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J Am Acad Child Adolesc Psychiatry. 2002 Aug;41(8):999-1006; discussion 1007-9.
Noradrenergic and serotonergic neuroendocrine responses in prepubertal, peripubertal, and postpubertal rats pretreated with desipramine and sertraline.

Carrey NJ, Dursun S, Clements R, Renton K, Waschbusch D, MacMaster FP.

Department of Psychiatry, Dalhousie University, Halifax, Nova Scotia, Canada. Normand.Carrewk.nshealth.ca

OBJECTIVE: To explore whether developmental status of neurotransmitter systems may affect response to antidepressant treatment. This study investigated whether younger animals, compared with mature animals, showed the same neuroendocrine response to challenge drug probes when pretreated with a serotonergic or noradrenergic antidepressant. METHOD: Prepubertal, pubertal, and adult rats were pretreated with low- or high-dose sertraline or desipramine for 14 days. Animals were then challenged with a noradrenergic probe (clonidine for desipramine-treated animals) or a serotonergic probe (fenfluramine for sertraline-treated animals). The neurohormonal response of growth hormone to the clonidine challenge and prolactin to the fenfluramine challenge was then measured. RESULTS: In animals challenged with fenfluramine, the postpubertal control group showed a significantly higher prolactin response to fenfluramine than postpubertal animals pretreated with low- or high-dose sertraline. No differences were found in the pubertal or prepubertal group. In animals challenged with clonidine, there was a significant age by treatment interaction effect for the prepubertal group pretreated with high doses of desipramine (less growth hormone secretion) but not for the peri- or postpubertal groups. CONCLUSIONS: These data indicate neurodevelopmental factors may play a role in the functional physiology of neurotransmitter systems, which in turn may affect response to psychotropics.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12162636&dopt=Abstract

J Anim Sci. 2002 Jul;80(7):1962-9.
Inability of heterologous growth hormone (GH) to regulate GH binding protein in GH-transgenic swine.

Cifone D, Dominici FP, Pursel VG, Turyn D.

Instituto de Quimica y Fisicoquimica Biologicas, Facultad de Farmacia y Bioquimica, Universidad de Buenos Aires, Argentina.

Transgenic pigs expressing bovine, ovine, or human growth hormone (GH) structural genes fused to mouse metallothionein-I (mMT-bGH), ovine MT (oMT-oGH), or mouse transferrin (mTf-hGH) promoters were used to study the effects of GH on the regulation of serum GH-binding protein (GHBP). In the 14 transgenic pigs studied, circulating concentrations of heterologous GH ranged from 15 to 2,750 ng/mL. Using chromatographic methods, specific binding of GH was detected in serum from normal pigs but was undetectable in serum from all the transgenic pigs used, probably as a result of the high serum concentrations of heterologous GH present in these animals. Thus, to avoid interference of binding by high GH concentrations, serum samples were subjected to immunoblotting using a specific anti-GHBP antibody. A specific 54-kDa band was detected in normal pig serum as well as in sera from mMT-bGH, oMT-oGH, and mTf-hGH pigs. Additionally, sera from transgenic mMT-bGH pigs and their sibling controls were subjected to immunoprecipitation with an anti-GHBP antibody followed by immunoblotting with the same antibody. With this technique, we detected two specific bands of 53 and 45 kDa that could represent different degrees of glycosylation of GHBP. As determined by densitometric analysis the amount of GHBP in transgenic pig sera was similar to that detected in sera of the respective control animals. The amount of circulating GHBP remained unchanged even in oMT-oGH and mTf-hGH pigs that were exposed from birth to circulating concentrations of GH as high as 2,750 ng/mL. Thus, we conclude that heterologous GH do not act as modulators ofthe serum GHBP in pigs.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12162666&dopt=Abstract

J Anim Sci. 2002 Jul;80(7):1999-2005.
Effects of dietary copper on the expression of lipogenic genes and metabolic hormones in steers.

Lee SH, Engle TE, Hossner KL.

Department of Animal Science, Colorado State University, Fort Collins 80523, USA.

An experiment was conducted to determine the effects of Cu supplementation on performance, subcutaneous adipose tissue mRNA expression of acetyl CoA carboxylase (ACC), stearoyl CoA desaturase (SCD), uncoupling protein 2 (UCP2), and leptin in growing and finishing steers. Forty-eight purebred Angus steers were allotted to one of five treatments: 1) control (no supplemental Cu); 2) 10 mg Cu/kg DM from CuSO4; 3) 10 mg Cu/kg DM from a Cu amino acid complex (Availa Cu); 4) 20 mg Cu/kg DM from CuSO4; 5) 20 mg Cu/kg DM from Availa Cu. Steers were fed an alfalfa hay corn-based diet for 56 d (basal diet contained 7.1 mg Cu/kg DM) and switched to a high-concentrate diet for 144 d (basal diet contained 6.1 mg Cu/kg DM). Blood samples were obtained every 28 d throughout the entire experiment. On d 112 of the finishing period, subcutaneous adipose tissue biopsies were obtained from the tailhead of three animals per treatment and analyzed for ACC, SCD, UCP2, and leptin mRNA expression. Animal performance was not affected by Cu supplementation during the growing phase. Steers receiving 10 mg Cu/kg DM from Availa Cu had higher (P < 0.05) ending body weights and tended (P < 0.10) to have higher ADG than steers receiving 10 mg Cu/kg DM from CuSO4 during the finishing phase. Serum concentrations of nonesterified fatty acid and insulin were not affected by Cu supplementation. Steers receiving supplemental Cu tended (P < 0.11) to have less backfat relative to controls. However, dietary Cu did not influence the level of subcutaneous adipose tissue ACC and SCD mRNA. Neither UCP2 nor leptin gene expression was affected by Cu supplementation. These results indicate that dietary Cu supplementation (10 to 20 mg Cu/kg DM diet) may alter lipid metabolism of subcutaneous adipose tissue; however, it does not seem to affect expression of certain lipogenic genes.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12162670&dopt=Abstract

J Mol Biol. 2002 Aug 16;321(3):537-47.
Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI).

Barbosa Pereira PJ, Segura-Martin S, Oliva B, Ferrer-Orta C, Aviles FX, Coll M, Gomis-Ruth FX, Vendrell J.

Institut de Biologia Molecular de Barcelona, C.I.D. - C.S.I.C., Jordi Girona, 18-26, E-08034, Barcelona, Spain.

Besides their classical role in alimentary protein degradation, zinc-dependant carboxypeptidases also participate in more selective regulatory processes like prohormone and neuropeptide processing or fibrinolysis inhibition in blood plasma. Human pancreatic procarboxypeptidase B (PCPB) is the prototype for those human exopeptidases that cleave off basic C-terminal residues and are secreted as inactive zymogens. One such protein is thrombin-activatable fibrinolysis inhibitor (TAFI), also known as plasma PCPB, which circulates in human plasma as a zymogen bound to plasminogen. The structure of human pancreatic PCPB displays a 95-residue pro-segment consisting of a globular region with an open-sandwich antiparallel-alpha antiparallel-beta topology and a C-terminal alpha-helix, which connects to the enzyme moiety. The latter is a 309-amino acid residue catalytic domain with alpha/beta hydrolase topology and a preformed active site, which is shielded by the globular domain of the pro-segment. The fold of the proenzyme is similar to previously reported procarboxypeptidase structures, also in that the most variable region is the connecting segment that links both globular moieties. However, the empty active site of human procarboxypeptidase B has two alternate conformations in one of the zinc-binding residues, which account for subtle differences in some of the key residues for substrate binding. The reported crystal structure, refined with data to 1.6A resolution, permits in the absence of an experimental structure, accurate homology modelling of TAFI, which may help to explain its properties.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12162965&dopt=Abstract

Biochem Biophys Res Commun. 2002 Aug 16;296(2):383-7.
Endothelin-1 inhibits resistin secretion in 3T3-L1 adipocytes.

Zhong Q, Lin CY, Clarke KJ, Kemppainen RJ, Schwartz DD, Judd RL.

Department of Anatomy, Physiology and Pharmacology, College of Veterinary Medicine, Auburn University, 219 Greene Hall, Auburn, AL 36849-5518, USA.

Resistin is an adipocyte-derived hormone whose role in the development of insulin resistance is controversial. Endothelin-1 (ET-1) is a 21 amino acid peptide demonstrated to possess vasoconstrictor, positive inotropic, mitogenic, and metabolic properties. In numerous disease states, including congestive heart failure, obesity, and diabetes, elevated levels of ET-1 have been reported and are thought to contribute to the pathology of the disease. A recent study demonstrated that ET-1 induces the expression and stimulates the secretion of the adipose tissue-derived hormone leptin. However, the effect of ET-1 on resistin secretion has not been determined. To characterize the effect of ET-1 on resistin secretion, 3T3-L1 fibroblasts were differentiated into adipocytes and allowed to mature for 14 days. Cells were incubated for 24h with ET-1 (1-100 nM), insulin (1-100 nM), insulin+ET-1 (100 nM I+E) or the appropriate vehicle or antagonist. At the end of the incubation period, resistin secretion was determined in the media by immunoblotting and densitometric analysis. ET-1 (1-100 nM) significantly decreased basal resistin secretion by 49% (1 nM), 43% (10nM), and 59% (100 nM). Insulin (1-100 nM) produced a concentration-dependent increase in resistin secretion from 3T3-L1 adipocytes (1 nM-42%, 10nM-55%, and 100 nM-86% vs. control). Insulin-stimulated resistin secretion (100 nM) was almost completely inhibited (94%) by ET-1 (100 nM). The effects of ET-1 on resistin protein secretion were inhibited by co-incubation with the ET(A) receptor antagonist BQ-610. In conclusion, our studies demonstrate that basal and hormonal stimulation of resistin secretion by insulin are inhibited by ET-1. Such findings demonstrate that resistin secretion is regulated in a similar manner to other adipose tissue factors, including leptin, in 3T3-L1 adipocytes. In addition, our findings suggest that vascular factors such as ET-1 may regulate whole body energy metabolism through adipocyte-derived hormones, including leptin and resistin.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12163029&dopt=Abstract

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