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Pathogen research abs 1 || Pathogen research abs 2 || Pathogen research abs 3 || Pathogen research abs 4 || Pathogen research abs 5 || Hormone and endocrine research abs 1 || Hormone and endocrine research abs 2 || Hormone and endocrine research abs 3 || Hormone and endocrine research abs 4 || Hormone and endocrine research abs 5

Cancer Epidemiol Biomarkers Prev. 1999 Feb;8(2):147-51.
Laboratory assay reproducibility of serum estrogens in umbilical cord blood samples.

Shibata A, Lee MM, Meyer PB.

Department of Health Research and Policy, Stanford University School of Medicine, California 94305-5405, USA.

We evaluated the reproducibility of laboratory assays for umbilical cord blood estrogen levels and its implications on sample size estimation. Specifically, we examined correlation between duplicate measurements of the same blood samples and estimated the relative contribution of variability due to study subject and assay batch to the overall variation in measured hormone levels. Cord blood was collected from a total of 25 female babies (15 Caucasian and 10 Chinese-American) from full-term deliveries at two study sites between March and December 1997. Two serum aliquots per blood sample were assayed, either at the same time or 4 months apart, for estrone, total estradiol, weakly bound estradiol, and sex hormone-binding globulin (SHBG). Correlation coefficients (Pearson's r) between duplicate measurements were calculated. We also estimated the components of variance for each hormone or protein associated with variation among subjects and variation between assay batches. Pearson's correlation coefficients were >0.90 for all of the compounds except for total estradiol when all of the subjects were included. The intraclass correlation coefficient, defined as a proportion of the total variance due to between-subject variation, for estrone, total estradiol, weakly bound estradiol, and SHBG were 92, 80, 85, and 97%, respectively. The magnitude of measurement error found in this study would increase the sample size required for detecting a difference between two populations for total estradiol and SHBG by 25 and 3%, respectively.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10067812&dopt=Abstract

Can J Physiol Pharmacol. 1998 Sep;76(9):843-9.
The effect of estradiol on output of adrenocorticotropin and prolactin by fetal sheep anterior pituitary cells.

Wang S, Matthews SG, Yang K, Challis JR.

Department of Physiology, University of Toronto, Ontario, Canada. s.wantoronto.ca

We examined the hypothesis that estradiol (E2) would affect fetal anterior pituitary corticotroph and lactotroph function in vitro, and that any effects would be influenced by gestational age. Anterior pituitary cells from fetal sheep at day 129 (n = 4) and at day 139 (n = 5) of gestation were cultured. After 96 h in culture, cells were treated for 18 h with E2 concentrations ranging from 0 to 1000 nM, in the presence or absence of 100 nM of corticotropin-releasing hormone (CRH), cortisol, arginine vasopressin (AVP), or CRH and cortisol, to examine their effects on corticotroph function. Cells were also treated with bromocriptine or increasing concentrations of E2 to study their effects on lactotroph function. Immunoreactive (ir) adrenocorticotropin (ACTH) and prolactin in the culture medium were measured by radioimmunoassay. Levels of cellular pro-opiomelanocortin (POMC) mRNA and prolactin mRNA were determined by in situ hybridization. Immunohistochemistry was used to determine the percentage of cells that were immunopositive for ACTH (corticotrophs) or prolactin (lactotrophs). ACTH output was stimulated by CRH treatment at day 139 but not at day 129 of gestation, and cortisol attenuated this response. ACTH output by cells cultured with 10 nM E2 and 100 nM CRH, at 139 days of gestation, was greater than with CRH alone (p < 0.05). E2 did not affect basal ACTH output or ACTH output with any other treatment or levels of POMC mRNA. Prolactin output was not affected by E2 treatment. Bromocriptine significantly decreased prolactin output but not levels of prolactin mRNA. We conclude that E2 may affect CRH-stimulated fetal sheep pituitary corticotroph function late in gestation, but only within a narrow, physiological range of concentration.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10066133&dopt=Abstract

Am J Med Genet. 1999 Feb 19;82(5):382-4.
Adrenal insufficiency in Smith-Lemli-Opitz syndrome.

Andersson HC, Frentz J, Martinez JE, Tuck-Muller CM, Bellizaire J.

Human Genetics Program, Hayward Genetics Center, Tulane University Medical School, New Orleans, Louisiana 70112, USA. handermcpop.tmc.tulane.edu

We describe three unrelated patients with adrenal insufficiency and RSH or Smith-Lemli-Opitz syndrome (SLOS), a disorder due to deficient synthesis of cholesterol. These patients presented with hyponatremia, hyperkalemia, and decreased aldosterone-to-renin ratio, which is a sensitive measure of the renin-aldosterone axis. All patients had profound serum total cholesterol deficiency (14-31 mg/dl) and marked elevation of 7-dehydrocholesterol (10-45 mg/ dl). Two patients were newborn infants with 46, XY karyotypes and complete failure to masculinize; one of these patients also had cortisol deficiency. Both patients died within 10 days of birth of cardiopulmonary complications while on adrenal replacement therapy. The third patient diagnosed with SLOS at birth presented at age 7months with fever and diarrhea and was noted to have profound hyponatremia. This patient is maintaining normal serum electrolytes on mineralocorticoid replacement. We conclude that adrenal insufficiency may be a previously undetected and treatable manifestation in SLOS. We hypothesize that deficiency of cholesterol, an adrenal hormone precursor, may lead to insufficient synthesis of adrenal steroid hormones.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10069708&dopt=Abstract

Genes Dev. 2003 Feb 1;17(3):410-8.
AFP is a novel negative regulator of ABA signaling that promotes ABI5 protein degradation.

Lopez-Molina L, Mongrand S, Kinoshita N, Chua NH.

Laboratory of Plant Molecular Biology, The Rockefeller University, New York, New York 10021-6399, USA.

Plants have evolved protective mechanisms to ensure their survival when threatened by adverse environmental conditions during their transition to autotrophic growth. During germination, there is a 2- to 3-d period during which a plant can execute growth arrest when challenged by water deficit. This postgermination developmental checkpoint is signaled by the stress hormone abscisic acid (ABA), which induces the expression of the bZIP transcription activator ABI5. The growth arrest efficiency depends on ABI5 levels, and abi5 mutants are ABA-insensitive and unable to execute the ABA-mediated growth arrest. Here we show that a novel ABI5-interacting protein, designated as AFP, can form high molecular weight (Mr) complexes with ABI5 in embryo-derived extracts. Like ABI5, ABI five binding protein (AFP) mRNA and protein levels are induced by ABA during seed germination. Two different afp mutant alleles (afp-1 and afp-2) are hypersensitive to ABA, whereas transgenic plants overexpressing AFP are resistant; in these plants, AFP and ABI5 protein levels are inversely correlated. Genetic analysis shows that abi5-4 is epistatic to afp-1, indicating the ABA hypersensitivity of afp mutants requires ABI5. Proteasome inhibitor studies show that ABI5 stability is regulated by ABA through ubiquitin-related events. When expressed together, AFP and ABI5 are colocalized in nuclear bodies, which also contain COP1, a RING motif protein. Our results suggest that AFP attenuates ABA signals by targeting ABI5 for ubiquitin-mediated degradation in nuclear bodies.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12569131&dopt=Abstract

Cell Mol Life Sci. 1999 Jan;55(1):121-7.
Juvenile hormone regulation of HMG-R gene expression in the bark beetle Ips paraconfusus (Coleoptera: Scolytidae): implications for male aggregation pheromone biosynthesis.

Tittiger C, Blomquist GJ, Ivarsson P, Borgeson CE, Seybold SJ.

Department of Biochemistry/330, University of Nevada, Reno 89557, USA. cred.unr.edu

Juvenile hormone III (JH III) induces acyclic isoprenoid pheromone production in male Ips paraconfusus. A likely regulatory enzyme in this process is 3-hydroxy-e-methylglutaryl-CoA reductase (HMG-R). To begin molecular studies on pheromone production, a 1.16-kb complementary DNA representing approximately one-third of I. paraconfusus HMG-R was isolated by polymerase chain reaction and sequenced. The predicted translation product is 59% and 75% identical to the corresponding portion of HMG-R from the fruit fly, Drosophila melanogaster, and the German cockroach, Blattella germanica, respectively. Northern blots show that topical application of JH III increases HMG-R transcript levels in male thoraces in an apparent dose- and time-dependent manner. These data support the model that JH III raises HMG-R transcript levels, resulting in increased activity of the isoprenoid pathway and de novo pheromone production.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10065157&dopt=Abstract

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