[Migration. Opportunities for recruitment of skilled employees in the care sector]. / Migration. Chancen für die Gewinnung von Fachkräften in der Pflegewirtschaft.

A central objective of this study was to estimate the potential workforce for the elderly care sector in Germany and to compare it with the predicted demand for nurses in 2030. The authors describe the opportunities and obstacles in recruiting skilled professionals from EU member states and from countries outside the EU. Different scenarios of how to raise labor input are discussed so as to determine the domestic potential until 2030 in Germany. The results show that only by assuming unrealistic conditions, e. g., expectations of a high full-time working quota or far more working women, can the domestic potential meet the predicted future demands. Therefore, Germany's chances of attracting skilled foreign workers were assessed by analyzing wage differentials, unemployment probabilities, demographic developments, and professional and cultural aspects between the countries. A major finding study is that the German labor market cannot provide enough nursing care professionals for the elderly care sector by 2030. Secondly, most of the other EU member states are facing similar challenges, at least in the long run. Therefore, it is recommendable to intensify collaboration with populous Asian countries in the future.

p53 gene mutations in radiation-induced thyroid cancer.

Little is known about the role of specific oncogenes and tumor suppressor genes in radiation-induced thyroid cancer (RITC). In thyroid cancer, mutations in the p53 tumor suppressor gene have been largely confined to the more aggressive anaplastic forms. We studied point mutations in the p53 gene in 22 patients exposed in childhood to radiation in the head and neck area who later developed papillary thyroid cancers (RITC). Eighteen thyroid cancer patients without exposure to radiation, selected to match by gender and age the RITC group, were used as the control group. After histological identification, DNA was extracted from paraffin-embedded specimens. Exons 5-8 of p53 were PCR amplified and screened for mutations by single strand conformation polymorphism analysis and cycle sequencing. Four of 22 RITC patients (18%) showed missense point mutations. No missense mutations were found in the cancer control group. The missense mutations in the RITC group occurred at codon 208 in 2 patients, codon 177 in 1, and codon 217 in 1. The mutations were transitions from G to A and C to T. All patients with missense mutations were male and had lymph node involvement. Three of the 4 patients with p53 missense mutations had invasion of the cancer beyond the thyroid capsule compared to 2 of the 17 remaining RITC patients. None of the patients with p53 mutations had distant metastases or recurrence of the tumor. These results suggest that p53 gene point mutations may play a pathogenetic role in some radiation-induced, well differentiated thyroid cancers and in their local spread.

Phylogenetically conserved amino acids of MBP and P0 from amphibian myelin.

Myelin basic protein (MBP) and P0 glycoprotein are major structural proteins of myelin. In adult frog, MBP is found in both the central and peripheral nervous systems (CNS and PNS), while P0 is found exclusively in the PNS. To assess the phylogenetic conservation of these proteins, MBP and P0 were isolated from adult bull-frog. A cyanogen bromide cleavage peptide of MBP (8-26), and the amino-terminal region (1-20) and an endoproteinase Lys-C peptide (67-79) of P0 were sequenced and compared to those of other vertebrate species. Residues that were conserved among other vertebrate species were found also to be conserved in frog: MBP--Ala18, Ser19, Thr20, Asp22; P0--Ile1, Val3, Thr5, Val13, Gly14, Ser15, Val17, Leu19, Trp72, Val73, Gly74, Lys79. These residues are located within or adjacent to regions that have been postulated to form beta strands and to be essential to the folding and function of these proteins.

Generation of DM-20 splice site in myelin proteolipid protein gene: a hypothesis based on analysis of the amphibian protein.

The DM-20 isoform of proteolipid protein (PLP) of central nervous system myelin is undetectable in amphibia, but readily detectable in reptiles, birds and mammals. To explain the phylogenetic origin of DM-20, it has been proposed that a donor-acceptor RNA splice site was generated by the introduction of a single base change in the codon encoding amino acid 116 of PLP. We tested this hypothesis by isolating and sequencing peptides from bullfrog PLP. One of the peptides corresponded to mammalian residues 110-122, which contain the N-terminal boundary region for the domain excluded from DM-20 in higher vertebrates. We found that the Thr115-Val116 sequence is conserved between frog and mammal. Therefore, we propose that a single base change in the third position of the codon for Thr115 would account for the appearance of the new donor-acceptor splice site. Three amino acids elsewhere in this thirteen-residue peptide were found to differ between bullfrog and mammal, which could account for the previously reported weak recognition of amphibian PLP by an antiserum specific for peptide 109-128. A second peptide from bullfrog PLP had a sequence identical to that of residues 45-52 in mammalian PLP. Our findings explain how a specific change in the myelin PLP gene could generate a new form of the PLP protein.

Identification of the active site tyrosine of Flp recombinase. Possible relevance of its location to the mechanism of recombination.

A combination of site-directed mutagenesis and amino acid sequence analysis identifies Tyr-343 of Flp recombinase as the residue that covalently attaches to DNA during the strand-cleavage step of recombination. This residue is part of the invariant His-Arg-Tyr triad of the Int family of recombinases. Tyr-343 is located in a highly protease-accessible (and hence "open") region of Flp. This placement may provide the conformational flexibility required for the dual role of Tyr-343 in recombination: nicking of the DNA strands to initiate recombination and joining of the nicked strands across partner substrates to complete recombination. In-frame insertion of a few amino acids close to Tyr-343 (and to its amino-terminal side) does not affect substrate recognition by Flp but abolishes its catalytic function.