Impaired sports performance of athletes suffering from pollen-induced allergic rhinitis: a cross-sectional, observational survey in German athletes.

BACKGROUND: Allergic rhinitis has major impacts on sports performance of athletes. The present study aimed at determining the frequency of seasonal pollen allergy and analyzing the impacts of pollen allergy, the choice of allergy treatments and their benefits for sports performance in a group of professional and recreational athletes. METHODS: The study was conducted as a self-reported questionnaire survey. Subjects were recruited from the German Sport University and the Cologne Marathon 2014 during the peak pollen season of 2014. RESULTS: Athletes returned 636 completed questionnaires, 42.6% of participants reported suffering from a pollen allergy and 30.2% also suffered from asthma. Performance impairments were reported in more than 80% of allergic subjects. In all, 82.2% of subjects used symptomatic medications, 32.3% alternative therapies, and 47.6% allergen immunotherapy. Subjects who used immunotherapy had fewer impaired training bouts than those who used symptomatic and alternative therapies. The majority of subjects had concerns about allergy treatment such as side effects, negative impacts on sports performance and lack of long-term effects. CONCLUSIONS: This study confirmed a high prevalence of pollen allergy among German athletes. The majority of allergic rhinitis athletes were undertreated, and the reason could be their reservations about allergy treatments. Pollen allergy tremendously reduced sports performance of athletes during the pollen season. This impact can be lessened with proper treatment such as immunotherapy. Better understanding of available treatment modalities should be provided to patients and physicians to improve sports performance of athletes suffering from pollen allergy.

Relationship between RNA lariat debranching and Ty1 element retrotransposition.

The Saccharomyces cerevisiae DBR1 gene encodes a 2'-5' phosphodiesterase that debranches intron RNA lariats following splicing. Yeast dbr1 mutants accumulate intron lariats and are also defective for mobility of the retrotransposons Ty1 and Ty3. We used a mutagenic PCR method to generate a collection of dbr1 mutant alleles to explore the relationship between the roles of DBR1 in transposition and debranching. Eight mutants defective for Ty1 transposition contained single amino acid changes in Dbr1p. Two mutations, G84A and N85D, are in a conserved phosphoesterase motif that is believed to be part of the active site of the enzyme, supporting a connection between enzymatic activity and Ty1 transposition. Two other mutations, Y68F and Y68D, occur at a potential phosphorylation site, and we have shown that Dbr1p is phosphorylated on tyrosine. We have developed an RNase protection assay to quantitate intron RNA accumulation in cells. The assay uses RNA probes that hybridize to ACT1 intron RNA. Protection patterns confirm that sequences from the 5' end of the intron to the lariat branch point accumulate in dbr1 mutants in a branched (lariat) conformation. RNase protection assays indicate that all of the newly generated dbr1 mutant alleles are also deficient for debranching, further supporting a role for 2'-5' phosphodiesterase activity in Ty1 transposition. A Ty1 element lacking most of its internal sequences transposes independently of DBR1. The existence of Dbr1p-dependent Ty1 sequences raises the possibility that Dbr1p acts on Ty1 RNA.

Support for a meiotic recombination initiation complex: interactions among Rec102p, Rec104p, and Spo11p.

Initiation of meiotic recombination in the yeast Saccharomyces cerevisiae requires at least 10 gene products. The initiation event creates double-strand breaks, which are then processed by other recombination enzymes. A variety of classical observations, such as the existence of recombination nodules, have suggested that the proteins catalyzing recombination form a complex. A variety of lines of evidence indicate that Rad50p, Mre11p, and Xrs2p interact, and genetic data suggesting interactions between Rec102p and Rec104p have been reported. It has recently been shown that Spo11p coimmunoprecipitates with Rec102p in meiosis as well. In this paper, we provide genetic and biochemical evidence that the meiosis-specific proteins Rec102p, Rec104p, and Spo11p all interact with each other in meiosis. Furthermore, we demonstrate that the interaction between Rec102p and Spo11p does not require Rec104p. Likewise, the interaction between Rec104p and Rec102p does not require Spo11p, although Spo11p may stabilize that association. The interactions suggest that Spo11p, Rec102p, and Rec104p may form a trimeric complex during the initiation of recombination.