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Biomedical subjects

C C Chen

Publications and source records attributed to C C Chen.

At least 595 records · Page 33Linked to original sources
PubMed1987

Persistence of hepatitis B viral antigens in Culex quinquefasciatus.

Culex quinquefasciatus mosquitoes were fed on or inoculated with blood or serum positive for hepatitis B viral antigens and pools of mosquitoes were tested by radioimmunoassay daily for 3 weeks after exposure to detect the viral antigens. Hepatitis B surface antigen (HBsAg) was detectable up to 3 weeks, while hepatitis B e antigen (HBeAg) persisted only for 3 days in mosquitoes after feeding on hepatitis B viral antigens-positive blood. Mosquitoes inoculated with serum were HBsAg-positive for 3 weeks and HBeAg positive for 4 days after inoculation. These results suggest that biological multiplication of hepatitis B virus did not occur in these mosquitoes. The possibility of mechanical transmission of hepatitis B antigens by mosquitoes is discussed.

Animals↗
PubMed1986

Decreased Na+-K+-ATPase activity and [3H]ouabain binding sites in various tissues of spontaneously hypertensive rats.

Na+-K+-ATPase activity and [3H]ouabain binding were studied in cerebral cortex, kidney and heart isolated from spontaneously hypertensive rats (SHR) in both the prehypertensive (6 week old) and the hypertensive stages (14 week old). Na+-K+-ATPase activity of heart and kidney was found to be decreased by about 38 and 16% in the prehypertensive and hypertensive stages of SHR respectively; that of cerebral cortex decreased by 23.5% only in the hypertensive stages. Similar results were obtained by pretreatment of membranes with either 0.001% Triton X-100 or by increasing the K concentration from 4.7 to 12.7 mM in the Krebs solution. No significant differences in microsomal protein yield were noted between prehypertensive or hypertensive SHR and the age-matched WKY rats. The study of binding of [3H]ouabain to cerebral cortex, kidney and heart showed that the decreased Na+-K+-ATPase in hypertensive SHR was due to a 31.6, 21.8 and 41.3% reduction in the number of high affinity binding sites respectively, while the affinity constants (Kd) of ouabain binding sites on this enzyme in cerebral cortex, kidney and heart of the normotensive WKY rats were 26.5, 455.9 and 74.7 nM respectively and those from the hypertensive SHR were not altered. The plasma K concentration of the SHR in the prehypertensive and hypertensive stages was 4.07 and 4.13 mM, respectively, significantly less than that of the age-matched WKY rats. It appears that the decrease of plasma K and Na+-K+-ATPase activity in heart and kidney in SHR is derived from a genetic defect and may be related to the abnormal Na handling in this genetically hypertensive strain.

Animals↗
PubMed1986

Solubilization and functional reconstitution of the proline transport system of Escherichia coli.

The membrane carrier for L-proline (product of the putP gene) of Escherichia coli K12 was solubilized and functionally reconstituted with E. coli phospholipid by the cholate dilution method. The counterflow activity of the reconstituted system was studied by preloading the proteoliposomes with either L-proline or the proline analogues: L-azetidine-2-carboxylate or 3,4-dehydro-L-proline. The dilution of such preloaded proteoliposomes into a buffer containing [3H]proline resulted in the accumulation of this amino acid against a considerable concentration gradient. A second driving force for proline accumulation was an electrochemical potential difference for Na+ across the membrane. More than a 10-fold accumulation was seen with a sodium electrochemical gradient while no accumulation was found with proton motive force alone. The optimal pH for the L-proline carrier activities for both counterflow and sodium gradient-driven uptake was between pH 6.0 and 7.0. The stoichiometry of the co-transport system was approximately one Na+ for one proline. The effect of different phospholipids on the proline transport activity of the reconstituted carrier was also studied. Both phosphatidylethanolamine and phosphatidylglycerol stimulate the carrier activity while phosphatidylcholine and cardiolipin were almost inactive.

Amino Acid Transport Systems, Neutral↗
PubMed1986

The effects of proteoglycans from different cartilage types on in vitro hydroxyapatite proliferation.

Proteoglycans extracted from nasal and articular cartilages have previously been shown to inhibit hydroxyapatite proliferation in vitro. This study now demonstrates that proteoglycans isolated (dissociatively extracted and reaggregated in vitro) from bovine fetal growth plate and bovine occipital condyle, as well as those from bovine nasal cartilage, all retard hydroxyapatite seeded-growth in vitro. On a weight basis (1 mg/ml), the growth plate proteoglycan preparation had a significantly greater inhibitory effect. The greater inhibitory effect of the growth plate proteoglycans as compared to the other cartilage proteoglycan preparations may be related to the unique properties of the proteoglycans in the growth plate, a tissue that undergoes physiological calcification.

Animals↗