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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

Biochemistry. 2002 Nov 5;41(44):13224-33.
Residue 19 of the parathyroid hormone (PTH) modulates ligand interaction with the juxtamembrane region of the PTH-1 receptor.

Shimizu M, Shimizu N, Tsang JC, Petroni BD, Khatri A, Potts JT Jr, Gardella TJ.

Endocrine Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114, USA.

Recent data suggest that the binding of parathyroid hormone (PTH)-(1-34) to the PTH-1 receptor (P1R) involves a high-affinity interaction between the C-terminal (15-34) domain of the ligand and the amino-terminal extracellular (N) domain of the receptor and a low-affinity interaction between the N-terminal (1-14) portion of PTH and the juxtamembrane (J) region of the receptor, with the latter interaction giving rise to signal transduction. We investigated whether residues C-terminal of position 14 in PTH(1-34) contribute to the J component of the interaction mechanism by comparing the capacity of PTH analogues N-terminally modified to improve J domain affinity and C-terminally truncated at position 14, 20, or 34 to stimulate cAMP formation in COS-7 cells transiently transfected with P1R-delNt, a P1R construct that lacks most of the N domain. In these cells, the potency of [M]PTH(1-34) (M = Ala(1,3,12),Gln(10),Har(11),Trp(14),Arg(19)) was 120-fold greater than that of [M]PTH(1-14) (EC(50)s = 3.0 +/- 0.8 and 360 +/- 90 nM, respectively) but was equal to that of [M]PTH(1-20) (EC(50) = 2.3 +/- 0.3 nM). Reverting the Arg(19) substitution of [M]PTH(1-20) to the native Glu reduced cAMP signaling potency on P1R-delNt by 12-fold (EC(50) of [M]PTH(1-20)-Glu(19) = 27 +/- 4 nM), and it decreased the analog's capacity to inhibit the binding of the J domain-selective radioligand, (125)I-[Aib(1,3),Nle(8),M,Tyr(21)]ratPTH(1-21), to the full-length P1R stably expressed in LLC-PK1 cells by 40-fold. The Glu(19) --> Arg modification, however, did not affect the capacity of PTH(15-31) to inhibit the binding of the N domain-selective radioligand (125)I-bPTH(3-34) to the full-length receptor. The overall data suggest that residues (15-20) of PTH, and particularly residue 19, contribute to the capacity of the N-terminal portion of the ligand to interact with the juxtamembrane region of the receptor. The NMR data presented in the accompanying manuscript suggests that this role could involve intramolecular effects on secondary structure in the N-terminal portion of the ligand.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12403624&dopt=Abstract

Biochem J. 2003 Feb 1;369(Pt 3):453-60.
Sorting of carboxypeptidase E to the regulated secretory pathway requires interaction of its transmembrane domain with lipid rafts.

Zhang CF, Dhanvantari S, Lou H, Loh YP.

Section on Cellular Neurobiology, Laboratory of Developmental Neurobiology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-4480, USA.

Carboxypeptidase E (CPE) functions as a regulated secretory pathway sorting receptor for several prohormones, including pro-opiomelanocortin (POMC), proenkephalin and proinsulin. The association of CPE with lipid rafts in the trans -Golgi network and secretory granule membranes is necessary for its sorting receptor function. We now provide evidence that a domain within the C-terminal 25 residues of CPE functions as a signal for both raft association and the sorting of CPE to the regulated secretory pathway. A fusion protein containing the extracellular domain of the human interleukin-2 receptor Tac (N-Tac) and the C-terminal 25 amino acids of CPE was transfected into Neuro2A cells. This fusion protein floated in sucrose density gradients, indicating raft association, and co-localized with chromogranin A (CGA), a secretory granule marker. To define further a minimum sequence required for raft association and sorting, deletion mutants of CPE that lacked the C-terminal four or 15 residues (CPE-Delta4 and CPE-Delta15 respectively) were transfected into a clone of CPE-deficient Neuro2A cells. In contrast with full-length CPE, neither CPE-Delta4 nor CPE-Delta15 floated in sucrose density gradients. The sorting of both CPE-Delta4 and CPE-Delta15 to the regulated secretory pathway was impaired, as indicated by significantly increased basal secretion and a lack of response to stimulation. Additionally, there was a significant decrease in the co-localization of mutant CPE immunofluorescence with CGA when compared with full-length CPE. Finally, the sorting of the prohormone POMC to the regulated pathway was impaired in cells transfected with either CPE-Delta4 or CPE-Delta15. We conclude that the sorting of CPE to the regulated secretory pathway in endocrine cells is mediated by lipid rafts, and that the C-terminal four residues of CPE, i.e. Thr(431)-Leu-Asn-Phe(434), are required for raft association and sorting.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12403651&dopt=Abstract

Neuropeptides. 1998 Jun;32(3):211-4.
Alcoholism abolishes the effects of melatonin on growth hormone secretion in humans.

Coiro V, Vescovi PP.

Centro di Alcologia-Istituto di Clinica Medica Generale e Terapia Medica, Parma, Italy.

Chronic alcohol consumption profoundly affects hypothalamic-pituitary function. The present study was performed in order to establish whether alcoholism modifies the effects of melatonin (MEL) on the neuroendocrine control of growth hormone (GH) secretion. For this purpose, the effects of oral administration of 12 mg MEL or placebo on basal and hypoglycemia-stimulated GH secretion were tested in nine (40-52-year-old) alcoholic men after 10-31 days of abstinence and in nine age- and weight-matched normal controls. Hypoglycemia was induced with an intravenous bolus injection of 0.15 IU/kg body weight of insulin. MEL but not placebo administration induced a small, but significant increase in basal GH secretion in the normal controls. In contrast, neither MEL nor placebo treatment significantly changed the basal serum GH levels in alcoholic men. Both groups showed a similar hypoglycemic pattern after insulin administration. The GH response to insulin-induced hypoglycemia was significantly lower in alcoholic than in normal subjects. MEL administration significantly reduced hypoglycemia-induced GH rise in the normal controls, but not in alcoholic patients. These data show that alcoholism not only reduces the GH response to insulin-induced hypoglycemia, but also abolishes MEL actions on basal and hypoglycemia-stimulated GH secretion.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10189054&dopt=Abstract

J Biol Chem. 2002 Dec 27;277(52):50510-9. Epub 2002 Oct 25.
Metalloprotease-mediated GH receptor proteolysis and GHBP shedding. Determination of extracellular domain stem region cleavage site.

Wang X, He K, Gerhart M, Huang Y, Jiang J, Paxton RJ, Yang S, Lu C, Menon RK, Black RA, Baumann G, Frank SJ.

Department of Medicine, University of Alabama at Birmingham, Alabama 35294, USA.

Growth hormone-binding protein (GHBP) is complexed to a substantial fraction of circulating GH. In humans, rabbits, and other species, GHBP derives from proteolytic shedding of the GH receptor (GHR) extracellular domain. In cell culture studies, stimuli such as phorbol ester, platelet-derived growth factor, or serum induce GHR proteolysis, which concomitantly yields shed GHBP in cell supernatants and a cell-associated cytoplasmic domain-containing GHR remnant. This process is sensitive to metalloprotease inhibition, and genetic reconstitution studies identify tumor necrosis factor-alpha converting enzyme (TACE/ADAM-17), a transmembrane metalloprotease, as a GHR sheddase. Stimuli that induce GHR proteolysis render cells less responsive to GH, but the mechanism(s) of this desensitization is not yet understood. In this study, we mapped the rabbit (rb) GHR cleavage site. We adenovirally expressed a C-terminal epitope-tagged rbGHR lacking most of its cytoplasmic domain, purified the remnant protein induced by the phorbol ester, PMA, and derived the cleavage site by N-terminal sequencing of the purified remnant. The N-terminal sequence, (239)FTCEEDFR(246), matched perfectly the rbGHR and suggests that cleavage occurs eight residues from the membrane in the proximal extracellular domain stem region. Deletion and alanine substitution mutagenesis indicated that, similar to other TACE substrates, the spacing of residues in this region, more than their identity, influences GHR cleavage susceptibility. Further, we determined that PMA pretreatment desensitized a cleavage-sensitive GHR mutant, but not a cleavage-insensitive mutant, to GH-induced JAK2 activation. These results suggest that inducible GHR proteolysis can regulate GH signaling.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12403792&dopt=Abstract

Mol Endocrinol. 2002 Nov;16(11):2413-25.
Neuron-restricted expression of the rat gonadotropin-releasing hormone gene is conferred by a cell-specific protein complex that binds repeated CAATT elements.

Kelley CG, Givens ML, Rave-Harel N, Nelson SB, Anderson S, Mellon PL.

Department of Reproductive Medicine, Center for the Study of Reproductive Biology and Disease, University of California, San Diego, La Jolla, California 92093-0674, USA.

GnRH gene expression is restricted to a tiny population of neurons scattered throughout the mediobasal hypothalamus. The combination of a 300-bp enhancer and the 173-bp promoter from the rat GnRH gene can confer this narrow specificity in transgenic mice and in transfections of hypothalamic GT1-7 cells. In the present study, we identify repeated CAATT elements in the 3' region of the rat GnRH enhancer that bind a tissue-restricted protein complex and play a significant role in cell-restricted expression of the GnRH gene. Deletions of multiple repeats demonstrate their importance in transcriptional activity. In fact, even mutation of a single repeat reduces expression. This reduction can be compensated by the conserved GnRH promoter, which also contains such elements and binds this protein complex. In Southwestern analysis, three proteins from GT1-7 nuclear extract bind to the CAATT element, and these proteins are not found in NIH3T3 cells. This cell-specific protein complex has properties of the Q50 homeodomain family of transcription factors and binds to as many as seven binding sites in the enhancer and promoter to play a key role in GnRH gene expression in the hypothalamus.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12403831&dopt=Abstract

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