<?xml version="1.0" encoding="UTF-8"?>
<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:prism="http://prismstandard.org/namespaces/1.2/basic/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns="http://purl.org/rss/1.0/"><channel rdf:about="http://www.domesticanimalendo.com/?rss=yes"><title>Domestic Animal Endocrinology</title><description>Domestic Animal Endocrinology RSS feed: Current Issue.   
 
 
 Domestic Animal Endocrinology    publishes scientific papers dealing with the study of the endocrine 
physiology of domestic animal species. Those manuscripts utilizing other species as models for clinical or production problems associated 
with domestic animals are also welcome. 
 
Topics covered include: 
 
	classical and reproductive endocrinology  
 	clinical 
and applied endocrinology  
 	regulation of hormone secretion  
 	hormone action  
 	molecular biology  
 	
cytokines  
 	growth factors 
 
</description><link>http://www.domesticanimalendo.com/?rss=yes</link><dc:publisher>Elsevier Inc.</dc:publisher><dc:language>en</dc:language><dc:rights> © 2009 Published by Elsevier Inc. All rights reserved. </dc:rights><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:issn>0739-7240</prism:issn><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:publicationDate>February 2010</prism:publicationDate><prism:copyright> © 2009 Published by Elsevier Inc. All rights reserved. </prism:copyright><prism:rightsAgent>healthpermissions@elsevier.com</prism:rightsAgent><items><rdf:Seq><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009001350/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009001374/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009001003/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS073972400900099X/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009000988/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009000976/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009000964/abstract?rss=yes"/><rdf:li rdf:resource="http://www.domesticanimalendo.com/article/PIIS0739724009000952/abstract?rss=yes"/></rdf:Seq></items></channel><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009001350/abstract?rss=yes"><title>Editorial Board</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009001350/abstract?rss=yes</link><description></description><dc:title>Editorial Board</dc:title><dc:creator></dc:creator><dc:identifier>10.1016/S0739-7240(09)00135-0</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2010-02-01</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2010-02-01</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>i</prism:startingPage><prism:endingPage>i</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009001374/abstract?rss=yes"><title>Table of Contents</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009001374/abstract?rss=yes</link><description></description><dc:title>Table of Contents</dc:title><dc:creator></dc:creator><dc:identifier>10.1016/S0739-7240(09)00137-4</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2010-02-01</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2010-02-01</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>iii</prism:startingPage><prism:endingPage>iii</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009001003/abstract?rss=yes"><title>Visfatin gene expression in chickens is sex and tissue dependent</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009001003/abstract?rss=yes</link><description>Abstract: The present study investigated the expression of visfatin mRNA in various tissues of male and female broiler chickens. We also studied the effect of leptin, cerulenin, and food deprivation, known effectors of energy balance and insulin action, on visfatin gene expression in chickens. Using reverse transcription polymerase chain reaction (RT-PCR) and Northern blot analysis, we detected chicken visfatin mRNA transcript in the kidney, hypothalamus, gizzard, liver, pancreas, proventriculus, breast and leg muscle, ovary, testis, lung, intestine, adipose tissue, and heart. Expression of the visfatin gene in various tissues of male and female chickens was determined by real-time quantitative PCR and found to be tissue and sex dependent. In both sexes, compared to other tissues, the visfatin gene is highly expressed in the muscle. Females exhibited greater (P&lt;0.001) abundance of visfatin mRNA in adipose tissue compared to males, whereas compared to females, males showed greater (P&lt;0.05) visfatin mRNA abundance in the kidney. Also, the regulation of visfatin gene expression by leptin, cerulenin, and food deprivation is tissue specific. Leptin decreased (P&lt;0.05) visfatin mRNA abundance in the liver and hypothalamus, but not in muscle. In contrast, cerulenin increased (P&lt;0.01) visfatin gene expression in the liver and in muscle, but not in the hypothalamus. Interestingly, visfatin mRNA levels increased (P&lt;0.05) in the liver after 24-h food deprivation, but not in muscle or in the hypothalamus of genetically selected fat and lean line chickens. Our results showed that the visfatin gene is ubiquitously expressed in chickens with greater abundance in muscle, and that it is regulated in a tissue-specific manner by energy balance–related factors.</description><dc:title>Visfatin gene expression in chickens is sex and tissue dependent</dc:title><dc:creator>E. Ons, A. Gertler, J. Buyse, E. Lebihan-Duval, A. Bordas, B. Goddeeris, S. Dridi</dc:creator><dc:identifier>10.1016/j.domaniend.2009.08.007</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2009-09-28</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2009-09-28</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>63</prism:startingPage><prism:endingPage>74</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS073972400900099X/abstract?rss=yes"><title>Endothelin-1, endothelin converting enzyme-1 and endothelin receptors in the porcine corpus luteum</title><link>http://www.domesticanimalendo.com/article/PIIS073972400900099X/abstract?rss=yes</link><description>Abstract: Porcine corpora lutea (CL) fail to show a luteolytic response to prostaglandin-F-2α (PGF-2α) (ie, luteolytic sensitivity [LS]) until about day 12-13 of the estrous cycle. Although little is known of the control of LS in any species, endothelin-1 (EDN1) is believed to play a role in LS control in ruminants. Therefore, we measured mRNA and protein expression and examined the cellular localization of EDN1 precursor (pre-pro EDN1, or ppEDN1), EDN-converting enzyme-1 (ECE1), and EDN receptors (A, EDNRA and B, EDNRB) in porcine CLs collected on days 4, 7, 10, 13, and 15 of the estrous cycle to look for differences between CLs displaying (days 13-15) versus those lacking (days 4-10) LS. Abundance of ppEDN1 mRNA was greatest (and significant vs all other days) on day 7 of the cycle, whereas EDN1 protein expression did not vary during the cycle and was localized exclusively to endothelial cells (EC). Abundance of ECE1 mRNA was also greatest on day 7 (vs all other days), but ECE1 protein was significantly elevated on day 10 (vs day 4) and was immunolocalized to ECs and large luteal cells (LLC). Abundance of EDNRA mRNA was also maximal on day 7 (vs all other days) of the cycle, whereas EDNRA protein expression was not significantly changed during the cycle and was observed in LLCs, ECs, and small luteal cells (SLC). On day 13, EDNRB mRNA was significantly decreased (versus day 7). Expression of EDNRB protein was decreased on day 10 (versus all other days), and on days 13-15 (vs day 4), and was primarily localized to ECs. In conclusion, the observed elevation in ECE1 protein concentrations on day 10 and the presence of EDNRA on LLC suggests a possible role for EDN1 (resulting from the actions of ECE1) acting via EDNRA in the control of LS in the pig.</description><dc:title>Endothelin-1, endothelin converting enzyme-1 and endothelin receptors in the porcine corpus luteum</dc:title><dc:creator>L.M. Zorrilla, R. Sriperumbudur, J.E. Gadsby</dc:creator><dc:identifier>10.1016/j.domaniend.2009.08.006</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2009-09-28</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2009-09-28</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>75</prism:startingPage><prism:endingPage>85</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009000988/abstract?rss=yes"><title>Metabolic adaptations to heat stress in growing cattle</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009000988/abstract?rss=yes</link><description>Abstract: To differentiate between the effects of heat stress (HS) and decreased dry matter intake (DMI) on physiological and metabolic variables in growing beef cattle, we conducted an experiment in which a thermoneutral (TN) control group (n=6) was pair fed (PF) to match nutrient intake with heat-stressed Holstein bull calves (n=6). Bulls (4 to 5 mo old, 135kg body weight [BW]) housed in climate-controlled chambers were subjected to 2 experimental periods (P): (1) TN (18°C to 20°C) and ad libitum intake for 9 d, and (2) HS (cyclical daily temperatures ranging from 29.4°C to 40.0°C) and ad libitum intake or PF (in TN conditions) for 9 d. During each period, blood was collected daily and all calves were subjected to an intravenous insulin tolerance test (ITT) on day 7 and a glucose tolerance test (GTT) on day 8. Heat stress reduced (12%) DMI and by design, PF calves had similar nutrient intake reductions. During P1, BW gain was similar between environments and averaged 1.25kg/d, and both HS and PF reduced (P&lt;0.01) average daily gain (-0.09kg/d) during P2. Compared to PF, HS decreased (P&lt;0.05) basal circulating glucose concentrations (7%) and tended (P&lt;0.07) to increase (30%) plasma insulin concentrations, but neither HS nor PF altered plasma nonesterified fatty acid concentrations. Although there were no treatment differences in P2, both HS and PF increased (P&lt;0.05) plasma urea nitrogen concentrations (75%) compared with P1. In contrast to P1, both HS and PF had increased (16%) glucose disposal, but compared with PF, HS calves had a greater (67%; P&lt;0.05) insulin response to the GTT. Neither period nor environment acutely affected insulin action, but during P2, calves in both environments tended (P=0.11) to have a blunted overall glucose response to the ITT. Independent of reduced nutrient intake, HS alters post-absorptive carbohydrate (basal and stimulated) metabolism, characterized primarily by increased basal insulin concentrations and insulin response to a GTT. However, HS-induced reduction in feed intake appears to fully explain decreased average daily gain in Holstein bull calves.</description><dc:title>Metabolic adaptations to heat stress in growing cattle</dc:title><dc:creator>M.D. O’Brien, R.P. Rhoads, S.R. Sanders, G.C. Duff, L.H. Baumgard</dc:creator><dc:identifier>10.1016/j.domaniend.2009.08.005</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2009-09-28</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2009-09-28</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>86</prism:startingPage><prism:endingPage>94</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009000976/abstract?rss=yes"><title>Oral glucose leads to a differential response in glucose, insulin, and GLP-1 in lean versus obese cats</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009000976/abstract?rss=yes</link><description>Abstract: The response to oral glucose was examined in 10 obese and 9 lean age-matched, neutered cats. In all cats, oral administration of 2g/kg glucose was followed by a prompt increase in glucose, insulin, and glucagon-like peptide (GLP)-1. There were significant differences between lean and obese cats in the areas under the curve for glucose, insulin, and GLP-1. However, the responses were variable, and a clear distinction between individual lean and obese cats was not possible. Therefore, this test cannot be recommended as a routine test to examine insulin resistance in individual cats as it is used in people. A further disadvantage for routine use is also the fact that this test requires gastric tubing for the correct administration of the glucose and associated tranquilization to minimize stress and that it was associated with development of diarrhea in 25% of the cats. GLP-1 concentrations were much lower in obese than lean cats. The low GLP-1 concentrations in obese cats might indicate a contribution of GLP-1 to the lower insulin sensitivity of obese cats, but this hypothesis needs to be further investigated.</description><dc:title>Oral glucose leads to a differential response in glucose, insulin, and GLP-1 in lean versus obese cats</dc:title><dc:creator>M. Hoenig, E.T. Jordan, D.C. Ferguson, F. de Vries</dc:creator><dc:identifier>10.1016/j.domaniend.2009.08.004</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2009-09-27</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2009-09-27</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>95</prism:startingPage><prism:endingPage>102</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009000964/abstract?rss=yes"><title>Evidence for a potential role of neuropeptide Y in ovine corpus luteum function</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009000964/abstract?rss=yes</link><description>Abstract: Neuropeptide Y (NPY) is a neurohormone that is typically associated with food intake, but it has also been reported to affect the production of progesterone from luteal tissue in vitro. However, NPY has not been previously immunolocalized in the ovine ovary or in the corpus luteum (CL) of any species, and the effects of this neurohormone on luteal function in vivo are not known. Thus, we performed fluorescent immunohistochemistry (IHC) to localize NPY in the ovine ovary and used avidin-biotin immunocytochemistry (ICC) to further define the intracellular localization within follicles and the CL. We then infused NPY directly into the arterial supply of the autotransplanted ovaries of sheep to determine the in vivo effect of exogenous NPY on ovarian blood flow and on the luteal secretion rate of progesterone and oxytocin. Immunohistochemistry revealed that the NPY antigen was localized to cells within the follicles and CL, in the nerve fibers of the ovarian stroma, and in the vessels of the ovarian hilus. In the follicle, the NPY antigen was localized to nerves and vessels within the theca interna layer, and strong staining was observed in the granulosal cells of antral follicles. In the CL, NPY was localized in large luteal cells and in the vascular pericytes and/or endothelial cells of blood vessels, found dispersed throughout the gland and within the luteal capsule. In vivo incremental infusions of NPY at 1, 10, 100, and 1,000 ng/min, each for a 30-min period, into the arterial supply of the transplanted ovary of sheep bearing a CL 11 d of age increased (P≤0.05) ovarian blood flow. The intra-arterial infusions of NPY also increased (P≤0.05) in a dose-dependent manner the secretion rate of oxytocin, which was positively correlated (P≤0.05) with the observed increase in ovarian blood flow. The infusions of NPY had a minimal effect on the secretion rate of progesterone, and similar intra-arterial infusions of NPY into sheep with ovarian transplants bearing a CL over 30 d of age had no significant effect on ovarian blood flow or on the secretion rate of progesterone. These results suggest that NPY acts on the luteal vascular system and the large luteal cells to rapidly stimulate blood flow and the secretion of oxytocin, respectively, which collectively implies a putative role for NPY during the process of luteolysis when increasing amounts of oxytocin are secreted from the ovine CL in response to uterine pulses of prostaglandin F2α.</description><dc:title>Evidence for a potential role of neuropeptide Y in ovine corpus luteum function</dc:title><dc:creator>C.S. Keator, E.E. Custer, T.A. Hoagland, D.T. Schreiber, K. Mah, A.M. Lawson, O.D. Slayden, J.A. McCracken</dc:creator><dc:identifier>10.1016/j.domaniend.2009.08.003</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2009-09-27</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2009-09-27</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>103</prism:startingPage><prism:endingPage>114</prism:endingPage></item><item rdf:about="http://www.domesticanimalendo.com/article/PIIS0739724009000952/abstract?rss=yes"><title>The beta-adrenergic system is involved in the regulation of the expression of avian uncoupling protein in the chicken</title><link>http://www.domesticanimalendo.com/article/PIIS0739724009000952/abstract?rss=yes</link><description>Abstract: Avian uncoupling protein (avUCP) is orthologous to UCP3, which is suggested to be involved in fatty acid metabolism and to limit the mitochondrial production of reactive oxygen species in mammals. In the chicken, the role and regulation of avUCP remain to be clarified. The aim of this study was to explore the control of avUCP expression by the β-adrenergic system, known to be involved in avian thermoregulation and lipid utilization, and in UCP expression in mammals. Therefore, we measured the expression of avUCP mRNA and protein in the Pectoralis major muscle of chickens injected with the β2 agonist isoproterenol, and we investigated the potential pathways involved in the regulation of avUCP mRNA expression. Avian UCP mRNA expression was increased 7-fold 4h after isoproterenol injection, leading to a tendency to a 40% increase in avUCP protein 24h post-injection. This increase was preceded, 30min after isoproterenol injection, by changes in the chicken thyroid status and in the muscular expression of PPARα, PPARβ/δ, and PPARγ coactivator-1α (PGC-1α). Moreover, the analysis of the avUCP promoter sequence suggested potential binding sites for PPARs and for thyroid hormone receptors. We also detected the activation of AMP-activated protein kinase, which has recently been reported to be involved in UCP3 regulation in mammals. This study presents for the first time evidence of β-adrenergic control on avUCP messenger expression in chicken muscle and suggests the potential involvement of AMPK and several transcription factors in this regulation.</description><dc:title>The beta-adrenergic system is involved in the regulation of the expression of avian uncoupling protein in the chicken</dc:title><dc:creator>R. Joubert, S. Métayer Coustard, Q. Swennen, V. Sibut, S. Crochet, E. Cailleau-Audouin, J. Buyse, E. Decuypere, C. Wrutniak-Cabello, G. Cabello, S. Tesseraud, A. Collin</dc:creator><dc:identifier>10.1016/j.domaniend.2009.08.002</dc:identifier><dc:source>Domestic Animal Endocrinology 38, 2 (2010)</dc:source><dc:date>2009-09-27</dc:date><prism:publicationName>Domestic Animal Endocrinology</prism:publicationName><prism:publicationDate>2009-09-27</prism:publicationDate><prism:volume>38</prism:volume><prism:number>2</prism:number><prism:issueIdentifier>S0739-7240(09)X0009-3</prism:issueIdentifier><prism:section></prism:section><prism:startingPage>115</prism:startingPage><prism:endingPage>125</prism:endingPage></item></rdf:RDF>