Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.6 (thromboplastin)
 13,278 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study aimed to evaluate the clinical and metabolic effects of a low-dose triphasic oral contraceptive containing gestodene, a new 19-nortestosterone derivative, among 42 healthy women aged 19-43 years during 6 months of treatment. Absence of any absolute or relative contraindications to hormonal contraception was the criterion for the subjects. Findings revealed that the pill exerted good cycle control and the incidence of irregular bleeding was very low. As for the coagulatory system, there was an increase in prothrombin activity and in fibrinopeptide A plasma levels, while there was a decrease in activated partial thromboplastin time. Antithrombin III activity, fibrinogen concentration and platelets count did not change during pill intake. No significant modifications in plasma total cholesterol, low density lipoprotein-cholesterol or in the subfraction high density lipoprotein 2-cholesterol (HDL2-CH) were observed. Serum triglyceride (HDL-CH and HDL3-CH) levels were significantly higher at the end of treatment. The pill did not alter fasting insulin and glucose levels or their response to an oral glucose tolerance test. Therefore, the preliminary findings suggest that the new triphasic formulation containing gestodene seems to be a safe and reliable preparation, as demonstrated by its regular cycle control, good contraceptive efficacy, and low incidence of subjective and objective side effects.
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PMID:Clinical and metabolic effects of a triphasic pill containing gestodene. 148 72

Apolipoprotein A-I (apoA-I), the major protein of high density lipoproteins, facilitates reverse cholesterol transport from peripheral tissue to liver. To determine the structural motifs important for modulating the in vivo catabolism of human apoA-I (h-apoA-I), we generated carboxyl-terminal truncation mutants at residues 201 (apoA-I201), 217 (apoA-I217), and 226 (apoA-I226) by site-directed mutagenesis. ApoA-I was expressed in Escherichia coli as a fusion protein with the maltose binding protein, which was removed by factor Xa cleavage. The in vivo kinetic analysis of the radioiodinated apoA-I in normolipemic rabbits revealed a markedly increased rate of catabolism for the truncated forms of apoA-I. The fractional catabolic rates (FCR) of 9.10 +/- 1.28/day (+/- S.D.) for apoA-I201, 6.34 +/- 0.81/day for apoA-I217, and 4.42 +/- 0.51/day for apoA-I226 were much faster than the FCR of recombinant intact apoA-I (r-apoA-I, 0.93 +/- 0.07/day) and h-apoA-I (0.91 +/- 0.34/day). All the truncated forms of apoA-I were associated with very high density lipoproteins, whereas the intact recombinant apoA-I (r-apoA-I) and h-apoA-I associated with HDL2 and HDL3. Gel filtration chromatography revealed that in contrast to r-apoA-I, the mutant apoA-I201 associated with a phospholipid-rich rabbit apoA-I containing particle. Analysis by agarose gel electrophoresis demonstrated that the same mutant migrated in the pre-beta position, but not within the alpha position as did r-apoA-I. These results indicate that the carboxyl-terminal region (residue 227-243) of apoA-I is critical in modulating the association of apoA-I with lipoproteins and in vivo metabolism of apoA-I.
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PMID:Carboxyl-terminal domain truncation alters apolipoprotein A-I in vivo catabolism. 789 Jun 63