{"title":"Adropin: A new regulatory peptide in cardiovascular endocrinology","authors":"Jens P. Goetze, Jakob Albrethsen","doi":"10.1016/j.regpep.2014.04.002","DOIUrl":"10.1016/j.regpep.2014.04.002","url":null,"abstract":"","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"190 ","pages":"Pages 41-42"},"PeriodicalIF":0.0,"publicationDate":"2014-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.04.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32257553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Dengyue Yuan, Chaowei Zhou, Tao Wang, Fangjun Lin, Hu Chen, Hongwei Wu, Rongbin Wei, Zhiming Xin, Ju Liu, Yundi Gao, Defang Chen, Shiyong Yang, Yan Wang, Yundan Pu, Zhiqiong Li
{"title":"Molecular characterization and tissue expression of peptide YY in Schizothorax prenanti: Effects of periprandial changes and fasting on expression in the hypothalamus","authors":"Dengyue Yuan, Chaowei Zhou, Tao Wang, Fangjun Lin, Hu Chen, Hongwei Wu, Rongbin Wei, Zhiming Xin, Ju Liu, Yundi Gao, Defang Chen, Shiyong Yang, Yan Wang, Yundan Pu, Zhiqiong Li","doi":"10.1016/j.regpep.2014.03.004","DOIUrl":"10.1016/j.regpep.2014.03.004","url":null,"abstract":"<div><p><span>Peptide YY<span> (PYY) is a potent anorectic neuropeptide implicated in feeding regulation in mammals. However, the involvement of PYY in the feeding behavior of teleosts has not been well understood. In this study, we employed molecular, real-time quantitative PCR and physiological studies to characterize the structure, distribution, and appetite regulatory effects of PYY in </span></span><em>Schizothorax prenanti</em> (<em>S. prenanti</em><span>). A very high conservation in PYY sequences was found in teleosts. PYY is widely expressed, with the highest levels of expression in telencephalon, medulla oblongata, pituitary and hypothalamus of </span><em>S. prenanti</em>. The PYY mRNA expression in the hypothalamus was highly elevated after a meal, suggesting a satiety signal role for PYY in <em>S. prenanti</em>. In addition, PYY gene expression in the hypothalamus was decreased after fasting and increased sharply after refeeding, which suggested that PYY might be involved in the central regulation of appetite in <em>S. prenanti</em>. Overall, our result provides basis for further investigation into the regulation of feeding in <em>S. prenanti</em>.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"190 ","pages":"Pages 32-38"},"PeriodicalIF":0.0,"publicationDate":"2014-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.03.004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32218149","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Urocortin 2 blocks the suppression of gastric antral contractions induced by lipopolysaccharide in freely moving conscious rats","authors":"Tsukasa Nozu , Kaoru Takakusaki , Toshikatsu Okumura","doi":"10.1016/j.regpep.2014.04.004","DOIUrl":"10.1016/j.regpep.2014.04.004","url":null,"abstract":"<div><p><span>Lipopolysaccharide<span> (LPS) inhibits gastric antral contractions in conscious rats. Since LPS regulates corticotropin-releasing factor type 2 receptor (CRF2) expression in the rat stomach, and activation of peripheral CRF2 alters gastric motility, we tried to determine the role of peripheral CRF2 in the LPS-induced suppression of gastric antral contractions. Intraluminal gastric pressure waves were measured in freely moving conscious non-fasted rats using the perfused manometric method. We assessed the area under the manometric trace as the motor index (MI), and compared this result with those obtained 1</span></span> <span>h before and after intraperitoneal injection of drugs. LPS (0.2</span> <!-->mg/kg) significantly decreased MI. Indomethacin (10<!--> <!-->mg/kg) itself did not alter MI but blocked this inhibitory action by LPS. Astressin 2-B (200<!--> <span>μg/kg), a selective CRF2 antagonist, modified neither the basal MI nor the action by LPS. Meanwhile, urocortin 2 (30</span> <!-->μg/kg), a selective CRF2 agonist, reversed the suppression by LPS without affecting the basal MI. This action by urocortin 2 was blocked by pretreatment with astressin 2-B. In conclusion, LPS inhibited gastric antral contractions possibly through a prostaglandin-dependent pathway. Peripheral CRF2 stimulation reversed this response by LPS.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"190 ","pages":"Pages 12-17"},"PeriodicalIF":0.0,"publicationDate":"2014-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.04.004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32312037","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Protective effect of short-term treatment with parathyroid hormone 1-34 on oxidative stress is involved in insulin-like growth factor-I and nuclear factor erythroid 2-related factor 2 in rat bone marrow derived mesenchymal stem cells","authors":"Young-Il Oh, Jong-Hoon Kim, Chang-Won Kang","doi":"10.1016/j.regpep.2013.12.008","DOIUrl":"10.1016/j.regpep.2013.12.008","url":null,"abstract":"<div><p><span><span>Bone marrow-derived mesenchymal stem cell (MSC)-mediated regeneration is a promising treatment for degenerative disease and traumatic injuries. MSCs can be isolated from rats using magnetic-activated cell sorting with CD105 antibody. We investigated the relationships between the expression of endogenous insulin-like growth factor-I (IGF-I) and nuclear factor erythroid 2-related factor 2 (Nrf-2) during short-term treatment with </span>parathyroid hormone (PTH) 1-34-induced protective response in MSCs. PTH 1-34 (10</span><sup>−<!--> <!-->9</sup> <span>M) decreased reactive oxygen species<span> (ROS) generation but increased cell viability and endogenous IGF-I (</span></span><em>p</em> <!--><<!--> <span>0.01). Suppression of IGF-I and Nrf-2 using specific small interfering RNA (siRNA) blocked the effects of PTH 1-34. Furthermore, increasing cell viability of PTH against hydrogen peroxide (H</span><sub>2</sub>O<sub>2</sub>) was suppressed by treatment with siRNA to IGF-I and Nr-2 (<em>p</em> <!--><<!--> <!-->0.05). Exogenous IGF-I (10<sup>−<!--> <!-->9</sup> <!-->M) also increased endogenous IGF-I, cell viability, and Nrf-2 expression. These incremental increases were lessened by Nrf-2 siRNA (<em>p</em> <!--><<!--> <!-->0.05). Exogenous IGF-I also inhibited the increase of H<sub>2</sub>O<sub>2</sub>-induced ROS generation, and the decrease of PTH 1-34-induced ROS generation in the presence of IGF-I and Nrf-2 siRNA. The increase of PTH 1-34-induced Nrf-2 expression was more significant in the nucleus than in the cytosol (<em>p</em> <!--><<!--> <!-->0.05). PTH 1-34 also inhibited H<sub>2</sub>O<sub>2</sub><span><span>-induced inducible nitric oxide synthase<span> expression, but increased the expression of heme oxygenase 1/2. The results implicate PTH 1-34, Nrf-2, and IGF-I </span></span>signaling pathways<span> in the response to oxidative stress. These factors could influence IGF-I regulation of metabolic fate and survival in MSCs.</span></span></p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages 1-10"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.12.008","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32018331","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Giuseppina Basini, Laura Baioni, Simona Bussolati, Stefano Grolli, Francesca Grasselli
{"title":"Prolactin is a potential physiological modulator of swine ovarian follicle function","authors":"Giuseppina Basini, Laura Baioni, Simona Bussolati, Stefano Grolli, Francesca Grasselli","doi":"10.1016/j.regpep.2014.01.003","DOIUrl":"10.1016/j.regpep.2014.01.003","url":null,"abstract":"<div><p>Apart from the well established role of prolactin (PRL) in the control of mammary development and lactation, this hormone appears to possess a variety of physiological functions and evidence exists about its expression in many extra-pituitary sites.</p><p><span>This experimental work was undertaken to gain knowledge about PRL and its receptor presence in the porcine antral follicle. In particular, we investigated the expression and local production of PRL in follicular fluid, theca and </span>granulosa cells<span> cultured in standard conditions and in hypoxia. Then, we also investigated its modulatory effect on several parameters mainly involved in granulosa cell function, namely redox status and steroidogenesis<span>. In order to verify an involvement of PRL in the control of ovarian angiogenesis<span>, a process strictly linked to follicle growth and development<span>, we have verified possible PRL effects on granulosa cell production of Vascular Endothelial Growth Factor (VEGF) and nitric oxide as well as its modulatory role on the angiogenic activity of endothelial cells.</span></span></span></span></p><p>Our data demonstrate that in the swine PRL is expressed in both components of the antral follicle, theca and granulosa layers, and it is produced by granulosa cells. Moreover, the hormone represents a relevant modulatory factor on key processes underlying follicular growth and development, such as steroidogenesis and angiogenesis.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages 22-30"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.01.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32120599","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Proteinase-activated receptor-1 (PAR1) and PAR2 mediate relaxation of guinea pig internal anal sphincter","authors":"Shih-Che Huang","doi":"10.1016/j.regpep.2014.03.001","DOIUrl":"10.1016/j.regpep.2014.03.001","url":null,"abstract":"<div><p>Activation of proteinase-activated receptor-1 (PAR<sub>1</sub><span>) and PAR</span><sub>2</sub><span> stimulates contraction of the rat but relaxation of the guinea pig colon. The aim of the present study was to investigate PAR effects on internal anal sphincter (IAS) motility. We measured relaxation of isolated muscle strips from the guinea pig IAS caused by PAR agonists using isometric transducers. Reverse transcription polymerase chain reaction (RT-PCR) was performed to determine the existence of PAR. In the IAS, thrombin and PAR</span><sub>1</sub> peptide agonists TFLLR-NH<sub>2</sub> and SFLLRN-NH<sub>2</sub> evoked moderate to marked relaxation in a concentration-dependent manner. In addition, trypsin and PAR<sub>2</sub> peptide agonists 2-furoyl-LIGRLO-NH<sub>2</sub>, SLIGRL-NH<sub>2</sub> and SLIGKV-NH<sub>2</sub> produced relaxation. In contrast, both PAR<sub>1</sub> and PAR<sub>2</sub> inactive control peptides did not elicit relaxation. Furthermore, the selective PAR<sub>1</sub><span> antagonist vorapaxar and PAR</span><sub>2</sub> antagonist GB 83 specifically inhibited thrombin and trypsin-induced relaxations, respectively. RT-PCR revealed the presence of PAR<sub>1</sub> and PAR<sub>2</sub> in the IAS. This indicates that PAR<sub>1</sub> and PAR<sub>2</sub> mediate the IAS relaxation. The relaxant responses of TFLLR-NH<sub>2</sub><span> and trypsin were attenuated by N(omega)-Nitro-L-arginine (L-NNA), indicating involvement of NO. These responses were not affected by tetrodotoxin, implying that the PAR effects are not neurally mediated. On the other hand, PAR</span><sub>4</sub> agonists GYPGKF-NH<sub>2</sub>, GYPGQV-NH<sub>2</sub> and AYPGKF-NH<sub>2</sub> did not cause relaxation or contraction, suggesting that PAR<sub>4</sub> is not involved in the sphincter motility. Taken together, these results demonstrate that both PAR<sub>1</sub> and PAR<sub>2</sub> mediate relaxation of the guinea pig IAS through the NO pathway. PAR<sub>1</sub> and PAR<sub>2</sub> may regulate IAS tone and might be potential therapeutic targets for anal motility disorders.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages 46-50"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.03.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32177276","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lena Ohlsson , Alison B. Kohan , Patrick Tso , Bo Ahrén
{"title":"GLP-1 released to the mesenteric lymph duct in mice: Effects of glucose and fat","authors":"Lena Ohlsson , Alison B. Kohan , Patrick Tso , Bo Ahrén","doi":"10.1016/j.regpep.2014.02.001","DOIUrl":"10.1016/j.regpep.2014.02.001","url":null,"abstract":"<div><p><span>Using a newly developed in vivo model measuring glucagon-like peptide-1 (GLP-1) in gut lymphatics in mice, we quantified GLP-1 secretion in vivo after glucose versus fat ingestion with and without concomitant DPP-4 inhibition. The mesenteric lymphatic duct was cannulated in anesthetized C57BL6/J mice and lymph was collected in 30</span> <!-->min intervals. Glucose or fat emulsion (Intralipid<sup>R</sup>) (0.03, 0.1 or 0.3<!--> <!-->kcal) with or without DPP-4-inhibition (NVP DPP728; 10<!--> <!-->μmol/kg) was administered by gastric gavage. Basal intact GLP-1 levels were 0.37<!--> <!-->±<!--> <!-->0.04<!--> <!-->pmol/l (<em>n</em> <!-->=<!--> <!-->61) in lymph compared to 0.07<!--> <!-->±<!--> <!-->0.03 in plasma (<em>n</em> <!-->=<!--> <!-->6; <em>P</em> <!-->=<!--> <!-->0.04) and basal DPP-4 activity was 4.7<!--> <!-->±<!--> <!-->0.3<!--> <!-->pmol/min/μl in lymph (<em>n</em> <!-->=<!--> <!-->23) compared to 22.3<!--> <!-->±<!--> <!-->0.9<!--> <!-->pmol/min/μl in plasma (<em>n</em> <!-->=<!--> <!-->8; <em>P</em> <!--><<!--> <span>0.001). Lymph flow increased from 1.2</span> <!-->±<!--> <!-->0.1<!--> <!-->μl/min to 2.3<!--> <!-->±<!--> <!-->02<!--> <!-->μl/min at 30<!--> <!-->min after glucose and fat administration, with no difference between type of challenge or dose (<em>n</em> <!-->=<!--> <!-->81). Lymph GLP-1 levels increased calorie-dependently after both glucose and fat but with different time courses in that glucose induced a transient increase which had returned to baseline after 90<!--> <span>min whereas the lipid induced a sustained increase which was still elevated above baseline after 210</span> <!-->min. Lymph GLP-1 appearance during 210<!--> <!-->min was two to three-fold higher after glucose (7.4<!--> <!-->±<!--> <!-->2.3<!--> <!-->fmol at 0.3<!--> <!-->kcal) than after isocaloric fat (2.9<!--> <!-->±<!--> <!-->0.8<!--> <!-->fmol at 0.3<!--> <!-->kcal; <em>P</em> <!--><<!--> <!-->0.001). The slope between caloric load and lymph GLP-1 appearance was, however, identical after glucose and fat. We conclude that lymph GLP-1 is higher than plasma GLP-1 whereas lymph DPP-4 activity is lower than plasma DPP-4 activity and that both glucose and fat clearly stimulate GLP-1 secretion calorie-dependently in vivo but with different time courses.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages 40-45"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.02.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32165151","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Carl Frederik Hansen , Efstathios Vassiliadis , Niels Vrang , Per T. Sangild , Bethany P. Cummings , Peter Havel , Jacob Jelsing
{"title":"The effect of ileal interposition surgery on enteroendocrine cell numbers in the UC Davis type 2 diabetes mellitus rat","authors":"Carl Frederik Hansen , Efstathios Vassiliadis , Niels Vrang , Per T. Sangild , Bethany P. Cummings , Peter Havel , Jacob Jelsing","doi":"10.1016/j.regpep.2014.01.002","DOIUrl":"10.1016/j.regpep.2014.01.002","url":null,"abstract":"<div><h3>Aim</h3><p>To investigate the short-term effect of ileal interposition (IT) surgery on gut morphology and enteroendocrine cell numbers in the pre-diabetic UC Davis type 2 diabetes mellitus (UCD-T2DM) rat.</p></div><div><h3>Study design</h3><p>Two-month old male UCD-T2DM rats underwent either sham (n<!--> <!-->=<!--> <!-->5) or IT (n<!--> <!-->=<!--> <!-->5) surgery. Intestines were collected 1.5<!--> <span>months after surgery. The jejunum, ileum and colon regions were processed for histochemical and immunohistochemical labeling and stereological analyses of changes in gut morphometry and number of enteroendocrine cells.</span></p></div><div><h3>Results</h3><p>Stereological analysis showed that intestinal volume, luminal surface area and the number of all chromogranin A-positive enteroendocrine cells were markedly increased in the IT rats compared with sham-operated animals. Subanalyses of the glucagon-like peptide 2, cholecystokinin<span>, serotonin cells and the neurotensin immunoreactive sub-pool of enteroendocrine cells in the IT region revealed an increase in numbers across phenotypes. However, the density of the different cell types varied.</span></p></div><div><h3>Conclusion</h3><p>IT surgery in the UCD-T2DM rat leads to rapid alterations in gut morphometry and an increase in the number of enteroendocrine cells. This effect may potentially explain why IT surgery delays the onset of type 2 diabetes in the UCD-T2DM rat.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages 31-39"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.01.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32103366","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Peter Spégel , Andreas Lindqvist , Monica Sandberg , Nils Wierup
{"title":"Glucose-dependent insulinotropic polypeptide lowers branched chain amino acids in hyperglycemic rats","authors":"Peter Spégel , Andreas Lindqvist , Monica Sandberg , Nils Wierup","doi":"10.1016/j.regpep.2013.12.009","DOIUrl":"10.1016/j.regpep.2013.12.009","url":null,"abstract":"<div><p><span><span>Hypersecretion of the incretin hormone<span> glucose-dependent insulinotropic polypeptide (GIP) has been associated with obesity and glucose intolerance. This condition has been suggested to be linked to GIP resistance. Besides its insulinotropic effect, GIP also directly affects </span></span>glucose uptake<span> and lipid metabolism. This notwithstanding, effects of GIP on other circulating metabolites than glucose have not been thoroughly investigated. Here, we examined effects of infusion of various concentrations of GIP in normo- and hyperglycemic rats on serum metabolite profiles. We found that, despite a decrease in serum glucose levels (−</span></span> <!-->26%, p<!--> <!--><<!--> <span>0.01), the serum metabolite profile was largely unaffected by GIP infusion in normoglycemic rats. Interestingly, levels of branched chain amino acids<span> and the ketone body β-hydroxybutyrate were decreased by 21% (p</span></span> <!--><<!--> <!-->0.05) and 27% (p<!--> <!--><<!--> <!-->0.001), respectively, in hyperglycemic rats infused with 60<!--> <!-->ng/ml GIP. Hence, our data suggest that GIP provokes a decrease in BCAA levels and ketone body production. Increased concentrations of these metabolites have been associated with obesity and T2D.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages 11-16"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.12.009","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32020228","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Hemodynamic regulator and mitogenic growth factor: Re-visiting the age old question with ACE2 and Jak2","authors":"Peter P. Sayeski","doi":"10.1016/j.regpep.2014.03.002","DOIUrl":"10.1016/j.regpep.2014.03.002","url":null,"abstract":"","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":"189 ","pages":"Pages v-vi"},"PeriodicalIF":0.0,"publicationDate":"2014-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2014.03.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32177275","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}