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Biomedical subjects

M Clinton

Publications and source records attributed to M Clinton.

At least 55 records · Page 3Linked to original sources

Perceptions of stressors and reported coping strategies in nurses caring for residents with Alzheimer's disease in a dementia unit.

A study was undertaken on the perceptions of stressors and coping behaviours in a group of nurses caring for residents with Alzheimer's disease in a dementia unit. The purpose of this paper is to report on the preliminary findings of the study. Repertory grid data were used to explore how nurses perceive residents, the stressors nurses experience in their work, and the coping strategies nurses use when caring for residents. The nurses identified 92 sources of stress, 683 coping behaviours and 708 coping strategies. Analyses of selected repertory grid data are presented and the stressors reported by the nurses are summarized. The coping strategies the nurses report using are classified into categories of adaptive and maladaptive responses to stress. In addition, the nursing implications of the coping strategies used by the nurses are also considered.

Adaptation, Psychological↗

A rapid protocol for sexing chick embryos (Gallus g. domesticus).

A method for establishing the sex of chick embryos before the appearance or morphological differences between males and females has been developed. DNA was isolated from 5-7-day-old embryos by proteinase K digestion and subjected to polymerase chain reaction (PCR) amplification with W-chromosome specific primers. Sexing can be achieved within 1 day using as little as 1 ng template DNA.

Animals↗

Prothymosin alpha gene in humans: organization of its promoter region and localization to chromosome 2.

A genomic clone encoding prothymosin alpha (gene symbol: PTMA), a nuclear-targeted protein associated with cell proliferation, was isolated and the 5'-regulatory region subcloned and sequenced. Because of previously reported discrepancies between several cDNA clones and a genomic clone for prothymosin alpha, we determined the sequence of the first exon and of a 1.7-kb region 5' to the first exon. The sequence of the genomic clone reported here corresponds to the published cDNA sequences, suggesting that the previously noted discrepancies may be due to genetic polymorphism in this region. In addition, our sequence data extend the known 5'-upstream sequence by an additional 1.5 kb allowing the identification of numerous, potential cis-acting regulatory sites. This 5'-flanking cloned probe permitted us to localize the prothymosin gene to chromosome 2 in humans.

Base Sequence↗

Evidence for nuclear targeting of prothymosin and parathymosin synthesized in situ.

To test the hypothesis that prothymosin and parathymosin contain amino acid sequences that cause them to be targeted to the cell nucleus, expression vectors were constructed containing a simian virus 40 promoter and cDNAs that would code for chimeric proteins composed of truncated human growth hormone (hGH) linked to the NH2 terminus of prothymosin or parathymosin. The truncated hGH lacked the signal peptide sequence required for its secretion. After transfection of these constructs into HeLa S3 cells, which do not normally synthesize hGH, the use of indirect immunofluorescence staining to follow the localization of the hGH chimeras demonstrated that both prothymosin and parathymosin caused targeting to the cell nucleus. Controls with a construct coding for native hGH only, and one coding for the truncated hGH lacking the signal peptide, revealed secretion into culture medium and staining in the endoplasmic reticulum and Golgi apparatus in the first case, and diffuse staining throughout the cytoplasm in the second. The results provide direct evidence, with proteins synthesized in situ, for the presence of nuclear localization signals in both prothymosin and parathymosin.

Base Sequence↗

Prothymosin alpha and parathymosin: mRNA and polypeptide levels in rodent tissues.

Blot hybridization analyses have established the presence of mRNAs for prothymosin alpha (ProT alpha) and for parathymosin (ParaT) in rat and mouse lung, liver, kidney, and brain, confirming the biosynthesis of these peptides in nonlymphoid tissues. In these tissues the levels of mRNAs paralleled the content of the polypeptides, determined with specific radioimmunoassays. The mRNA levels also confirmed the reciprocal relation between the two polypeptides; ProT alpha and its mRNA were found in highest concentrations in spleen and thymus, followed by lung, kidney, and brain, with lowest concentrations in liver. On the other hand, liver contained highest concentrations of ParaT and the mRNA for ParaT, with lowest levels present in spleen and thymus. In comparison to tissues from young (6-8 week) mice, older (18 month) mice contained lower concentrations (20-40%) of both polypeptides, with qualitatively similar decreases in mRNA content.

Aging↗

The sequence of human parathymosin deduced from a cloned human kidney cDNA.

The amino acid sequence of human parathymosin has been deduced from the cDNA sequence of a clone isolated from a human kidney cDNA library. Screening of the cDNA library with a probe containing a partial rat cDNA sequence yielded two clones containing inserts of 1200 and 1100 base pairs respectively, each including the complete open reading frame for human parathymosin. The open reading frame contains 306 nucleotides, including the codon for the initiator methionine. Analysis of the 5' flanking sequence excluded the presence of a hydrophobic signal peptide in the translated sequence. It may therefore be concluded that parathymosin, like prothymosin alpha, is synthesized without formation of a large precursor polypeptide. Comparison of the deduced amino acid sequence with the known primary structure of rat and bovine parathymosins shows that the primary structure of parathymosin is highly conserved among these species.

Amino Acid Sequence↗