread among pathogenic bacteria. Members of this protein family are found in avian pathogenic Escherichia coli (Tsh), Haemophilus influenzae (Hap), and Shigella flexneri (SepA). Although these proteins and EspC do not encode IgA protease activity, they have considerable homology with IgA protease from Neisseria gonorrhoeae and H. influenzae and appear to use a export system for secretion. We found that genes homologous to espC also exist in other pathogenic bacteria which cause attaching and effacing lesions, including Hafnia alvei biotype 19982, Citrobacter freundii biotype 4280, and rabbit diarrheagenic E. coli (RDEC-1). Although these strains secrete various proteins similar in molecular size to the proteins secreted by EPEC, we did not detect secretion of a 110-kDa protein by these strains. To examine the possible role of EspC in EPEC interactions with epithelial cells, we constructed a deletion mutant in espC by allelic exchange and characterized the mutant by standard tissue culture assays. We found that EspC is not necessary for mediating EPEC-induced signal transduction in HeLa epithelial cells and does not play a role in adherence or invasion of tissue culture cells.     

Study of correlations in DNA sequences

We present a method for unified statistical analysis of short and long range correlations between various nucleotides in genomic DNA strands. The approach is based on the mutual study of Fourier structure factor spectra and pair correlation functions. The analysis of cross correlations in the different ranges of structural spectra permits identification of the main sources of correlations, namely, the coherent point mutations, coincident periodicities or large scale density variations. The technique for assessment of structural coupling between various genes in the genome is also described.     

The production of interleukin-1 alpha immunoreactivity by human oviductal cells in a coculture system

PURPOSE: The aim of this study was to determine the concentration of interleukin-1 alpha in human embryo culture medium with or without oviductal cell coculture and to correlate the interleukin-1 alpha levels with pregnancy. METHODS: Culture media from 32 in vitro fertilization and embryo transfer cycles were assayed for interleukin-1 alpha by immunoassay technique. Human embryos were cultured in Earles' balanced salt solution supplemented with 15% preovulatory serum (sEBSS) in 16 of these cycles, while embryos in the rest of the cycles were cocultured with human oviductal cells in sEBSS. RESULTS: Both sEBSS and spent sEBSS after embryo culture contained low or undetectable levels of interleukin-1 alpha in the pregnant and nonpregnant cycles. On the other hand, oviductal cells significantly increased the amount of interleukin-1 alpha immunoreactivity in the conventional culture medium or coculture medium (P < 0.001, Mann-Whitney rank sum test). The concentrations of interleukin-1 alpha in the spent sEBSS after oviductal cell culture and after coculture with human embryos were 1.5 +/- 1.0 and 1.3 +/- 0.9 pg/ml, respectively. There was no difference in the interleukin-1 alpha concentration between the pregnant and the nonpregnant coculture cycles. CONCLUSIONS: These data showed that human oviductal cells produced interleukin-1 alpha immunoreactivity in a coculture system. However, this production could not be used as a marker for successful embryo implantation.