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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

Horm Behav. 1999 Feb;35(1):81-9.
Steroid hormones and paternal care in the plainfin midshipman fish (Porichthys notatus).

Knapp R, Wingfield JC, Bass AH.

Section of Neurobiology and Behavior, Cornell University, Ithaca, New York, 14853, USA.

The present study investigated the relationship between plasma steroid hormone levels and the expression ofpaternal behavior in the plainfin midshipman fish (Porichthys notatus), where males may simultaneously care for multiple clutches in different stages of development. Blood samples were collected from free-living parental males during that part of the breeding season when males may be found in various stages of parental care. Plasma 11-ketotestosterone levels were significantly higher in males with empty nests and nests containing only eggs than in males with nests containing embryos. All males with nests containing embryos had undetectable testosterone levels, whereas testosterone levels were detectable in many males with empty nests or nests containing only eggs. Estradiol levels were detectable in only a few males from nests with no eggs or nests containing only eggs. Cortisol levels were not correlated with stage of paternal care or with handling time. These results follow the frequently reported vertebrate pattern of declining androgen levels over the course of the breeding season or during the period of parental care. However, many male midshipman guarding nests containing only eggs had androgen levels similar to those of males whose nests contained no offspring. Thus the pattern of androgen levels exhibited by reproductively active parental male midshipman may reflect a compromise between investment in paternal care versus courtship and/or territoriality. 1999 Academic Press.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10049606&dopt=Abstract

J Neuroendocrinol. 1999 Feb;11(2):115-20.
Induction of pituitary cytokine transcripts by peripheral lipopolysaccharide.

Whiteside MB, Quan N, Herkenharn M.

Section on Functional Neuroanatomy, National Institute of Mental Health, Bethesda 20892-4070, USA.

Systemically administered lipopolysaccharide (LPS) elicits profound changes in pituitary hormone secretion. Pro-inflammatory cytokines have been proposed as mediators of these responses. In this study, we used in-situ hybridization histochemistry to investigate LPS-induced cytokine gene expression in the rat pituitary. After i.p. or i.v. injection of various doses of LPS, mRNA for the immediate-early gene IkappaBu (an inhibitor of NF-kappaB, a transcription factor that regulates the expression of many pro-inflammatory cytokines) was induced in the anterior lobe as early as 0.5 h. The induced IkappaBalpha mRNA expression peaked at 1 h. In the posterior lobe, IkappaBalpha mRNA was first induced at 0.5 h and peaked at 2 h. A similar spatiotemporal pattern of interleukin-1b (IL-1) mRNA induction was observed. In addition, at 2 h after injection, TNFalpha, IL-1beta converting enzyme (ICE), and IL-1 receptor antagonist (IL-1RA) mRNAs were induced in both anterior and posterior lobes. Type 1 IL-1 receptor (IL-1R1) mRNA was constitutively expressed in the pituitary, and its expression level did not change after the LPS injection. Interestingly, the mRNA coding for glial fibrillary acidic protein (GFAP), an astrocyte marker, was selectively induced in the posterior lobe at 2 h after LPS injection, suggesting that LPS affects pituicyte function. Together, these results suggest that LPS acts directly on the pituitary to rapidly induce cytokine expression. Locally synthesized cytokines may activate cytokine receptor bearing cells to modulate the endocrine activities of the pituitary.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10048466&dopt=Abstract

J Clin Endocrinol Metab. 1999 Feb;84(2):761-7. ["Cited in Books","window.top.location='/entrez/query.fcgi?tool=pmcited&cmd=search&db=books&term=10022450[pmid]'","",""],
Pituitary tumor transforming gene (PTTG) expression in pituitary adenomas.

Zhang X, Horwitz GA, Heaney AP, Nakashima M, Prezant TR, Bronstein MD, Melmed S.

Cedars-Sinai Research Institute-University of California School of Medicine, Los Angeles 90048, USA.

We recently cloned a novel pituitary tumor transforming gene (PTTG). Here we report PTTG expression in human pituitary adenomas and in normal pituitary tissue. In situ hybridization revealed PTTG expression in nonfunctioning and in GH-secreting adenomas but not in normal pituitary tissue. Using a more sensitive detection method, RT-PCR, low level PTTG expression was detected in normal pituitary. However, when expression levels in normal pituitary tissue were compared with those in 54 pituitary tumors using comparative reverse transcription polymerase chain reaction (RT-PCR), we found that most tumor samples expressed higher levels of PTTG. More than 50% PTTG increases were observed in 23 of 30 nonfunctioning pituitary tumors, all 13 GH-producing tumors, 9 of 10 prolactinomas, and 1 ACTH-secreting tumor, with more than 10-fold increases evident in some tumors. Furthermore, higher PTTG expression (P = 0.03) was observed in hormone-secreting tumors that had invaded the sphenoid bone (stages III and IV; 95% CI 3.118-9.715) compared with hormone-secreting tumors that were confined to the pituitary fossa (stages I and II; 95% CI 1.681-3.051). Therefore, PTTG abundance is a molecular marker for invasiveness in hormone-secreting pituitary tumors. The ubiquitous and prevalent expression of pituitary adenoma PTTG suggests that PTTG plays a role in pituitary tumorigenesis and invasiveness.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10022450&dopt=Abstract

J Biol Chem. 1999 Feb 26;274(9):5738-45.
A plant 126-kDa phosphatidylinositol 4-kinase with a novel repeat structure. Cloning and functional expression in baculovirus-infected insect cells.

Xue HW, Pical C, Brearley C, Elge S, Muller-Rober B.

Max Planck Institute of Molecular Plant Physiology, Karl-Liebknecht-Strabetae 25, Haus 20, D-14476 Golm/Potsdam, Germany.

Phosphatidylinositol metabolism plays a central role in signaling pathways in animals and is also believed to be of importance in signal transduction in higher plants. We report here the molecular cloning of a cDNA encoding a previously unidentified 126-kDa phosphatidylinositol (PI) 4-kinase (AtPI4Kbeta) from the higher plant Arabidopsis thaliana. The novel protein possesses the conserved domains present in animal and yeast PI 4-kinases, namely a lipid kinase unique domain and a catalytic domain. An additional domain, approximately 300 amino acids long, containing a high percentage (46%) of charged amino acids is specific to this plant enzyme. Recombinant AtPI4Kbeta expressed in baculovirus-infected insect (Spodoptera frugiperda) cells phosphorylated phosphatidylinositol exclusively at the D4 position of the inositol ring. Recombinant protein was maximally activated by 0.6% Triton X-100 but was inhibited by adenosine with an IC50 of approximately 200 microM. Wortmannin at a concentration of 10 microM inhibited AtPI4Kbeta activity by approximately 90%. AtPI4Kbeta transcript levels were similar in all tissues analyzed. Light or treatment with hormones or salts did not change AtPI4Kbeta transcript levels to a great extent, indicating constitutive expression of the AtPI4Kbeta gene.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10026194&dopt=Abstract

Biochem Pharmacol. 1999 Mar 15;57(6):597-601.
Interaction of human estrogen receptors alpha and beta with the same naturally occurring estrogen response elements.

Hyder SM, Chiappetta C, Stancel GM.

Department of Integrative Biology, Pharmacology and Physiology, University of Texas Medical School, Houston 77030, USA. shydearmr1.med.uth.tmc.edu

Estrogen receptors are derived from two different gene products referred to as estrogen receptor-alpha (ER-alpha) and ER-beta. Both receptors bind to the consensus estrogen response element (ERE) present in the vitellogenin gene, but their binding to hormone response elements present in other estrogen responsive genes has not been reported yet. Using in vitro expressed human receptors, we now show that ER-beta binds to a panel of six endogenous hormone response elements (vitellogenin, c-fos, c-jun, pS2, cathepsin D, and choline acetyltransferase) already known to bind ER-alpha and confer estrogen inducibility to reporter constructs. Binding of ER-alpha and ER-beta occurred at similar DNA concentrations for some EREs, but different DNA concentrations were required to form complexes of the two receptors with other elements. These results illustrate for the first time by direct receptor-DNA binding studies that both ER-alpha and ER-beta bind to a number of EREs present in endogenous hormone regulated genes, and further suggest that the two forms of the receptor display different patterns of affinities for naturally occurring hormone response elements.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10037443&dopt=Abstract

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