DOCSLIB.ORG

Localization of Neuropeptides in Endocrine Cells of the Chicken Thymus

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Localization of Neuropeptides in Endocrine Cells of the Chicken Thymus Localization of Neuropeptides in Endocrine Cells of the Chicken Thymus Yasuro ATOJI, Yoshio YAMAMOTO, Takeshi KOMATSU1), and Yoshitaka SUZUKI Laboratory of Veterinary Anatomy, Faculty of Agriculture and 1)United Graduate School of Veterinary Science, Gifu University, Yanagido, Gifu 501–11, Japan (Received 6 December 1996/Accepted 18 March 1997) ABSTRACT. Interactions between endocrine cells and epithelial cells, mediated by neurotensin, have been proposed in the chicken thymus. In this study, other neuropeptide candidates acting as mediators in the chicken thymus were examined immunohistochemically. Endocrine cells being oval, elongated or triangular in shape were immunoreactive with antibodies against methionine-enkephalin, neuropeptide Y, substance P, and vasoactive intestinal peptide. These findings suggest that 4 neuropeptides may be involved in cell-to-cell interactions in the chicken thymus. — KEY WORDS: immunohistochemistry, mediator, thymic microenvironment. J. Vet. Med. Sci. 59(7): 601–603, 1997 The mammalian thymus is physiologically under the (50 µm) sections were stained by the avidin-biotin-horseradish control of the pituitary and hypothalamus. In addition to peroxidase complex (ABC) immunohistochemical method. this control, intrathymic interactions via pituitary hormones, The monoclonal or polyclonal antibodies used in this study hypothalamic neuropeptides, and thymic hormones produced were as follows: substance P (1:2,000), vasoactive intestinal within the thymus exist between epithelial cells and peptide (1:5,000), galanin (1:10,000), methionine-enkephalin thymocytes, as well as the in situ production of their (1:12,000), neuropeptide Y (1:10,000), calcitonin gene- respective receptors [3, 6–8]. Intrathymic interactions have related peptide (1:10,000). Characteristics of the antibodies been implicated in the control of the thymic used are shown in Table 1. Dewaxed sections were blocked microenvironment involving T-cell differentiation and with 0.3% H2O2-methanol for 30 min, preincubated with maturation. In the avian thymus, intrathymic interactions 2% normal goat serum for 30 min, and incubated with the via thymic hormones, avian thymic hormone and thymulin, primary antiserum overnight at 4°C. The sections were are generally accepted, as they are in mammals [10]. The incubated with biotinylated anti-rabbit IgG or anti-mouse avian thymus contains endocrine cells as one of its major IgG (1:400, Vector Lab., U.S.A.) for 30 min at room cellular components. In fact, endocrine cells in the chicken temperature and incubated with the ABC complex (ABC thymus were found to contain serotonin, somatostatin, and Elite Kit, Vector Lab.) for 30 min at room temperature. neurotensin at this time [4, 9, 12]. Of these, the neurotensin Peroxidase in the ABC complex was visualized by pathway from endocrine cells to epithelial cells within the incubation in Tris-HCl buffer containing 3,3’- thymus was suggested first [1, 2]. The route from endocrine diaminobenzidine (20 mg/100 ml) and 0.003% H2O2. cells to epithelial cells is different from the interaction Frozen sections were immersed for 30 min in 0.3% H2O2 in pathways in the mammalian thymus. In this study, we PBS, and preincubated in 2% normal goat serum for 60 min examined whether other neuropeptides could be mediatory at room temperature. Sections were then incubated candidates for interactions among cells within the chicken overnight at 4°C in PBS containing the primary antiserum thymus. An immunohistochemical technique was employed as described above, rinsed 3 times in PBS and incubated for by the use of antibodies against 6 neuropeptides. 60 min at room temperature with biotinylated goat Eight adult female White Leghorn chickens (Gallus antibodies against rabbit or mouse IgG (1:400, Vector Lab.). domesticus) (1.7–1.8 kg in weight and 16–18 months of After 3 washes, sections were incubated for 60 min at room age) were used in this study. They were anesthetized with temperature with the ABC complex. The peroxidase sodium pentobarbital (25 mg/kg, i.v.) and perfused reaction was performed as described above for the paraffin transcardially with Ringer’s solution followed by Bouin’s sections. Then, preparations were washed in PBS, mounted fixative. Thymuses were removed and processed for the on gelatin-coated glass slides, air-dried, dehydrated in a preparation of paraffin and cryostat sections for graded ethanol series, cleared in xylene, and covered with immunohistochemistry. All paraffin (4 µm) and cryostat the coverslips. In the controls, the primary antiserum was Table 1. Characteristics of the antibodies used in this study Antibody Immunogen Produced in Source References calcitonin gene-related peptide (CGRP) synthetic rat CGRP rabbit Amersham Int. [11] galanin (Gal) synthetic porcine Gal rabbit Peninsula Lab. not available methionine-enkephalin (ENK) synthetic ENK rabbit Incstar not available neuropeptide Y (NPY) synthetic porcine NPY rabbit Amersham Int. [11] substance P (SP) SP rat* Chemicon Int. [5] vasoactive intestinal peptide (VIP) synthetic VIP rabbit Bioproducts not available * Monoclonal IgG2a. 602 Y. ATOJI, Y. YAMAMOTO, T. KOMATSU, AND Y. SUZUKI Fig. 1. Immunoreactive endocrine cells in the chicken thymus stained with antisera against a: methionine- enkephalin (ENK), b: neuropeptide Y (NPY), c: substance P (SP), and d: vasoactive intestinal peptide (VIP). c and d: paraffin sections lightly counterstained with hematoxylin. a-c: × 530, d: × 690. replaced by non-immune rabbit or mouse serum. However, no secretory granules are formed in their Immunoreactivity of 6 neuropeptides was examined in cytoplasm, which is called the cryptocrine [7]. Epithelial cryostat sections and paraffin sections. In both sections, cells and thymocytes in the chicken thymus have not been endocrine cells were immunostained with antibodies against stained with antibodies against neuropeptides so far. This methionine-enkephalin, neuropeptide Y, substance P, and does not immediately indicate the absence of cryptocrine in vasoactive intestinal peptide (Fig. 1a-d). They were oval, epithelial cells and thymocytes of the avian thymus. elongated or triangular in shape and were sparsely The presence of 6 neuropeptides and serotonin has been distributed in the medulla. In the paraffin sections in elucidated in endocrine cells of the chicken thymus from particular, immunoreactive fine granules were observed in this and previous studies [1, 4, 9, 12]. Håkanson et al. [9] the cytoplasm of endocrine cells (Fig. 1d). Calcitonin gene- ultrastructurally observed 2 types of endocrine cells from related peptide and galanin did not show specific the size and shape of secretory granules in the chicken immunoreactivity in endocrine cells. In the control sections, thymus. Thus, it is considered that each endocrine cell no immunoreactivity was seen. must produce more than one neuropeptide. We fully expect This study demonstrated the presence of methionine- that neuropeptides co-localize in secretory granules. Further enkephalin, neuropeptide Y, substance P, and vasoactive studies will determine what kind of neuropeptides secretory intestinal peptide in endocrine cells in the chicken thymus. granules of endocrine cells contain. The previous study suggested that neurotensin is a mediator in the pathway between endocrine cells and epithelial cells REFERENCES [1]. It is not known whether methionine-enkephalin, neuropeptide Y, substance P, and vasoactive intestinal 1. Atoji, Y., Yamamoto, Y., and Suzuki, Y. 1996. Arch. Histol. peptide go to epithelial cells or thymocytes after endocrine Cytol. 59: 197–203. cells excrete them. However, it is possible that the 4 2. Atoji, Y., Yamamoto, Y., and Suzuki, Y. 1997. Acta Anat. neuropeptides are mediators in the chicken thymus and are Nippon 72: 181–186. 3. Campbell, R. M. and Scanes, C. G. 1995. J. Endocrinol. 147: involved in cell-to-cell interactions in the thymic 383–396. microenvironment. Neuropeptides in the mammalian 4. Carraway, R. E. and Bhatnagar, Y. M. 1980. Peptides 1: thymus are produced by epithelial cells and thymocytes. 159–165. NEUROPEPTIDES IN CHICKEN THYMUS 603 5. Cuello, A. C., Glafra, G., and Milstein, C. 1979. Proc. Natl. istry 39: 25–34. Acad. Sci. U.S.A. 76: 3532–3536. 10. Marsh, J. A. and Scanes, C. G. 1994. Poultry Sci. 73: 1049– 6. Dardenne, M. and Savino, W. 1994. Immunol. Today 15: 1061. 518–523. 11. Schultzberg, M., Hökfelt, T., Nilsson, G., Terenius, L., 7. Geenen, V., Martens, H., Robert, F., Legros, J.-J., Defresne, Rehfeld, J. F., Brown, M., Elde, R., Goldstein, M., and Said, M. P., Boniver,J., Martial, J., Lefèvre, P. J., and Franchimont, S. 1980. Neuroscience 3: 689–744. P. 1991. Prog. Neuroendocrinoimmunol. 4: 135–142. 12. Sundler, F., Carraway, R. E., Håkanson, R., Hammer, R. A., 8. Hadden, J. W. 1992. Int. J. Immunopharmac. 14: 345–352. Alumets, J., and Dubois, M. P. 1978. Cell Tissue Res. 194: 9. Håkanson, R., Larsson, L. I., and Sundler, F. 1974. Histochem- 367–376..
Load more

Recommended publications
  • (12) United States Patent (10) Patent No.: US 7,256.253 B2 Bridon Et Al
    US00725.6253B2 (12) United States Patent (10) Patent No.: US 7,256.253 B2 Bridon et al. (45) Date of Patent: Aug. 14, 2007 (54) PROTECTION OF ENDOGENOUS 6,500,918 B2 12/2002 Ezrin et al. THERAPEUTIC PEPTIDES FROM 6,514,500 B1 2/2003 Bridon et al. PEPTIDASE ACTIVITY THROUGH 6,593,295 B2 7/2003 Bridon et al. CONUGATION TO BLOOD COMPONENTS 6,602,981 B2 8/2003 Ezrin et al. 6,610,825 B2 8, 2003 Ezrin et al. (75)75 Inventors: Dominique P. Bridon, San Francisco, 6,706,892 B1 3/2004 Ezrin et al. CA (US); Alan M. Ezrin, Moraga, CA (US); Peter G. Milner, Los Altos, CA 6,849,714 B1 2/2005 Bridon et al. (US); Darren L. Holmes, Anaheim, CA 2002fOO18751 A1 2/2002 Bridon et al. (US); Karen Thibaudeau, Rosemere 2003, OO73630 A1 4/2003 Bridon et al. (CA) 2003/O105867 A1 6/2003 Colrain et al. 2003. O108568 A1 6/2003 Bridon et al. (73) Assignee: Conjuchem Biotechnologies Inc., 2003/0170250 A1 9, 2003 EZrin et al. Montreal (CA) 2004/O127398 A1 7, 2004 Bridon et al. (*) Notice: Subject to any disclaimer, the term of this 2004/O138100 A1 7/2004 Bridon et al. patent is extended or adjusted under 35 2004/O156859 A1 8, 2004 Ezrin et al. U.S.C. 154(b) by 0 days. 2004/0248782 A1 12/2004 Bridon et al. 2004/0266673 Al 12/2004 Bakis et al. (21) Appl. No.: 11/066,697 2005, 0037974 A1 2/2005 Krantz et al. 2005, OO65075 A1 3, 2005 Erickson et al.
    [Show full text]
  • Monoclonal Antibody to Parathyroid Hormone / PTH (1-38) - Purified
    OriGene Technologies, Inc. OriGene Technologies GmbH 9620 Medical Center Drive, Ste 200 Schillerstr. 5 Rockville, MD 20850 32052 Herford UNITED STATES GERMANY Phone: +1-888-267-4436 Phone: +49-5221-34606-0 Fax: +1-301-340-8606 Fax: +49-5221-34606-11 [email protected] [email protected] AM02147PU-N Monoclonal Antibody to Parathyroid hormone / PTH (1-38) - Purified Alternate names: Parathormone, Parathyrin Quantity: 0.1 mg Background: Parathyroid hormone (PTH), or Parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. Uniprot ID: P01270 NCBI: NP_000306.1 GeneID: 5741 Host / Isotype: Mouse / IgG1 Recommended Isotype SM10P (for use in human samples), AM03095PU-N Controls: Clone: A1/70 Immunogen: Synthetic Human PTH (aa 1-38) poly-Lysine conjugated. AA Sequence: SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALG Format: State: Lyophilized purified IgG fraction from Cell Culture Supernatant Purification: Protein G Chromatography Buffer System: PBS, pH 7.4 Reconstitution: Restore in aqua bidest to 1 mg/ml Applications: RIA: 20 ng/ml. ELISA: 1 µg/ml (Ref.1). ILMA: 20 µg/ml (Ref.3). Immunohistochemistry on Cryosections and Paraffin Sections: 2 µg/ml. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user. Specificity: This antibody detects PTH peptide (aa 15-25; 1-34; 1-38; 1-84; 7-84). There were no cross reactivities obtained with synthetic Human PTH (aa 1-3; 1-10; 4-16; 28-48; 39-84; 44-68; 53-84) nor with PTHrP (aa 1-86), Calcitonin, Gastrin, Beta-2 Microglobulin, Thymulin, Thyroglobulin, Streptavidin, or Glutathione S-transferase.
    [Show full text]
  • Activity of the Pineal Gland, Thymus and Hypophysial- Adrenal System in Oncological Patients I.F
    138 Experimental Oncology 25, 138-142, 2003 (June) ACTIVITY OF THE PINEAL GLAND, THYMUS AND HYPOPHYSIAL- ADRENAL SYSTEM IN ONCOLOGICAL PATIENTS I.F. Labunets*, Yu.A. Grinevich Institute of Oncology, Academy of Medical Sciences of Ukraine, Kyiv 03022, Ukraine ÀÊÒÈÂÍÎÑÒÜ ÝÏÈÔÈÇÀ, ÒÈÌÓÑÀ È ÃÈÏÎÔÈÇÀÐÍÎ- ÍÀÄÏÎ×Å×ÍÈÊÎÂÎÉ ÑÈÑÒÅÌÛ Ó ÁÎËÜÍÛÕ ÎÍÊÎËÎÃÈ×ÅÑÊÎÃÎ ÏÐÎÔÈËß È.Ô. Ëàáóíåö*, Þ.À. Ãðèíåâè÷ Èíñòèòóò îíêîëîãèè ÀÌÍ Óêðàèíû, Êèåâ, Óêðàèíà Melatonin, thymic serum factor (FTS), alpha-melanocytestimulating hormone (alpha-MSH) and cortisol levels in blood serum and urine of healthy subjects and patients with skin melanoma and malignant thymoma of different age groups have been studied. It has been found that in healthy 20–29 year old men the highest melatonin level was observed in winter, those of FTS, cortisol and alpha-MSH — in summer-autumn, autumn-winter and summer, respectively. In male induviduals over 30 years, the increase of melatonin level in winter was not registered, and in those over 40, the stable secretion of FTS and cortisol and decrease of alpha-MSH acrophase at spring time were observed. In healthy women under 40, melatonin level was heightened in follicular and luteal phase of cycle and that of FTS — in luteal phase. Stability of melatonin secretion and reduction of FTS content in luteal phase of cycle were typical for women over 40. The age-related disorders of indices were more pronounced upon tumor development. In men under 40 years suffering from melanoma and thymoma, circannual changes of pineal gland, thymus and hypophysial-adrenal system function were typical for healthy subjects after 40 years. In women with melanoma and thymoma under 40 years melatonin and FTS level during menstrual cycle were similar with those in healthy women over 40.
    [Show full text]
  • MINIREVIEWS Central Nervous System-Immune System Interactions: Psychoneuroendocrinology of Stress and Its Immune Consequences PAUL H
    ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, Jan. 1994, p. 1-6 Vol. 38, No. 1 0066-4804/94/$04.OO+O Copyright X 1994, American Society for Microbiology MINIREVIEWS Central Nervous System-Immune System Interactions: Psychoneuroendocrinology of Stress and Its Immune Consequences PAUL H. BLACK* Department ofMicrobiology, Boston University School ofMedicine, Boston, Massachusetts 02118 The past 20 years has witnessed the emergence of the field receiving information from the periphery, integrating it with of psychoneuroimmunology (48). This field deals with the the internal environment, and adjusting certain functions influence of the central nervous system (CNS) on the im- such as sympathetic nervous system function and endocrine mune system, or more specifically, whether and how secretion (28). The hypothalamus influences the pituitary thoughts and emotions affect immune function. Studies have gland through a variety of polypeptide "releasing factors," concentrated, for the most part, on the effects of stress on for example, corticotropin-releasing factor (CRF), which the immune system. Stress is defined as a state of dishar- controls the release of corticotropin (ACTH) from the ante- mony or threatened homeostasis provoked by a psycholog- rior pituitary gland. Other hypothalamic releasing hormones ical, environmental, or physiologic stressor (12, 40). It has (RHs) include thyrotropin RH, growth hormone RH, and also become apparent from these studies that the immune luteinizing hormone RH; these control the release of thyro- system can influence the CNS, and thus, a circuit exists tropin, growth hormone, gonadotropin, and luteinizing hor- between these two systems. Regulatory molecules or cyto- mone from the anterior pituitary gland. In addition, hypo- kines elaborated from activated immune cells evoke a thalamic somatostatin and dopamine inhibit the release of CNS response which, in turn, affects the immune system growth hormone and prolactin, respectively, from the ante- (26).
    [Show full text]
  • Bearing Mice
    \ PERGAMON International Journal of Immunopharmacology 10 "0888# 16Ð35 Melatonin administration in tumor!bearing mice "intact and pinealectomized# in relation to stress\ zinc\ thymulin and IL!1 E[ Mocchegiania\\ L[ Perissinb\ L[ Santarellia\ A[ Tibaldia\ S[ Zorzetc\ V[ Rapozzib\ R[ Giacconia\ D[ Buliana\ T[ Giraldic a Immunolo`y Center\ Gerontolo`y Research Department\ Italian National Research Centres on A`in`\"I[N[R[C[A[#\ Ancona\ Italy b Department of Biomedical Sciences and Technolo`ies\ University of Udine\ Udine\ Italy c Department of Biomedical Sciences\ University of Trieste\ Trieste\ Italy Received 10 May 0887^ accepted 09 August 0887 Abstract Melatonin "MEL# may counteract tumors through a direct oncostatic role[ MEL is also an antistress agent with immunoenhancing properties against tumors due to a suppressive role of MEL on corticosterone release[ Rotational stress "RS# "spatial disorientation# facilitates metastasis progression in mice[ Also\ MEL counteracts tumors because of its in~uence on immune responses via the metabolic zinc pool\ which\ is reduced in tumors and stress[ Zinc is required for normal thymic endocrine activity "i[e[ thymulin# and interleukin!1 "IL!1# production[ Because in vivo data is still controversial\ exogenous MEL treatment "11 days in drinking water# in both intact and pinealectomized "px# mice bearing Lewis lung carcinoma leads to signi_cant decrements of metastasis volume\ restoration of the negative crude zinc balance\ recovery of thymulin activity and increment of IL!1 exclusively in intact and
    [Show full text]
  • Endocrine System
    Chapter 17 *Lecture PowerPoint The Endocrine System *See separate FlexArt PowerPoint slides for all figures and tables preinserted into PowerPoint without notes. Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display. Introduction • In humans, two systems—the nervous and endocrine—communicate with neurotransmitters and hormones • This chapter is about the endocrine system – Chemical identity – How they are made and transported – How they produce effects on their target cells • The endocrine system is involved in adaptation to stress • There are many pathologies that result from endocrine dysfunctions 17-2 Overview of the Endocrine System • Expected Learning Outcomes – Define hormone and endocrine system. – Name several organs of the endocrine system. – Contrast endocrine with exocrine glands. – Recognize the standard abbreviations for many hormones. – Compare and contrast the nervous and endocrine systems. 17-3 Overview of the Endocrine System • The body has four principal mechanisms of communication between cells – Gap junctions • Pores in cell membrane allow signaling molecules, nutrients, and electrolytes to move from cell to cell – Neurotransmitters • Released from neurons to travel across synaptic cleft to second cell – Paracrine (local) hormones • Secreted into tissue fluids to affect nearby cells – Hormones • Chemical messengers that travel in the bloodstream to other tissues and organs 17-4 Overview of the Endocrine System • Endocrine system—glands, tissues, and cells that secrete hormones
    [Show full text]
  • Thymosin Al Down-Regulates the Growth of Human Non-Small Cell Lung Cancer Cells in Vitro and in Vivo Terry W
    [CANCER RESEARCH 53, 5214-5218, November 1, 1993] Thymosin al Down-regulates the Growth of Human Non-Small Cell Lung Cancer Cells in Vitro and in Vivo Terry W. Moody,1 MírelaFagarasan, Farah Zia, Mirjana Cesnjaj, and Allan L. Goldstein Department of Biochemistry and Molecular Biology, The George Washington University School of Medicine and Health Sciences, Washington, DC 20037 ¡T.W. M., M. F., E Z., A. L. G.I, and Laboratory of Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, NIH, Bethesda, Maryland 20892 [M. C.I ABSTRACT increased survival especially in patients with nonbulky tumors (15): THNal in combination with interferon after cyclophosphamide treat The elicci of thymosin al (THNal) and its NH2-terminal fragment (THN1-14) and COOH-terminal fragment (THIS15-2") on non-small cell ment increased survival of mice with Lewis lung carcinomas (16). lung cancer (NSCLC) growth was evaluated. Using an anti-THNal anti These data suggest that THNal inhibits lung cancer proliferation. Here the effects of THN-like peptides on NSCLC cells were investi body, receptors were identified on NSCLC cells that were pretreated with IO-6 M THNal. | 'll| \niihidoMic acid was readily taken up by NSCLC gated. cells and THNal significantly increased the rate of arachidonic acid re lease. THN1-15 slightly stimulated but THN1"" and THNß4did not alter MATERIALS AND METHODS arachidonic acid release troni NCT-H1299 cells. In clonogenic growth assays in vitro, THNal (10~* M) significantly decreased NSCLC colony Cell Culture. NSCLC cells were cultured in RPMI 1640 containing 10% number whereas THN'-'4, THN1"8, and THNß4were less potent.
    [Show full text]
  • Responses of Bovine Pituitary Transcriptome Profiles to Consumption of Toxic Tall Fescue and Forms of Selenium in Vitamin-Mineral Mixes
    University of Kentucky UKnowledge Theses and Dissertations--Animal and Food Sciences Animal and Food Sciences 2019 RESPONSES OF BOVINE PITUITARY TRANSCRIPTOME PROFILES TO CONSUMPTION OF TOXIC TALL FESCUE AND FORMS OF SELENIUM IN VITAMIN-MINERAL MIXES Qing Li University of Kentucky, [email protected] Digital Object Identifier: https://doi.org/10.13023/etd.2019.035 Right click to open a feedback form in a new tab to let us know how this document benefits ou.y Recommended Citation Li, Qing, "RESPONSES OF BOVINE PITUITARY TRANSCRIPTOME PROFILES TO CONSUMPTION OF TOXIC TALL FESCUE AND FORMS OF SELENIUM IN VITAMIN-MINERAL MIXES" (2019). Theses and Dissertations--Animal and Food Sciences. 99. https://uknowledge.uky.edu/animalsci_etds/99 This Doctoral Dissertation is brought to you for free and open access by the Animal and Food Sciences at UKnowledge. It has been accepted for inclusion in Theses and Dissertations--Animal and Food Sciences by an authorized administrator of UKnowledge. For more information, please contact [email protected]. STUDENT AGREEMENT: I represent that my thesis or dissertation and abstract are my original work. Proper attribution has been given to all outside sources. I understand that I am solely responsible for obtaining any needed copyright permissions. I have obtained needed written permission statement(s) from the owner(s) of each third-party copyrighted matter to be included in my work, allowing electronic distribution (if such use is not permitted by the fair use doctrine) which will be submitted to UKnowledge as Additional File. I hereby grant to The University of Kentucky and its agents the irrevocable, non-exclusive, and royalty-free license to archive and make accessible my work in whole or in part in all forms of media, now or hereafter known.
    [Show full text]
  • Interactions Between the Immune System, Stress and Thymulin
    AN ABSTRACT OF THE THESIS OF Richard L. Christian for the degree of Master of Science in Animal Sciences presented on March 4, 1997. Title: Interactions Between the 1Sy tep;, Stress and Thymulin. Redacted for Privacy Abstract approved: Steven L. Davis This study was conducted to determine the effects of shipping stress on the immune system in domestic lambs (Ovis aries) and to determine the potential of the thymic peptide, thymulin, to reduce those effects of stress on the immune system. Treatments consisted of no shipping (as unstressed controls), shipping (as stressed controls) or shipping plus two doses of thymulin. The shipping procedure was conducted for two consecutive days. The responses were measured in three ways. First, the ability of peripheral blood mononuclear cells (PBMN) to respond to four different doses of the mitogen, Interleukin-2 (IL-2), was measured. Second, antibody response to a standard antigen dose over a three week period following the stress was examined. Third, the plasma cortisol concentrations in stressed versus unstressed and in thymulin treated lambs were compared. There were no differences between any of the four treatment groups (p > 0.44) with respect to the animals' lymphocyte proliferative ability. Although there were no detectable differences, caution should be used in interpreting these results, because of technical difficulties encountered with a key reagent in the assay. Antibody titers were measured at weekly intervals for each of three consecutive weeks following the stressing procedure. These results also showed no treatment effect between any of the four groups (p > 0.39). A comparison of cortisol levels in the four groups revealed that shipping stress increased plasma cortisol concentrations, and thymulin treatment at either dose and on both days of shipment inhibited (p < 0.0001 and p < 0.047, for day one and two, respectively) that stress-induced increase in cortisol.
    [Show full text]
  • Design and Synthesis of Handles for Solid-Phase Peptide Synthesis And
    Louisiana State University LSU Digital Commons LSU Doctoral Dissertations Graduate School 2003 Design and synthesis of handles for solid-phase peptide synthesis and convergent peptide synthesis Jose Giraldes Louisiana State University and Agricultural and Mechanical College, [email protected] Follow this and additional works at: https://digitalcommons.lsu.edu/gradschool_dissertations Part of the Chemistry Commons Recommended Citation Giraldes, Jose, "Design and synthesis of handles for solid-phase peptide synthesis and convergent peptide synthesis" (2003). LSU Doctoral Dissertations. 1146. https://digitalcommons.lsu.edu/gradschool_dissertations/1146 This Dissertation is brought to you for free and open access by the Graduate School at LSU Digital Commons. It has been accepted for inclusion in LSU Doctoral Dissertations by an authorized graduate school editor of LSU Digital Commons. For more information, please [email protected]. DESIGN AND SYNTHESIS OF HANDLES FOR SOLID-PHASE PEPTIDE SYNTHESIS AND CONVERGENT PEPTIDE SYNTHESIS A Dissertation Submitted to the Graduate Faculty of the Louisiana State University and Agricultural and Mechanical College in partial fulfillment of the requirements for the degree of Doctor of Philosophy in The Department of Chemistry by José Giraldés B.S., University of Puerto Rico, 1997 May, 2003 To my family ii ACKNOWLEDGMENTS I would like to thank my major professor Dr. Mark McLaughlin for his invaluable guidance and support during my stay at LSU. I am very grateful for the freedom and encouragement he gave me to develop my own ideas. A major amount of thanks must be given to Dr. Frank Zhou for the magic angle spinning NMR, to Martha Juban for help with peptide synthesis and purification, to Dr.
    [Show full text]
  • Characterization of the Bacterial Metallothionein, Pmta in the Human Pathogen Pseudomonas Aeruginosa Kathryn M
    University of Connecticut OpenCommons@UConn Doctoral Dissertations University of Connecticut Graduate School 6-23-2014 Characterization of the Bacterial Metallothionein, PmtA in the Human Pathogen Pseudomonas aeruginosa Kathryn M. Pietrosimone University of Connecticut - Storrs, [email protected] Follow this and additional works at: https://opencommons.uconn.edu/dissertations Recommended Citation Pietrosimone, Kathryn M., "Characterization of the Bacterial Metallothionein, PmtA in the Human Pathogen Pseudomonas aeruginosa" (2014). Doctoral Dissertations. 498. https://opencommons.uconn.edu/dissertations/498 Characterization of the Bacterial Metallothionein, PmtA, from the Human Pathogen Pseudomonas aeruginosa Kathryn M. Pietrosimone, Ph.D. University of Connecticut, 2014 Small, cysteine-rich proteins called metallothioneins (MTs) bind essential divalent heavy metal cations, such as zinc and copper, as well as toxic heavy metals, such as cadmium and mercury. Stressful conditions such as exposure to heavy metals or reactive oxygen species (ROS) increase the expression of MTs. The numerous cysteine residues in MTs allow the protein to neutralize toxic effects of ROS, bind heavy metals, influence immune cell movement and proliferation. The bacteria Pseudomonas aeruginosa expresses an MT, PmtA, that is similar in structure the eukaryotic MTs. Evidence presented in these suggests that PmtA is an immunomodulatory protein, similar to the eukaryotic counterpart. Jurkat T cells pre-incubated with PmtA and subsequently exposed to a gradient of SDF-1α, lost the ability to move in a persistent direction, while Jurkat T cells pre-incubated with GST did respond to the SDF-1α gradient. Incubation with PmtA also decreased SDF-1α-induced internalization of the receptor CXCR4 on Jurkat T cells. P. aeruginosa strain PW4670 lacks PmtA expression, and is also more sensitive to oxidant exposure than the parent strain PA01.
    [Show full text]
  • 1056 T CELLS and AGING, JANUARY 2002 UPDATE Graham
    [Frontiers in Bioscience 7, d1056-1183, May 1, 2002] T CELLS AND AGING, JANUARY 2002 UPDATE Graham Pawelec1, Yvonne Barnett2, Ros Forsey3, Daniela Frasca4, Amiela Globerson5, Julie McLeod6, Calogero Caruso7, Claudio Franceschi8, Támás Fülöp9, Sudhir Gupta10, Erminia Mariani8, Eugenio Mocchegiani11, Rafael Solana12 1University of Tübingen, Center for Medical Research, ZMF, Waldhörnlestr. 22, D-72072 Tübingen, Germany, 2 University of Ulster, Coleraine, UK, 3 Unilever Research, Bedford, UK, 4 University of Miami, FL, 5 University of the Negev, Israel, 6 University of the West of England, Bristol, UK, 7 University of Palermo, Italy, 8 University of Bologna, Italy, 9 University of Sherbrooke, Quebec, Canada, 10 University of California, Irvine, CA, 11 INRCA, Ancona, Italy, 12 University of Córdoba, Spain TABLE OF CONTENTS 1. Abstract 2. Introduction: How do we establish whether immunosenescence exists and if so whether it means anything to immunological defence mechanisms in aging? 3. Factors contributing to immunosenescence 3.1. Hematopoiesis 3.2. Thymus 4. Post-thymic aging 4.1. T cell subsets 4.2. T cell repertoire 4.3. T cell function 4.3.1. Accessory cells 4.3.2. T cell receptor signal transduction 4.3.3. Costimulatory pathways 4.3.3.1. CD28 family coreceptors and CD80 family ligands 4.3.3.2. Other costimulators 4.4. Cytokine production and response 4.4.1. Regulation of gene transcription 4.4.2. Cytokine secretion 4.4.3. Confounding factors affecting cytokine secretion results 4.4.4. Levels of cytokines in plasma 4.4.5. Cytokine antagonists 4.4.6. Cytokine receptor expression 5. Clonal expansion after T cell activation 5.1.
    [Show full text]