Background: The aim of this study was to evaluate the efficacy and safety of acupuncture in the treatment for allergic rhinitis. Methods: This study was a multicenter, randomized, parallel-controlled study. Participants were randomized to either the active acupuncture, sham acupuncture, or waitlist groups. The active and sham acupuncture groups received acupuncture treatment three times per week for 4 weeks. In the sham group, minimal acupuncture at nonacupuncture points was used. The waitlist group did not receive any acupuncture treatment. Results: Of the 238 participants, 97, 94, and 47 individuals were assigned to the active acupuncture, sham acupuncture, and waitlist group, respectively. After the treatment, the difference in the total nasal symptom score (TNSS) was significantly reduced in the active acupuncture group compared with the sham acupuncture (difference: À1.03, 95% confidence interval [CI]: À1.96, À0.09, P = 0.03) and waitlist (difference: À2.49, 95% CI: À3.68, À1.29, P < 0.0001). The active acupuncture group exhibited a significant change in the total non-nasal symptom score (TNNSS) compared with the waitlist (difference: À0.78, 95% CI: À1.22, À0.34, P = 0.0002), but not the sham acupuncture group (difference; 0.15, 95% CI: À0.21, 0.5, P = 0.56). Both active and sham acupuncture treatments resulted in significant improvements in TNSS and TNNSS compared to baseline. Conclusion: Active acupuncture showed a significantly greater effect on symptoms of allergic rhinitis than either sham acupuncture or no active treatment. The symptoms of allergic rhinitis decreased significantly after treatment in the both acupuncture and sham acupuncture groups. Acupuncture appears to be an effective and safe treatment for allergic rhinitis.

Methods for treating MS/MS data to achieve accurate peptide identification are currently the subject of much research activity. In this study we describe a new method for filtering MS/MS data and refining precursor masses that provides highly accurate analyses of massive sets of proteomics data. This method, coined "postexperiment monoisotopic mass filtering and refinement" (PE-MMR), consists of several data processing steps: 1) generation of lists of all monoisotopic masses observed in a whole LC/MS experiment, 2) clusterization of monoisotopic masses of a peptide into unique mass classes ( MS has evolved into a robust and powerful tool for analyzing biomolecules. For example, MS is presently a preferred analytical tool for proteomics experiments in which dynamic populations of proteins are to be identified and quantified. In shotgun proteomics, hundreds or thousands of proteins are routinely identified through LC/MS/MS experiments using the proteolytic digests of proteome samples. During these LC/ MS/MS experiments, peptides are dynamically selected for fragmentation; the resultant tandem mass spectra (usually on the order of 10 5 spectra) are subsequently subjected to database searching (e.g. SEQUEST or Mascot) to best describe or annotate the peptide.Searching a large set of tandem mass spectra against a protein sequence database is a computationally expensive process; the resultant peptide spectral matches (PSMs) 1 are prone to false-positive (FP) identifications, which have led to the development of several validation methods (1, 2). Acquisition of high quality tandem mass spectra is critical to the whole process of protein identification through the shotgun approach because the measured fragment ion masses are compared with the theoretical values predicted by the search algorithms; any factors that adversely affect the acquisition of tandem mass spectra would undoubtedly lead to incorrect peptide assignments. Venable and Yates (3) systematically studied the effects that variability in tandem mass spectral quality had on peptide identification (i.e. peptide scores) and suggested an approach involving both presearch spectral averaging and postsearch XCorr averaging.Large portions (up to 90%) of tandem mass spectral data are not assigned to peptide sequences (4, 5) for many reasons, such as the presence of unknown protein sequences, the possibility of chemical (or post-translational) modification having occurred, insufficient spectral quality for high confi-

Transcription and replication of mitochondrial DNA (mtDNA) are regulated by nuclear DNA-encoded proteins that are targeted into mitochondria. A decrease in mtDNA copy number results in mitochondrial dysfunction, which may lead to insulin resistance and metabolic syndromes. We analyzed mitochondrial proteins that physically bind to human mitochondrial D-loop DNA using a shot-gun proteomics approach following protein enrichment by D-loop DNA-linked affinity chromatography. A total of 152 D-loop DNA binding proteins were identified by peptide sequencing using ultra high pressure capillary reverse-phase liquid chromatography/tandem mass spectrometry. Bioinformatic analysis showed that 68 were mitochondrial proteins, 96 were DNA/RNA/protein binding proteins and 114 proteins might form a complex via protein-protein interactions. Histone family members of H1, H2A, H2B, H3, and H4, were detected in abundance among them. In particular, histones H2A and H2B were present in the mitochondrial membrane as integral membrane proteins and not bound directly to mtDNA inside the organelle. Histones H1.2, H3 and H4 were associated with the outer mitochondrial membrane. Silencing of H2AX expression inhibited mitochondrial protein transport. Our data suggests that many mitochondrial proteins may reside in multiple subcellular compartments like H2AX and exert multiple functions.

KCT0000496.

Our results suggest that acupuncture in addition to usual care is associated with marked clinical improvement in hot flashes and menopause-related symptoms in perimenopausal or postmenopausal women.