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A cross-sectional study was conducted to understand the medication compliance of elderly osteoporosis patients and to further analyze the influencing factors of drug compliance. The elderly osteoporosis patients who were admitted to the First People's Hospital of Huzhou, Zhejiang from March 2015 to January 2017 were selected as the research subjects. Subsequently, the three months, six months and 12 months of follow-up were performed from the group of subjects who prescribe anti-osteoporosis drugs to determine the patient's medication status. Hereon, a cross-sectional survey was conducted to investigate the status of drug compliance in elderly patients with osteoporosis. Moreover, multivariate logistic regression analysis was used to analyze the influencing factors of medication compliance. The discontinuation rates and causes were not the same in different time periods and the cumulative withdrawal rate was high (37%) within one year. A total of 492 cases of elderly osteoporosis patients were included in this study, whereas only 45.73% of patients had good drug compliance. Elderly patients with osteoporosis have poor medication compliance and education, marital status, and medication types all affect medicine-taking compliance of patients. Therefore, it is suggested that health education should be carried out, and psychological care of patients should also be strengthened. Meanwhile, the follow-up system for drug compliance should be established to improve medication compliance as well world wide.

Previous studies by others and our group have demonstrated the expression of AQP3 protein in human chorioamniotic membranes. Here, we investigated whether cyclic adenosine monophosphate (cAMP) up-regulation of aquaporin 3 (AQP3) protein expression in human amniotic epithelial cells (hAECs) is mediated by protein kinase A (PKA) dependent or independent pathway. Cells were treated with various concentrations of Forskolin, SP-cAMP, H-89 at various time intervals or optimal concentration of Forskolin in combination with H-89 in the blocking experiments. Forskolin significantly increased cAMP levels and the expression of PKA, p-CREB and AQP3. SP-cAMP had similar effects. H-89 inhibited PKA, p-CREB and AQP3 protein expression, and attenuated the stimulatory effect of Forskolin. These results show that the AQP3 protein expression in hAECs was regulated by cAMP-PKA-CREB signal pathway. A relatively short biological half life of AQP3 renders its rapid responsiveness to regulation.

Objective: To investigate the expression of aquaporins-3 (AQP3) in amniotic epithelial cells regulated by cyclic adenosine monophosphate-protein kinase A (cAMP-PKA) signal pathway and to explore the mechanisms of its expression., Methods: The amniotic epithelial cells were collected from 30 patients who underwent elective caesarean sections at term with normal amniotic fluid volume and primarily cultured. The cultured cells were treated with (1)forskolin groups: different concentration (0, 2.5, 5, 50 or 100 µmol/L) of forskolin treated cells for 2 hours, and the optimal concentration of forskolin treated cells with different time (0, 1, 2, 10 or 20 hours); (2)SP-cAMP groups: different concentration (0, 2.5, 5, 50 or 100 µmol/L) of SP-cAMP treated cells for 2 hours, and the optimal concentration of SP-cAMP treated cells with different time (0, 1, 2, 10 or 20 hours); (3)H-89 groups: different concentration (0, 5, 10, 50 or 100 µmol/L) of H-89 treated cells for 2 hours, and the optimal concentration of H-89 treated cells with different time (0, 1, 2, 10 or 20 hours ). The level of intracellular cAMP and activity of PKA were detected by using ELISA, and immunohistochemistry was used to detect the localization of AQP3, the protein expression of total cAMP-response element binding protein (CREB) and phospho-CREB (p-CREB) and AQP3 were assessed by western blot analysis. Cell proliferation was assessed by cell counting kit-8 (CCK-8) assay., Results: (1) The brown staining of AQP3 was detected in both cell membrane and cytoplasm in each group. (2) There was no significant change of the cell proliferation rate among groups with different concentration of forskolin, SP-cAMP and H-89 treatment (P > 0.05). (3) After different concentration of forskolin treated 2 hours, the expression of total CREB had no significant difference among them(P > 0.05). While the expression of cAMP level, PKA activity, p-CREB and AQP3 protein were significantly changed, which were higher in 2.5 µmol/L, 5 µmol/L, 50 µmol/L forskolin group when compared with 0 µmol/L (P < 0.05). Their expressions in 5 µmol/L forskolin group were higher than that in 2.5 µmol/L and 50 µmol/L (P < 0.05). The optimal forskolin concentration was 5 µmol/L. (4) After different concentration of SP-cAMP treated 2 hours, the expression of total CREB and cAMP level had no significant difference among them (P > 0.05), while the expression of PKA activity, p-CREB and AQP3 protein were significantly changed, which were higher in 5 µmol/L, 50 µmol/L SP-cAMP group when compared with 0 µmol/L (P < 0.05). Their expressions in 50 µmol/L SP-cAMP group were higher than that in 5 µmol/L (P < 0.05). The optimal SP-cAMP concentration was 50 µmol/L. (5) After different concentration of H-89 treated 2 hours, the expression of total CREB and cAMP level had no significant difference among them (P > 0.05), while the expression of PKA activity, p-CREB and AQP3 protein were significantly changed, which were lower in 10 µmol/L, 50 µmol/L and 100 µmol/L H-89 group when compared with 0 µmol/L (P < 0.05). Their expressions in 10 µmol/L H-89 group were lower than that in 50 µmol/L, 100 µmol/L (P < 0.05). The optimal H-89 concentration was 10 µmol/L. (6) p-CREB and AQP3 protein expression were significantly lower in 5 µmol/L forskolin combined 10 µmol/L H-89 incubating 2 hours group when compared with 5 µmol/L forskolin, but higher than that in 10 µmol/L H-89 treated group (P < 0.05). Total CREB was no significant difference among the three groups (P > 0.05)., Conclusion: cAMP-PKA signal transduction pathway may regulate AQP3 protein expression in human amniotic epithelial cells.

Previous studies by our group as well as other researchers have found expression of Aquaporins (AQPs) 1, 3, 8, and 9 in human chorioamniotic membranes and placenta. Our previous study found that the alteration of the expression of AQPs 1, 3, 8, and 9 in placenta and fetal membranes was an adaptive response to maintain amniotic fluid homeostasis in case of abnormal amniotic fluid volume, which is likely to affect the intramembranous absorption and transport of water and solute from mother to fetus. However, the actual regulation mechanisms of intramembranous absorption and placental water flow are not yet clear, making it difficult to treat abnormal amniotic fluid volume effectively. Several studies found that many factors, including hormone levels, osmotic pressure, temperature, and oxygen concentration, regulate expression of AQPs in placenta, fetal membranes, and other mammalian organs through several signal transduction pathways, such as the cAMP, the MAPK, the PI3K/AKT, and the PKC pathways. These factors could provide potential therapeutic targets for the treatment of abnormal amniotic fluid volume.