Water Pipe Smoking Affects Young Females and Males Differently with Some Effects on Immune System Cells, but None for C-reactive Protein, Thyroid Hormones, and Vitamin D.

INTRODUCTION: Water pipe smoking (WPS) is a major health threat leading to higher mortality, morbidity, and incidence of many diseases, such as inflammatory, respiratory and cardiovascular diseases; and cancers. This study aimed to determine the differences in the effects of WPS on the immune system, inflammatory markers, lipids, vitamin D, and thyroid hormones in female and male WP smokers, and compared to nonsmokers of both sexes. No other studies showed the differences between female and male WP smokers for the parameters investigated here, with the exception of the lipid profile. METHODOLOGY: The study was carried on 76 randomly chosen subjects (17 female and 17 male WP smokers, 21 female and 21 male nonsmokers) living in Saudi Arabia with an age range of 20-35 years. Blood samples were collected to determine the differential complete blood counts; lipid profiles; and C-reactive protein, triiodothyronine, thyroxine, and vitamin D concentrations. RESULTS: Results showed no significant differences between female smokers and nonsmokers for all parameters. Male smokers had a significantly lower mean monocytes count and a significantly higher mean red blood cell count and hemoglobin concentration compared to male nonsmokers. Comparing females and males among smokers and nonsmokers separately, the only significant difference in the parameters that was not found in both comparisons was a significantly lower mean basophil count in female nonsmokers compared to male nonsmokers. CONCLUSION: It may be concluded that the effects of WPS were limited to males with immune cells and hematology minimally affected, and that females and males were affected differently by WPS.

Carrying epirubicin on nanoemulsion containing algae and cinnamon oils augments its apoptotic and anti-invasion effects on human colon cancer cells.

The nanotherapeutics holds great potential in cancer therapy since they may consist of more than one anticancer agent that has a different mechanism of action. The present study aimed to incorporate the epirubicin (EPI) into a nanoemulsion containing the algae and cinnamon oils (ALG-CN-EPI) using ultrasonication technique. The apoptotic efficacy of ALG-CN-EPI was assessed in the HCT116 human colon cancer cells using the assays of CCK-8, DNA fragmentation, reactive oxygen species (ROS) generation, and Annexin V-FITC/PI while the anti-invasion effect of ALG-CN-EPI was determined by the transwell invasion assay. The zeta average diameters and zeta potential of the nano-suspensions of ALG-CN-EPI, measured by the zetasizer, were 117.2 ± 3.02 nm and -1.810 ± 0.07 mV, respectively. Results of the apoptotic evaluation revealed that the half-maximal inhibitory concentration (IC50) of ALG-CN-EPI (0.7 ± 0.21 µM) was distinctly lower than that of free EPI (6.00 ± 1.56 µM). The DNA fragmentation of HCT116 cells was amplified by a factor of 8 ± 0.24 when treated with ALG-CN-EPI but it did not considerably differ when treated with the free EPI (1.13 ± 0.31). Additionally, cells treated with ALG-CN-EPI resulted in a significant elevation of the intracellular ROS production and higher percentages of late apoptotic cells relative to the EPI treated cells. ALG-CN-EPI treatment suppressed the invasion ability of HCT116 cells to (32.98 ± 3.28)%, whereas the invasion ability of EPI exposed cells was only reduced to about (56 ± 1.81)%. In conclusion, the resulted new nanotherapeutics (ALG-CN-EPI) has potentiated the antitumor activity of EPI.

Purification of a murine IgM monoclonal antibody.

An IgM monoclonal antibody, S11-23.4, raised against the 47-62 amino acid sequence in bovine prothrombin fragment 1 (F-1, the amino-terminal 156 residues of prothrombin), was purified from tissue culture supernatants and ascites using different purification schemes to determine the best method. There are many different purification schemes for the purification of IgG antibodies, which are generally easier to purify than IgM antibodies. Several different methods and schemes were tried to purify S11-23.4, and it was determined that the best purification schemes are ion exchange chromatography for cell culture IgM antibodies, and a G-100 gel filtration column, in conjunction with precipitation, reduction, and alkylation, for the same IgM antibody in ascites.

Production of metal ion-dependent monoclonal antibodies against peptides in bovine prothrombin fragment 1.

Bovine prothrombin fragment 1 (F-1: the amino-terminal 156 residues of prothrombin) is used as a model to study the Ca(II) and phospholipid binding of prothrombin. The 35-46 segment in F-1 posses an alpha-helical region and three aromatic residues, conserved in several vitamin K-dependent blood coagulation factors. These residues are believed to have a specific function and to be important in the phospholipid binding of F-1. The 47-62 region, a disulfide loop, is believed to stabilize the gamma-carboxyglutamic acid domain of the protein. Goals of this research were to produce monoclonal antibodies against the above two sequences, for later functional studies. Antibodies S9-32.8 and S9-5.5 were produced against the 35-46 sequence; antibody S11-23.4 was raised against the 47-62 region. Both S9-32.8 and S9-5.5 bound to F-1 immobilized on ELISA plates in the presence of 10 mM Ca(II) with higher affinity than to F-1 coated in the presence of 10 mM Mg(II) or in the absence of metal ions. S11-23.4 showed greatest binding to F-1 coated in the presence of 10 mM Mg(II). Thus, the epitopes of the antibodies are metal ion-dependent and are developed by Ca(II) binding to F-1.