Phenotype Prevalence and Health-Related Quality of Life of Lebanese Women With Polycystic Ovary Syndrome

ObjectivePolycystic ovary syndrome (PCOS) is one of the most common endocrine disorders. Our study aimed to assess, for the first time, the phenotype prevalence and the health-related quality of life of Lebanese women with PCOS.MethodsThis was a cross-sectional study conducted on 322 Lebanese women with PCOS, using a questionnaire containing sociodemographic data, comorbidities, disease-related clinical questions, and the validated PCOS questionnaire (PCOSQ). The quality of life mean scores and phenotypes were compared and correlated among the different sociodemographic data, comorbidities, and disease-related questions.ResultsPhenotype A (67%) was the most common phenotype. High waist circumference and higher Body Mass Index (BMI) were reported mostly in classic phenotypes in comparison with nonclassic (P < .05). The mean total score of all PCOSQ domains was 3.61 ± 1.60. The mean score for each domain (from the greatest to the least serious concern) was menstrual problems (3.31 ± 1.26), emotion (3.33 ± 1.22), weight (3.41 ± 2.12), body hair (3.86 ± 1.79), and infertility (4.15 ± 1.61). Age was negatively correlated only to weight domain score (r = ?0.17, P = .002). BMI was associated only with emotion and weight domain scores (P = .017 and P < .001, respectively). A bigger impairment in nearly all subscales of the PCOSQ in patients presenting with abdominal obesity, glucose intolerance, and increased blood pressure was noted (P < .05).ConclusionMost Lebanese women with PCOS present phenotype A and have a serious impairment in their health-related quality of life, particularly in the menstrual and emotional domains. This highlights the need for community and individual support.     

Phenotype modulation in primary cultures of rat aortic smooth muscle cells

The transition of adult rat aortic smooth muscle cells from a contractile to a synthetic phenotype during the first week of primary culture on a substrate of fibronectin in serum-free medium was studied by light and electron microscopy. The weak base chloroquine and the carboxylic ionophore monensin were both found to inhibit the spreading of the cells and the accompanying changes in cellular fine structure. The exchange of myofilament bundles for a prominent rough endoplasmic reticulum and Golgi complex was delayed and vacuoles filled with incompetely degraded material accumulated in the cytoplasm. The microtubule-disruptive drugs colchicine and nocodazole likewise opposed the spreading and fine structural reorganization of the cells. Most typically, the Golgi stacks were small and widely dispersed. In addition, vacuoles of the type mentioned above increased in number. On the other hand, there was surprisingly little effect of cytochalasin B, a drug that is supposed to interfere with the assembly of actin filaments. The observations suggest that the phenotypic modulation of arterial smooth muscle cells is dependent on: (a) lysosomal degradation of discarded cellular constituents, (b) active vesicular transport along the exocytic pathway to provide the expanding cell surface with new membrane, and (c) a normal microtubular cytoskeleton to ensure the establishment of a new and functionally efficient intracellular organization.     

Binding sites for maize nuclear proteins in the terminal inverted repeats of the Mul transposable element

Summary Nuclear protein extracts from Mu-active, Mu-inactive and non-Mutator lines of maize were used to identify the binding sites for maize nuclear proteins in the terminal inverted repeats (TIR) of the Mul transposable element. We found binding activities of nuclear proteins that specifically interact with both TIRs of the Mu1 element. DNase I footprinting was performed to localize the binding sites. We found that the nuclear proteins from Mu-active lines and non-Mu lines bound to the Mu1 TIR at two different sites, i.e. a 13 by sequence (CGGGAACGGTAAA, designated as site I) and another 8 by sequence (CGGCGTCT, designated as site II). However, the nuclear proteins from Mu-inactive lines bound only one of these sites, i.e. site I. Mobility shift assays with synthetic oligonucleotides containing site I and 11 respectively confirmed the specificities of these binding activities. Site I was shown to be an imperfect direct repeat of a hexamer binding site (CGGGAA CGGTAA). Oligonucleotides containing either of the hexamers showed specific binding activity to nuclear protein from both Mu-active and Mu-inactive lines. The possible role of these proteins in Mu transposition is discussed.