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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

Endocrinology. 2003 Jul;144(7):3046-57.
Inhibition of spontaneous and androgen-induced prostate growth by a nonhypercalcemic calcitriol analog.

Crescioli C, Ferruzzi P, Caporali A, Mancina R, Comerci A, Muratori M, Scaltriti M, Vannelli GB, Smiroldo S, Mariani R, Villari D, Bettuzzi S, Serio M, Adorini L, Maggi M.

Department of Clinical Physiopathology, University of Florence, Viale Pieraccini 6, 50139 Florence, Italy.

We have recently found that analog V (BXL-353, a calcitriol analog) inhibits growth factor (GF)-stimulated human benign prostate hyperplasia (BPH) cell proliferation by disrupting signal transduction, reducing Bcl-2 expression, and inducing apoptosis. We now report that BXL-353 blocks in vitro and in vivo testosterone (T) activity. BPH cells responded to T and dihydrotestosterone (DHT) with dose-dependent growth and reduced apoptosis. Exposure of BPH cells to BXL-353 significantly antagonized both T- and DHT-induced proliferation and induced apoptosis, even in the presence of T. To verify whether BXL-353 reduced prostate growth in vivo, we administered it orally to either intact or castrated rats, supplemented with T enanthate. Nonhypercalcemic doses of BXL-353 time- and dose-dependently reduced the androgen effect on ventral prostate weight, similarly to finasteride. Comparable results were obtained after chronic administration of BXL-353 to intact rats. Clusterin (an atrophy marker) gene and protein were up-regulated by BXL-353 in rat prostate, and nuclear fragmentation was widely present. The antiandrogenic properties of BXL-353 did not interfere with pituitary and testis function, as assessed by serum determination of rat LH and T. BXL-353 did not compete for androgen binding to BPH homogenates and failed to inhibit 5alpha-reductase type 1 and type 2 activities. In conclusion, BXL-353 blocks in vitro and in vivo androgen-stimulated prostate cell growth, probably acting downstream from the androgen receptor, without affecting calcemia or sex hormone secretion. BXL-353 and other vitamin D(3) analogs might thus represent an interesting class of compounds for treating patients with BPH.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12810561&dopt=Abstract

Endocrinology. 2003 Jul;144(7):3138-47.
Sp3/Sp1 in the parathyroid gland: identification of an Sp1 deoxyribonucleic acid element in the parathyroid hormone promoter.

Alimov AP, Langub MC, Malluche HH, Koszewski NJ.

Division of Nephrology, Bone and Mineral Metabolism, University of Kentucky Medical Center, 800 Rose Street, Lexington, KY 40536-0298, USA.

A highly conserved region in the PTH promoter was identified using the basic local alignment search tool (BLAST) 2 Sequences comparison. Strong specific complexes were observed with a DNA probe that contained much of the computer-derived conserved sequence in the EMSA using bovine parathyroid gland (bPTG) nuclear extracts. Ethylation interference footprinting indicated that the major complex made contacts to a sequence strikingly similar to an Sp1 binding site. Sp3 was evident in the major DNA-binding complexes, whereas the contribution by Sp1 was substantially weaker. Specific binding by additional unidentified bPTG nuclear factors was also evident. Immunocytochemical and Western blotting analyses established that Sp1 and Sp3 were positively localized in the nuclei of chief cells of the bPTG and of the expected molecular weights, with particularly robust expression of Sp3. Affinity DNA-binding experiments using the bovine PTH Sp1 element demonstrated specific recovery of intact Sp3 and Sp1 proteins, although a significant portion of both proteins failed to interact with the affinity-tagged DNA. Treatment of the bPTG nuclear extracts with phosphatase, however, significantly increased the DNA-binding capacity of the Sp1/Sp3 complexes. Finally, transient transfection analysis indicated that the bovine Sp1-like element acted as an enhancer of heterologous gene expression. The present study identified an Sp1 element in the promoter of the PTH gene that represents a complex DNA-binding site involving interactions primarily with Sp1/Sp3 proteins. The data, therefore, highlight the likely involvement of the Sp family in regulating PTH gene expression through interactions with an Sp1 DNA element in the hormone's promoter.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12810570&dopt=Abstract

Endocrinology. 2003 Jul;144(7):3182-95.
Nuclear translocation and retention of growth hormone.

Mertani HC, Raccurt M, Abbate A, Kindblom J, Tornell J, Billestrup N, Usson Y, Morel G, Lobie PE.

Centre National de la Recherche Scientifique, Unite Mixte de Recherche 5123 Physiologie Energetique Cellulaire et Moleculaire, Universite Claude Bernard, 69622 Lyon I, France.

We have previously demonstrated that GH is subject to rapid receptor-dependent nuclear translocation. Here, we examine the importance of ligand activation of the GH-receptor (GHR)-associated Janus kinase (JAK) 2 and receptor dimerization for hormone internalization and nuclear translocation by use of cells stably transfected with cDNA for the GHR. Staurosporine and herbimycin A treatment of cells did not affect the ability of GH to internalize but resulted in increased nuclear accumulation of hormone. Similarly, receptor mutations, which prevent the association and activation of JAK2, did not affect the ability of the hormone to internalize or translocate to the nucleus but resulted in increased nuclear accumulation of GH. These results were observed both by nuclear isolation and confocal laser scanning microscopy. Staurosporine treatment of cells in which human GH (hGH) was targeted to the cytoplasm (removal of secretion sequence) or to the nucleus (addition of the nuclear localization sequence of SV40 large T antigen) resulted in preferential accumulation of hGH in the nucleus. We further investigated the requirement of receptor dimerization for GH nuclear translocation using the non-receptor-dimerizing hGH antagonist, hGH-G120R, conjugated to fluorescein isothiocyanate. Confocal laser scanning microscopy demonstrated efficient internalization of both hGH and hGH-G120R but lack of nuclear translocation of hGH-G120R. Thus, we conclude that activation of JAK2 kinase and the subsequent tyrosine phosphorylation is not required for nuclear translocation of GH but is pivotal for the removal of the hormone from the nucleus, and that GH translocates into the nucleus in a GHR dimerized-dependent fashion.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12810575&dopt=Abstract

Endocrinology. 2003 Jul;144(7):3225-36.
Central orexin A has site-specific effects on luteinizing hormone release in female rats.

Small CJ, Goubillon ML, Murray JF, Siddiqui A, Grimshaw SE, Young H, Sivanesan V, Kalamatianos T, Kennedy AR, Coen CW, Bloom SR, Wilson CA.

Department of Obstetrics, St. George's Hospital Medical School, Cranmer Terrace, London SW17 0RE, United Kingdom.

Orexin A stimulates GnRH release from hypothalamic explants in vitro. The sites of action of orexin A in the regulation of LH release have been investigated in vivo in ovariectomized rats that were given vehicle or estradiol benzoate (EB), with or without an injection of progesterone 48 h later. Orexin A was administered intrahypothalamically under Saffan anesthesia, 50 h after the EB or vehicle; its effects on plasma LH levels were monitored in sequential blood samples. Orexin A (1.0 microg/side) injected into the rostral preoptic area (rPOA) at the level of the organum vasculosum of the lamina terminalis had a stimulatory effect on LH release in EB-treated ovariectomized rats. When orexin A was injected into the medial POA (mPOA) or the arcuate/median eminence, it had an inhibitory effect on the LH surge that occurs in ovariectomized rats primed with EB plus progesterone. Orexin A injected into the mPOA also reduced LH levels in ovariectomized rats untreated with ovarian steroids. Both the stimulatory and inhibitory effects of orexin A were antagonized by SB334867A, a selective orexin 1 receptor antagonist. Furthermore, when given alone into the rPOA, this antagonist attenuated the LH surge induced by EB plus progesterone. Thus, orexin appears to have a dual effect on LH release, being stimulatory in the rPOA and inhibitory in the mPOA or arcuate/median eminence. Both effects may be mediated, at least in part, by the orexin 1 receptor. Double label immunohistochemistry revealed close appositions between orexin A immunoreactive varicosities and a small proportion of GnRH cell bodies in the rPOA. It is suggested that the stimulatory effect of orexin A on LH release may involve direct actions on GnRH neurons.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12810579&dopt=Abstract

Gen Comp Endocrinol. 1999 May;114(2):181-90.
Somatolactin in the white sturgeon and African lungfish and its evolutionary significance.

Amemiya Y, Sogabe Y, Nozaki M, Takahashi A, Kawauchi H.

School of Fisheries Sciences, Kitasato University, Sanriku, Iwate, 022-0101, Japan.

Somatolactin (SL) is a newly characterized pituitary hormone belonging to the growth hormone-prolactin family. Until now SL has been identified only in teleosts, the most highly derived ray-finned fishes. We report here the cloning of SL cDNAs from two species of bony fish, the white sturgeon (Acipenser transmontanus) and the African lungfish (Protopterus annectens). Overlapping partial cDNA clones corresponding to teleost SLs were amplified by polymerase chain reaction (PCR) from either single-strand or double-strand cDNA from pituitary glands. Excluding the poly(A) tail, the sturgeon SL cDNA is 881 base pairs (bp). This is comparable to 1.0 kb estimated by Northern blot analysis. It contains a 696-bp open reading frame encoding a prehormone of 232 amino acids (aa) with a signal peptide of 24 aa and a mature protein of 208 aa. Excluding the poly(A) tail, the lungfish SL cDNA is 938 bp. This is comparable to 1.1 kb estimated by Northern blot analysis. It contains a 696-bp open reading frame encoding a prehormone of 232 aa with a signal peptide of 26 aa and a mature protein of 206 aa. The deduced aa sequences of sturgeon and lungfish SLs show 76-60% and 65-54% identity with teleost SLs, respectively. These values are significantly higher than the 30% identity with nonteleostean growth hormones and prolactins. Immunostaining of sturgeon pituitary with anti-salmon SL serum demonstrated that the SL cells were localized in the pars intermedia, as in teleosts. The present results demonstrate that the SL gene is present in two divergent lineages, the Actinopterygii (Chondrostei: white sturgeon) and the Sarcopterygii (Dipnoi: African lungfish). 1999 Academic Press.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10208767&dopt=Abstract

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