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1.
J Pediatr Adolesc Gynecol ; 20(3): 179-80, 2007 Jun.
Article in English | MEDLINE | ID: mdl-17561186

ABSTRACT

PURPOSE: We determined the incidence of Fitz-Hugh-Curtis syndrome (FHCS) in adolescents who had mild to moderately severe pelvic inflammatory disease (PID). DESIGN: Prospective cohort study. SETTING: Harris County Juvenile Detention Center, April 2000-April 2006. PARTICIPANTS: Incarcerated female adolescents. INTERVENTION: In patients who met accepted criteria for the diagnosis of PID, we determined the proportion that had right upper quadrant pain that responded to therapy for PID. They were diagnosed as having FHCS. RESULTS: The 117 subjects' mean age (SD) was 15.6 (1.8) years; 37% were Hispanic, 34% black, and 26% white. 5/117 (4.3%, 95% confidence interval 1.4-9.7%) had symptomatic FHCS. Fifteen (13%) of all subjects, including 1 with FHCS, had fever and/or nausea and vomiting (moderately severe PID): none had generalized peritonitis or tubo-ovarian abscess (severe PID). Thirty-four had chlamydial, 4 gonorrheal, and 9 combined infections. All improved with standard outpatient PID therapy. CONCLUSION: FHCS was uncommon (4%) in adolescents who had mild to moderate PID and chlamydia as the most common pathogen.


Subject(s)
Hepatitis/complications , Pelvic Inflammatory Disease/complications , Tissue Adhesions/complications , Adolescent , Cohort Studies , Female , Hepatitis/epidemiology , Humans , Incidence , Prisoners , Prospective Studies , Syndrome , Texas/epidemiology , Tissue Adhesions/epidemiology
2.
Biochem Biophys Res Commun ; 204(1): 142-9, 1994 Oct 14.
Article in English | MEDLINE | ID: mdl-7945352

ABSTRACT

We have investigated sonication-, osmotic shock-, and A23187-induced calcium and horseradish peroxidase release from phosphatidylcholine liposomes. We report that sonication and osmotic shock both cause release of liposome-entrapped horseradish peroxidase activity, thus, completely releasing the entrapped volume into and mixing it with the external medium. However, we find that neither sonication nor osmotic shock releases significant amounts of calcium from liposomes pre-loaded with calcium, while A23187 causes release of significant amounts of calcium from similarly prepared liposomes. We also find that A23187 can release calcium from liposomes after release of entrapment volume by sonication or osmotic shock. Alteration of the net charge of liposomes by substitution of phosphatidylcholine with phosphatidylserine or stearylamine dramatically changes the amount of calcium associated with calcium-loaded liposomes; sonication or addition of A23187 to liposomes containing significant amounts of PS does not appear to release calcium bound to these vesicles. These results suggest that a large fraction (> 99%) of the calcium associated with liposomes is bound to the membranes of the liposomes and that the calcium released by A23187 is due to release of bound rather than entrapped calcium.


Subject(s)
Calcimycin/chemistry , Calcium/chemistry , Liposomes , Amines , Arsenazo III , Kinetics , Models, Biological , Phosphatidylcholines , Phosphatidylserines
3.
J Biol Chem ; 268(24): 17930-4, 1993 Aug 25.
Article in English | MEDLINE | ID: mdl-8394354

ABSTRACT

Previous chemical modification studies have suggested that Cys-369, Cys-658, Lys-482, Asp-712, and Asp-716 are essential for Na,K-ATPase function. To determine if the side chains of these amino acid residues are required for enzyme activity, rat alpha 1 cDNAs containing the mutations Cys-369-->Ser, Cys-658-->Ala, Lys-482-->Ala, Asp-712-->Asn, and Asp-716-->Asn were prepared and stably expressed in HeLa cells, which normally cannot survive in medium containing microM concentrations of ouabain. Expression of rat alpha 1 wild-type and the mutants Cys-369-->Ser, Cys-658-->Ala, and Lys-482-->Ala causes the appearance of HeLa cells that survive in medium containing 0.5 microM ouabain. Membranes isolated from the rat alpha 1 mutant clones exhibit Na,K-ATPase activities, ratios of Na,K-ATPase:phosphoenzyme, and apparent affinities for ouabain and ATP which are comparable to those of the rat alpha 1 wild-type enzyme. HeLa cells expressing mRNA and protein for Asp-712-->Asn and Asp-716-->Asn rat alpha 1 mutants cannot survive in 0.1 microM ouabain, and membranes isolated from these clones exhibit very little or no ouabain-insensitive rat alpha 1 Na,K-ATPase activity. The Asp-712-->Asn, but not Asp-716-->Asn, mutant rat alpha 1 can be phosphorylated by ATP. We conclude that Cys-369, Cys-658, and Lys-482 are not essential for Na,K-ATPase function but that the Asp residues at 712 and 716 are both essential.


Subject(s)
Mutagenesis, Site-Directed , Sodium-Potassium-Exchanging ATPase/biosynthesis , Adenosine Triphosphate/metabolism , Amino Acid Sequence , Animals , Binding Sites , Blotting, Northern , Cell Membrane/enzymology , HeLa Cells , Humans , Kinetics , Ouabain/pharmacology , Rats , Recombinant Proteins/biosynthesis , Recombinant Proteins/metabolism , Sodium-Potassium-Exchanging ATPase/genetics , Sodium-Potassium-Exchanging ATPase/metabolism , Transfection
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