Assessment of sexual dysfunction and determination of its risk factors in the Republic of Korea.

OBJECTIVE: To assess sexual function among women via self-evaluation of female sexual dysfunction (FSD) and to determine risk factors for FSD among Korean women. METHODS: A preliminary questionnaire-based study in Ansan, Korea, enrolled 935 women between January and December 2010. Participants completed the Female Sexual Function Index and a self-administered survey. Participants were divided into 2 groups: in the recognized group (RG), women were aware of their sexual problems; in the unrecognized group (URG), women were not. RESULTS: The prevalence of FSD was 46.1% (n=431). The prevalence of recognized FSD was 21.5% (n=201), whereas that of unrecognized FSD was 24.6% (n=230) Younger women showed a significantly more positive attitude toward sex compared with older individuals (P<0.001). Sexual desire, sexual arousal, dyspareunia, lubrication, and sexual satisfaction were factors of sexual dysfunction in the RG. In the URG, sexual arousal, sexual desire, orgasm, dyspareunia, and sexual satisfaction were identified as significant factors. CONCLUSION: Women in the RG had positive attitudes toward sex, whereas those in the URG had negative attitudes. Women who were unsatisfied with their sexual life did not express a need for treatment. The sociocultural background of Korean women should be considered in the diagnosis and treatment of FSD.

Human glutamate dehydrogenase is immunologically distinct from other mammalian orthologues.

Five monoclonal antibodies (mAbs) that recognize human glutamate dehydrogenase (GDH) have been selected and designated as monoclonal antibodies hGDH60-6, hGDH60-8, hGDH63-10, hGDH63-11, and hGDH91-14. A total of five mAbs recognizing different epitopes of the enzyme were obtained, two of which inhibited human GDH activity. When total proteins of human homogenate separated by SDS- PAGE, were probed with mAbs, a single reactive protein band of 55 kDa, which co-migrated with purified recombinant human GDH was detected. When the purified GDH was incubated with each of the mAbs, its enzyme activity was inhibited by up to 58%. Epitope mapping analysis identified, two subgroups of mAbs recognizing different peptide fragments. Using the individual anti-GDH antibodies as probes, the cross reactivities of brain GDH obtained from human and other animal brain tissues were investigated. For the human and animal tissues tested, immunoreactive bands on Western blots appeared to have the same molecular mass of 55 kDa when hGHD60-6, hGHD60-8, or hGHD91-14 mAbs were used as probes. However, the anti-human GDH mAbs immunoreactive to bands on Western blots reacted differently on the immunoblots of the other animal brains tested, i.e., the two monoclonal antibodies hGDH63-10 and hGDH63-11 only produced positive results for human. These results suggest that human brain GDH is immunologically distinct from those of other mammalian brains. Thorough characterization of these anti-human GDH mAbs could provide potentially valuable tool as immunodiagnostic reagents for the detection, identification and characterization of the various neurological diseases related to the GDH enzyme.