International Journal of Peptides最新文献

{"title":"Diet-induced obesity in mice overexpressing neuropeptide y in noradrenergic neurons.","authors":"Suvi T Ruohonen,&nbsp;Laura H Vähätalo,&nbsp;Eriika Savontaus","doi":"10.1155/2012/452524","DOIUrl":"https://doi.org/10.1155/2012/452524","url":null,"abstract":"<p><p>Neuropeptide Y (NPY) is a neurotransmitter associated with feeding and obesity. We have constructed an NPY transgenic mouse model (OE-NPY(DBH) mouse), where targeted overexpression leads to increased levels of NPY in noradrenergic and adrenergic neurons. We previously showed that these mice become obese on a normal chow. Now we aimed to study the effect of a Western-type diet in OE-NPY(DBH) and wildtype (WT) mice, and to compare the genotype differences in the development of obesity, insulin resistance, and diabetes. Weight gain, glucose, and insulin tolerance tests, fasted plasma insulin, and cholesterol levels were assayed. We found that female OE-NPY(DBH) mice gained significantly more weight without hyperphagia or decreased activity, and showed larger white and brown fat depots with no difference in UCP-1 levels. They also displayed impaired glucose tolerance and decreased insulin sensitivity. OE-NPY(DBH) and WT males gained weight robustly, but no difference in the degree of adiposity was observed. However, 40% of OE-NPY(DBH) but none of the WT males developed hyperglycaemia while on the diet. The present study shows that female OE-NPY(DBH) mice were not protected from the obesogenic effect of the diet suggesting that increased NPY release may predispose females to a greater risk of weight gain under high caloric conditions.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"452524"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/452524","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31022290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Angiotensinogen gene transcription in pulmonary fibrosis.","authors":"Bruce D Uhal,&nbsp;My-Trang T Dang,&nbsp;Xiaopeng Li,&nbsp;Amal Abdul-Hafez","doi":"10.1155/2012/875910","DOIUrl":"https://doi.org/10.1155/2012/875910","url":null,"abstract":"<p><p>An established body of literature supports the hypothesis that activation of a local tissue angiotensin (ANG) system in the extravascular tissue compartment of the lungs is required for lung fibrogenesis. Transcriptional activation of the angiotensinogen (AGT) gene is believed to be a critical and necessary step in this activation. This paper summarizes the data in support of this theory and discusses transcriptional regulation of AGT, with an emphasis on lung AGT synthesis as a determinant of fibrosis severity. Genetic data linking AGT polymorphisms to the severity of disease in Idiopathic Pulmonary Fibrosis are also discussed.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"875910"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/875910","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30573949","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Leptin in anorexia and cachexia syndrome.","authors":"Diana R Engineer, Jose M Garcia","doi":"10.1155/2012/287457","DOIUrl":"10.1155/2012/287457","url":null,"abstract":"<p><p>Leptin is a product of the obese (OB) gene secreted by adipocytes in proportion to fat mass. It decreases food intake and increases energy expenditure by affecting the balance between orexigenic and anorexigenic hypothalamic pathways. Low leptin levels are responsible for the compensatory increase in appetite and body weight and decreased energy expenditure (EE) following caloric deprivation. The anorexia-cachexia syndrome is a complication of many chronic conditions including cancer, chronic obstructive pulmonary disease, congestive heart failure, chronic kidney disease, and aging, where the decrease in body weight and food intake is not followed by a compensatory increase in appetite or decreased EE. Crosstalk between leptin and inflammatory signaling known to be activated in these conditions may be responsible for this paradox. This manuscript will review the evidence and potential mechanisms mediating changes in the leptin pathway in the setting of anorexia and cachexia associated with chronic diseases.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":" ","pages":"287457"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3303568/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40169867","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Infection by CXCR4-Tropic Human Immunodeficiency Virus Type 1 Is Inhibited by the Cationic Cell-Penetrating Peptide Derived from HIV-1 Tat.","authors":"Shawn Keogan,&nbsp;Shendra Passic,&nbsp;Fred C Krebs","doi":"10.1155/2012/349427","DOIUrl":"https://doi.org/10.1155/2012/349427","url":null,"abstract":"<p><p>Cell-penetrating peptides (CPP), which are short peptides that are capable of crossing the plasma membrane of a living cell, are under development as delivery vehicles for therapeutic agents that cannot themselves enter the cell. One well-studied CPP is the 10-amino acid peptide derived from the human immunodeficiency virus type 1 (HIV-1) Tat protein. In experiments to test the hypothesis that multiple cationic amino acids within Tat peptide confer antiviral activity against HIV-1, introduction of Tat peptide resulted in concentration-dependent inhibition of HIV-1 IIIB infection. Using Tat peptide variants containing arginine substitutions for two nonionic residues and two lysine residues, HIV-1 inhibition experiments demonstrated a direct relationship between cationic charge and antiviral potency. These studies of Tat peptide as an antiviral agent raise new questions about the role of Tat in HIV-1 replication and provide a starting point for the development of CPPs as novel HIV-1 inhibitors.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"349427"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/349427","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30447679","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Natural Peptides with Potential Applications in Drug Development, Diagnosis, and/or Biotechnology.","authors":"Mirian A F Hayashi,&nbsp;Frédéric Ducancel,&nbsp;Katsuhiro Konno","doi":"10.1155/2012/757838","DOIUrl":"https://doi.org/10.1155/2012/757838","url":null,"abstract":"Natural peptides are central and crucial in many physiological processes playing either direct or indirect roles. Peptides are short linear chains of up to fifty amino acid residues, stabilized or not by disulphide bonds. They occur naturally in all living beings and exert highly specific biological activities, whose specificity is mainly based on and dependent on their primary sequence and, ultimately, to their conformational structure. The primary function of most peptides is the cell signalling role aiming to translate and deliver the biochemical “message” that triggers structural, molecular, cellular, and eventually biological effects. Thus, peptides can play roles as agonists, antagonists, modulators, mediators, hormones, effectors, cofactors, activators, stimulators, and so on. \u0000 \u0000Also, many peptides can act directly as enzyme inhibitors or as antimicrobial compounds with possible activity on biological membranes, although with no necessary membrane lipid bilayer permeabilisation ability, acting by interfering with metabolism and targeting cytoplasmic components. They are also potentially antigenic compounds and several other peptides are used as pathological biomarkers, since they can be easily and specifically detected and quantified in various biological fluids. \u0000 \u0000Based on the huge variety of mode of actions and physiological/pathological roles played by the peptides, in general, their structural and functional relationship has been widely studied by scientific researchers. Their functional roles, their reduced size, their low immunogenicity, their stability, in addition to the recent development of powerful strategies for chemical synthesis and/or recombinant expression, have given to the peptides the status of the most promising family of compounds with potential application for human diagnosis and therapy. Furthermore, their scaffold can been engineered to design compounds with modified biochemical, functional, or biophysical properties, allowing their labelling for in vivo imaging and vectorization applications, or also to functionalize nanoparticles. \u0000 \u0000This special issue aims to gather a recent set of six original articles that mainly further emphasizes the molecular diversity and the variety of mode of action of natural peptides. \u0000 \u0000Thus, C. Kairane and colleagues, from Estonia (Faculty of Medicine of University of Tartu), have examined the influence of the replacement of γ-Glu moiety to α-Glu in two gluthatione- (GSH-) related tetrapeptides UPF1 (Tyr (Me)-γ-Glu-Cys-Gly) and UPF17 (Tyr (Me)-α-Glu-Cys-Gly) in the antioxidative defense system in a human erythroleukemia K562 cell line. By monitoring the effects in these K562 cells via measurements of the cytosolic superoxide dismutase CuZnSOD activity and variations of intracellular GSH levels, followed by addressing the question of the stability of these two peptides against the action of the γ-glutamyltranspeptidase (GGT), allowed to the authors to open promising perspectives for ","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"757838"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/757838","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30862153","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pyrazinamide Effects on Cartilage Type II Collagen Amino Acid Composition.","authors":"Larysa B Bondarenko,&nbsp;Valentina M Kovalenko","doi":"10.1155/2012/781785","DOIUrl":"https://doi.org/10.1155/2012/781785","url":null,"abstract":"<p><p>Introduction. Current therapeutic regimens with first-line antitubercular agents are associated to a high rate of adverse effects which could cause pronounced changes in collagen's contents and structure. Investigation of these changes is very important for optimization of antitubercular therapy and minimization of treatment-caused harm. The aim of present paper was to investigate potential effect of pyrazinamide on male rats' cartilage type II collagen amino acid composition. Materials and Methods. Wistar albino male rats (160-200 g b.w.) were divided into three groups: I-received pyrazinamide per os at a dose of 1000 mg/kg b.w./day; II-at a dose of 2000 mg/kg b.w./day, in both groups it was given for 60 days; III-control. After 60 days of the experiment, rats of the experimental (groups I and II) and control groups were sacrificed and the amino acids contents of male rat cartilage type II collagens were determined using amino acid analyzer. Results and Discussion. The study of pyrazinamide effects (administered in different doses) on rat cartilage type II collagen amino acid contents demonstrated presence of dose-dependent pyrazinamide-mediated quantitative and qualitative changes in these rat extracellular matrix proteins in comparison with control.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"781785"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/781785","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30631517","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of Rabbit Epididymal Antimicrobial Peptide, REHbβP, on LPS-Induced Proinflammatory Cytokine Responses in Human Vaginal Cells In Vitro.","authors":"K V R Reddy, D Sukanya, M S Patgaonkar, C Selvaakumar","doi":"10.1155/2012/782019","DOIUrl":"10.1155/2012/782019","url":null,"abstract":"<p><p>Antimicrobial peptides (AMP's) protect epithelial surfaces including epididymis against pathogens and play a key role in orchestrating various defensive responses. Recently, we have identified one such AMP, rabbit epididymal hemoglobin-β subuit (REHbβP) from the epididymal fluid of rabbit, Oryctologus cuniculus. The demonstration of a protective role of REHbβP in epididymal epithelial cells (EPEC's) led us to investigate: (1) the identification of LPS interactive domain in REHbβP, and (2) whether the REHbβP of rabbit origin mediates vaginal cellular immune responses of another species (human). HeLa-S3, human vaginal epithelial cells (hVECs) were exposed to LPS or the LPS-stimulated cells treated with REHbβP or neutral peptide, nREHbβP. Effect of LPS and cytokines (IL-6 and IL-1α) and chemokines (IL-8, MCP-1) levels was determined in the culture supernatants. In response to the LPS, hVECs synthesized these mediators and the levels were significantly higher than controls. This enhancing effect was ameliorated when the LPS-induced hVECs were treated with REHbβP. Similar results were obtained on NF-κB protein and hBD-1 mRNA expression. Confocal microscopy studies revealed that REHbβP attenuated the LPS-induced internalization of E. coli by macrophages. The chemotaxis studies performed using Boyden chamber Transwell assay, which showed elevated migration of U937 cells when the supernatants of LPS-induced hVECs were used, and the effect was inhibited by REHbβP. REHbβP was found to be localized on the acrosome of rabbit spermatozoa, suggesting its role in sperm protection beside sperm function. In conclusion, REHbβP may have the potential to develop as a therapeutic agent for reproductive tract infections (RTI's).</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"782019"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3312295/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30576278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of selective antibacterial peptides by polarity index.","authors":"C Polanco,&nbsp;J L Samaniego,&nbsp;T Buhse,&nbsp;F G Mosqueira,&nbsp;A Negron-Mendoza,&nbsp;S Ramos-Bernal,&nbsp;J A Castanon-Gonzalez","doi":"10.1155/2012/585027","DOIUrl":"https://doi.org/10.1155/2012/585027","url":null,"abstract":"<p><p>In the recent decades, antibacterial peptides have occupied a strategic position for pharmaceutical drug applications and became subject of intense research activities since they are used to strengthen the immune system of all living organisms by protecting them from pathogenic bacteria. This work proposes a simple and easy statistical/computational method through a peptide polarity index measure by which an antibacterial peptide subgroup can be efficiently identified, that is, characterized by a high toxicity to bacterial membranes but presents a low toxicity to mammal cells. These peptides also have the feature not to adopt to an alpha-helicoidal structure in aqueous solution. The double-blind test carried out to the whole Antimicrobial Peptide Database (November 2011) showed an accuracy of 90% applying the polarity index method for the identification of such antibacterial peptide groups.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"585027"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/585027","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30631516","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peptidomic Analysis of the Brain and Corpora Cardiaca-Corpora Allata Complex in the Bombyx mori.","authors":"Xiaoguang Liu,&nbsp;Xia Ning,&nbsp;Yan Zhang,&nbsp;Wenfeng Chen,&nbsp;Zhangwu Zhao,&nbsp;Qingwen Zhang","doi":"10.1155/2012/640359","DOIUrl":"https://doi.org/10.1155/2012/640359","url":null,"abstract":"<p><p>The silkworm, Bombyx mori, is an important economic insect for silk production. However, many of the mature peptides relevant to its various life stages remain unknown. Using RP-HPLC, MALDI-TOF MS, and previously identified peptides from B. mori and other insects in the transcriptome database, we created peptide profiles showing a total of 6 ion masses that could be assigned to peptides in eggs, including one previously unidentified peptide. A further 49 peptides were assigned to larval brains. 17 new mature peptides were identified in isolated masses. 39 peptides were found in pupal brains with 8 unidentified peptides. 48 were found in adult brains with 12 unidentified peptides. These new unidentified peptides showed highly significant matches in all MS analysis. These matches were then searched against the National Center for Biotechnology Information (NCBI) database to provide new annotations for these mature peptides. In total, 59 mature peptides in 19 categories were found in the brains of silkworms at the larval, pupal, and adult stages. These results demonstrate that peptidomic variation across different developmental stages can be dramatic. Moreover, the corpora cardiaca-corpora allata (CC-CA) complex was examined during the fifth larval instar. A total of 41 ion masses were assigned to peptides.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"640359"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/640359","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31160010","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peptide-Modulated Activity Enhancement of Acidic Protease Cathepsin E at Neutral pH.","authors":"Masayuki Komatsu,&nbsp;Madhu Biyani,&nbsp;Sunita Ghimire Gautam,&nbsp;Koichi Nishigaki","doi":"10.1155/2012/316432","DOIUrl":"https://doi.org/10.1155/2012/316432","url":null,"abstract":"<p><p>Enzymes are regulated by their activation and inhibition. Enzyme activators can often be effective tools for scientific and medical purposes, although they are more difficult to obtain than inhibitors. Here, using the paired peptide method, we report on protease-cathepsin-E-activating peptides that are obtained at neutral pH. These selected peptides also underwent molecular evolution, after which their cathepsin E activation capability improved. Thus, the activators we obtained could enhance cathepsin-E-induced cancer cell apoptosis, which indicated their potential as cancer drug precursors.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2012 ","pages":"316432"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/316432","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31200611","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}