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1.
Proc Biol Sci ; 283(1843)2016 11 30.
Article in English | MEDLINE | ID: mdl-27881743

ABSTRACT

The BA allele of the Drosophila cytochrome P450 gene Cyp6g1 confers resistance to a range of insecticides. It is also subject to intralocus sexual conflict when introgressed into the Canton-S background, whose collection predates the widespread use of insecticides. In this genetic background, the allele confers a pleiotropic fitness benefit to females but a cost to males, and exhibits little sexual dimorphism in conferred insecticide resistance. It is unclear whether these sexually antagonistic effects also exist in current populations that have naturally evolved with insecticides, where genetic modifiers that offset male costs might be expected to evolve. Here, we explore these issues using Drosophila melanogaster caught recently from an Australian population in which the BA allele naturally segregates. While we find increased fecundity in insecticide-resistant BA females and no consistent evidence of fitness costs in males, experimental evolution indicates balancing selection at the locus. We suggest that this apparent discrepancy may be due to reduced investment in reproduction in resistant males. Our results at the population level are consistent with previous work, and suggest that individual-level fitness assays do not always capture sexually antagonistic fitness effects that emerge in a population context.


Subject(s)
Drosophila melanogaster/genetics , Genetic Fitness , Genetic Pleiotropy , Insecticide Resistance/genetics , Sex Characteristics , Alleles , Animals , Australia , Cytochrome P-450 Enzyme System/genetics , Drosophila Proteins/genetics , Female , Fertility , Male
2.
Magn Reson Med ; 45(3): 421-30, 2001 Mar.
Article in English | MEDLINE | ID: mdl-11241699

ABSTRACT

Hyperpolarized (3)He spin-lattice relaxation was investigated in the guinea pig lung using spectroscopy and imaging techniques with a repetitive RF pulse series. T(1) was dominated by interactions with oxygen and was used to measure the alveolar O(2) partial pressure. In animals ventilated with a mixture of 79% (3)He and 21% O(2), T(1) dropped from 19.6 sec in vivo to 14.6 sec after cardiac arrest, reflecting the termination of the intrapulmonary gas exchange. The initial difference in oxygen concentration between inspired and alveolar air, and the temporal decay during apnea were related to functional parameters. Estimates of oxygen uptake were 29 +/- 11 mL min(-1) kg(-1) under normoxic conditions, and 9.0 +/- 2.0 mL min(-1) kg(-1) under hypoxic conditions. Cardiac output was estimated to be 400 +/- 160 mL min(-1) kg(-1). The functional residual capacity derived from spirometric magnetic resonance experiments varied with body mass between 5.4 +/- 0.3 mL and 10.7 +/- 1.1 mL. Magn Reson Med 45:421-430, 2001.


Subject(s)
Helium , Image Enhancement , Lung/physiology , Magnetic Resonance Spectroscopy , Animals , Cardiac Output/physiology , Functional Residual Capacity/physiology , Guinea Pigs , Heart Arrest, Induced , Isotopes , Lung/pathology , Oxygen/blood , Pulmonary Gas Exchange/physiology
3.
J Biol Chem ; 270(38): 22229-35, 1995 Sep 22.
Article in English | MEDLINE | ID: mdl-7673201

ABSTRACT

Acyl carrier protein (ACP) is the carrier of fatty acids during their synthesis and utilization. ACPs (or ACP-like protein domains) have been found throughout biology and share significant amino acid sequence similarities. All ACPs undergo a post-translational modification in which 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group. Overproduction of Escherichia coli ACP from multicopy plasmids strongly inhibits growth of E. coli. We report that upon overexpression of ACP in E. coli post-translational modification is inefficient and the apo protein accumulates and blocks cell growth by inhibition of lipid metabolism. Moreover, a mutant form of ACP that is unable to undergo post-translational modification is a potent inhibitor of growth. Finally, we observed that an increase in the efficiency of modification of overexpressed ACP results in decreased toxicity. The accumulated apo-ACP acts as a potent in vitro inhibitor of the sn-glycerol-3-phosphate acyltransferase resulting in an inability to transfer the completed fatty acid to sn-glycerol 3-phosphate. The degree of inhibition depended upon the species of donor acyl chain. Utilization of cis-vaccenoyl-ACP by the sn-glycerol-3-phosphate acyltransferase was inhibited to a much greater extent by apo-ACP than was utilization of palmitoyl-ACP. 1-Acyl glycerol-3-phosphate acyltransferase was also inhibited in vitro by apo-ACP, although not at physiologically relevant concentrations. These in vitro data are supported by in vivo labeling data, which showed a large decrease in cis-vaccenate incorporation into phospholipid during overproduction of ACP, but no decrease in the rate of synthesis of long chain acyl-ACPs. These data indicate that acylation of sn-glycerol 3-phosphate is the major site of inhibition by apo-ACP.


Subject(s)
Acyl Carrier Protein/pharmacology , Apoproteins/pharmacology , Cell Division/drug effects , Escherichia coli , Fatty Acids/metabolism , Glycerol-3-Phosphate O-Acyltransferase/antagonists & inhibitors , Glycerol-3-Phosphate O-Acyltransferase/metabolism , Glycerophosphates/metabolism , Lipid Metabolism , Recombinant Proteins
4.
J Bacteriol ; 177(12): 3593-5, 1995 Jun.
Article in English | MEDLINE | ID: mdl-7768872

ABSTRACT

Siggaard-Andersen and coworkers (M. Siggaard-Andersen, M. Wissenbach, J. Chuck, I. Svendsen, J. G. Olsen, and P. von Wettstein-Knowles, Proc. Natl. Acad. Sci. USA 91:11027-11031, 1994) recently reported the DNA sequence of a gene encoding a beta-ketoacyl-acyl carrier protein synthase from Escherichia coli. These workers assigned this gene the designation fabJ and reported that the gene encoded a new beta-ketoacyl-acyl carrier protein synthase. We report that the fabJ gene is the previously reported fabF gene that encodes the known beta-ketoacyl-acyl carrier protein synthase II.


Subject(s)
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/genetics , Escherichia coli/genetics , Fatty Acids/biosynthesis , Genes, Bacterial , Escherichia coli/enzymology , Molecular Sequence Data
5.
Obstet Gynecol ; 69(3 Pt 2): 477-80, 1987 Mar.
Article in English | MEDLINE | ID: mdl-3492695

ABSTRACT

Diffuse leiomyomatosis of the uterus is a rarely reported condition which has been implicated as a cause of infertility and menorrhagia. We report the first documented case of pregnancy in the presence of this disorder. The course was complicated by cervical incompetence, spontaneous premature rupture of membranes, delivery by cesarean section, and intrapartum hemorrhage necessitating hysterectomy. The literature is reviewed and the clinical significance of this lesion discussed. Finally, speculations are made on the nature of this disorder.


Subject(s)
Leiomyoma/complications , Postpartum Hemorrhage/etiology , Pregnancy Complications, Neoplastic/etiology , Uterine Neoplasms/complications , Adult , Cesarean Section , Female , Humans , Hysterectomy , Leiomyoma/pathology , Postpartum Hemorrhage/surgery , Pregnancy , Pregnancy Complications, Neoplastic/surgery , Uterine Neoplasms/pathology
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