Amastatin . Hydrochloride Cat

Total Page:16

File Type:pdf, Size:1020Kb

Amastatin . Hydrochloride Cat Amastatin . hydrochloride Cat. No.: 10-016 Amastatin . hydrochloride PREDICTED MOLECULAR WEIGHT:474.6 . 36.5 Properties PURIFICATION: ?98% (HPLC) PHYSICAL STATE: White to off-white powder. Short Term Storage: +4°C. Long Term Storage: -20°C. Handling Advice: Keep cool and dry. STORAGE CONDITIONS: Protect from moisture. Use/Stability: Stable for at least 2 years after receipt when stored at -20°C. Additional Info ALTERNATE NAMES: [(2S,3R)-3-Amino-2-hydroxy-5-methyl-hexanoyl]-Val-Val-Asp-OH . HCl Background and References September 28, 2021 1 https://www.prosci-inc.com/amastatin-hydrochloride-10-016.html Slow, tight binding and competitive aminopeptidase (AP) inhibitor. Inhibits cytosolic leucine aminopeptidase, microsomal aminopeptidase M and bacterial leucine aminopeptidase, human serum aminopeptidase A (AP-A), aminopeptidase N (AP-N), tyrosine aminopeptidase, but not aminopeptidase B (AP-B). Amastatin is without effect on trypsin, papain, chymotrypsin, elastase, pepsin or thermolysin. Inhibits completely the Suc-Ala-Ala-Pro-Leu-pNA amidolytic enzyme. Slightly inhibits the formation of angiotensin III (Ang III) from Angiotensin II through AP-A, but significantly increases the potency of BACKGROUND: angiotensin III and [des-Asp1]-angiotensin I. Moderate inhibitor of mitochondrial intermediate peptidase (MIP). Weak inhibitor of simian immunodeficiency virus protease (SIV-PR). ANPEP (aminopeptidase N) is a host receptor targeted by porcine epidemic diarrhoea virus, human coronavirus 229E, feline coronavirus, canine coronavirus, transmissible gastroenteritis virus and infectious bronchitis virus. These viruses all belong to coronaviridae. ANPEP is therefore investigated as a potential target for SARS-CoV-2 infections. 1) Amastatin, an inhibitor of aminopeptidase A, produced by actinomycetes: T. Aoyagi, et REFERENCES: al.; J. Antibiot. 31, 636 (1978) 2) Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes: D.H. Rich, et al.; J. Med. Chem. 27, 417 (1984) 3) The slow, tight binding of bestatin and amastatin to aminopeptidases: S.H. Wilkes & J.M. Prescott; J. Biol. Chem. 260, 13154 (1985) 4) Inhibition of aminopeptidases by peptides containing ketomethylene and hydroxyethylene amide bond replacements: S.L. Harbeson & D.H. Rich; J. Med. Chem. 32, 1378 (1989) 5) Role of aminopeptidase activity in the regulation of the pressor activity of circulating angiotensins: S. Ahmad & P.E. Ward; J. Pharmacol. Exp. Ther. 252, 643 (1990) 6) Purification and biochemical characterization of recombinant simian immunodeficiency virus protease and comparison to human immunodeficiency virus type 1 protease: S.K. Grant, et al.; Biochemistry 30, 8424 (1991) 7) Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization: F. Kalousek, et al.; EMBO J. 11, 2803 (1992) 8) Vasopressin and amastatin induce V(1)-receptor-mediated suppression of excitatory transmission in the rat parabrachial nucleus: X. Chen & Q.J. Pittman; J. Neurophysiol. 82, 1689 (1999) 9) Inhibitors on an elastase-like enzyme activity catalyzing Suc-Ala-Ala-Pro-Leu-pNA amidolysis in human seminal plasma: Y. Matsuda, et al.; Arch. Androl. 44, 1 (2000) 10) The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure- based design, chemistry, and activity: J. Grembecka, et al.; J. Med. Chem. 46, 2641 (2003) ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 28, 2021 2 https://www.prosci-inc.com/amastatin-hydrochloride-10-016.html.
Recommended publications
  • Analytical Performance of an Immunoassay to Measure Proenkephalin ⁎ Leslie J
    Clinical Biochemistry xxx (xxxx) xxx–xxx Contents lists available at ScienceDirect Clinical Biochemistry journal homepage: www.elsevier.com/locate/clinbiochem Analytical performance of an immunoassay to measure proenkephalin ⁎ Leslie J. Donatoa, ,Jeffrey W. Meeusena, John C. Lieskea, Deborah Bergmannc, Andrea Sparwaßerc, Allan S. Jaffea,b a Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN 55905, United States b Division of Cardiology, Mayo Clinic, Rochester, MN 55905, United States c Sphingotec GmbH, Hennigsdorf, Germany ARTICLE INFO ABSTRACT Keywords: Background: Endogenous opioids, enkephalins, are known to increase with acute kidney injury. Since the mature Biomarkers pentapeptides are unstable, we evaluated the performance of an assay that measures proenkephalin 119–159 Proenkephalin (PENK), a stable peptide formed concomitantly with mature enkephalins. Enkephalin Methods: PENK assay performance was evaluated on two microtiterplate/chemiluminescence sandwich im- Pro-enkephalin munoassay formats that required 18 or 1 h incubation times. PENK concentration was measured in plasma from penKid healthy individuals to establish a reference interval and in patients with varied levels of kidney function and Assay validation comorbidities to assess the association with measured glomerular filtration rate (mGFR) using iothalamate clearance. Results: Assay performance characteristics in plasma were similar between the assay formats. Limit of quanti- tation was 26.0 pmol/L (CV = 20%) for the 1 h assay and 17.3 pmol/L (CV = 3%) for the 18 h assay. Measurable ranges were 26–1540 pmol/L (1 h assay) and 18–2300 pmol/L (18 h assay). PENK concentrations are stable in plasma stored ambient to 10 days, refrigerated to at least 15 days, and frozen to at least 90 days.
    [Show full text]
  • Antitumor Activity of Actinonin in Vitro and in Vivo
    Vol. 4, 171-176, January 1998 Clinical Cancer Research 171 Antitumor Activity of Actinonin in Vitro and in Vivo Yang Xu, Lawrence T. Lai, Janice L. Gabrilove, 8), mye!oid and monocytic cells, and most myeloblastic leuke- and David A. Scheinberg’ mias as well as on cells and tissues outside the hematopoietic system including fibroblasts, intestinal epithelium, renal tubular Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 epithelium, and synaptic membranes of the central nervous system (I ). APN occurs as a homodimer, and the molecule is a 150-kDa, transmembrane glycoprotein with an intracellular ABSTRACT amino terminus (1). F23, an antihuman CD13/APN mAb, is able Actinonin, an antibiotic and CD13/aminopeptidase N to completely block the active site of the enzyme (9). (APN) inhibitor, has been shown to be cytotoxic to tumor Bestatin, a CD 1 3/APN inhibitor, was examined in preclin- cell lines in vitro. We investigated the antiproliferative ef- ical and clinical studies; bestatin could inhibit lymph node fects of actinonin on human and murine leukemia and lym- metastasis of P388 leukemia in mice (10) and was used in phoma cells. Actinonin inhibited growth of NB4 and HL6O clinical trials in malignant skin tumors (1 1), in head and neck human cell lines and AKR mouse leukemia cells in vitro with cancer (12), in esophageal cancer (13), and in gynecologic an IC50 of about 2-S g/ml. The inhibitory effect on CD13- tumors (14). High doses of bestatin resulted in the significant positive cells was not blocked by pretreatment with the inhibition of preexisting experimental and spontaneous metas- anti-CD13/APN monoclonal antibody F23, which binds with tasis in mice (15).
    [Show full text]
  • Enkephalin After Peptidase Inhibition
    J Pharmacol Sci 106, 295 – 300 (2008)2 Journal of Pharmacological Sciences ©2008 The Japanese Pharmacological Society Full Paper Great Increase in Antinociceptive Potency of [Leu5]Enkephalin After Peptidase Inhibition Kazuhito Akahori1, Kenya Kosaka1, Xing Lu Jin1, Yoshiharu Arai1, Masanobu Yoshikawa1, Hiroyuki Kobayashi1, and Tetsuo Oka1,* 1Department of Clinical Pharmacology, School of Medicine, Tokai University, Isehara 259-1143, Japan Received August 9, 2007; Accepted December 19, 2007 Abstract. Previous in vitro studies have shown that the degradation of [Leu5]enkephalin during incubation with cerebral membrane preparations is almost completely prevented by a mixture of three peptidase inhibitors: amastatin, captopril, and phosphoramidon. The present in vivo study shows that the inhibitory effect of [Leu5]enkephalin administered intra-third-ventricularly on the tail-flick response was increased more than 500-fold by the intra-third-ventricular pretreatment with the three peptidase inhibitors. The antinociceptive effect produced by the [Leu5]enkephalin in rats pretreated with any combination of two peptidase inhibitors was significantly smaller than that in rats pretreated with the three peptidase inhibitors, indicating that any residual single peptidase could inactivate significant amounts of the [Leu5]enkephalin. The present data, together with those obtained from previous studies, clearly demonstrate that amastatin-, captopril-, and phosphoramidon-sensitive enzymes play important roles in the inactivation of short endogenous opioid
    [Show full text]
  • New Trends in the Development of Opioid Peptide Analogues As Advanced Remedies for Pain Relief
    Current Topics in Medicinal Chemistry 2004, 4, 19-38 19 New Trends in the Development of Opioid Peptide Analogues as Advanced Remedies for Pain Relief Luca Gentilucci* Dipartimento di Chimica “G. Ciamician”, via Selmi 2, Università degli Studi di Bologna, 40126- Bologna, Italy Abstract: The search for new peptides to be used as analgesics in place of morphine has been mainly directed to develop peptide analogues or peptidomimetics having higher biological stability and receptor selectivity. Indeed, most of the alkaloid opioid counterindications are due to the scarce stability and the contemporary activation of different receptor types. However, the development of several extremely stable and selective peptide ligands for the different opioid receptors, and the recent discovery of the m-receptor selective endomorphins, rendered this search less fundamental. In recent years, other opioid peptide properties have been investigated in the search for new pharmacological tools. The utility of a drug depends on its ability to reach appropriate receptors at the target tissue and to remain metabolically stable in order to produce the desired effect. This review deals with the recent investigations on peptide bioavailability, in particular barrier penetration and resistance against enzymatic degradation; with the development of peptides having activity at different receptors; with chimeric peptides, with propeptides, and with non-conventional peptides, lacking basic pharmacophoric features. Key Words. Opioid peptide analogues; opioid receptors; pain; antinociception; peptide stability; bioavailability. INTRODUCTION. OPIOID PEPTIDES, RECEPTORS, receptor interaction by structure-function studies of AND PAIN recombinant receptors and chimera receptors [7,8]. Experiments performed on mutant mice gave new The endogenous opioid peptides have been studied information about the mode of action of opioids, receptor extensively since their discovery aiming to develop effective heterogeneity and interactions [9].
    [Show full text]
  • Structural Basis for Multifunctional Roles of Mammalian Aminopeptidase N
    Structural basis for multifunctional roles of mammalian aminopeptidase N Lang Chen, Yi-Lun Lin, Guiqing Peng, and Fang Li1 Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455 Edited by Ralph S. Baric, University of North Carolina, Chapel Hill, NC, and accepted by the Editorial Board September 21, 2012 (received for review June 13, 2012) Mammalian aminopeptidase N (APN) plays multifunctional roles in sensation and mood regulation by catalyzing the metabolism of many physiological processes, including peptide metabolism, cell neuropeptides that process sensory information. One of these motility and adhesion, and coronavirus entry. Here we determined neuropeptides is enkephalin, which binds to opioid receptors and crystal structures of porcine APN at 1.85 Å resolution and its com- has pain-relief and mood-regulating effects (9). APN degrades plexes with a peptide substrate and a variety of inhibitors. APN is and shortens the in vivo life of enkephalin, and hence enhances a cell surface-anchored and seahorse-shaped zinc-aminopeptidase pain sensation and regulates mood. Second, APN is involved in that forms head-to-head dimers. Captured in a catalytically active blood pressure regulation. APN degrades vasoconstrictive peptide state, these structures of APN illustrate a detailed catalytic mech- angiotensin-III, causing vasodilation and lowered blood pressure anism for its aminopeptidase activity. The active site and peptide- (10). An endogenous APN inhibitor, substance P, blocks both binding channel of APN reside in cavities with wide openings, the enkephalin-dependent and angiotensin-dependent pathways allowing easy access to peptides. The cavities can potentially open (11, 12). Third, APN is overexpressed on the cell surfaces of up further to bind the exposed N terminus of proteins.
    [Show full text]
  • Nociceptin/Orphanin FQ (N/OFQ) Modulates Immunopathology and Airway Hyperresponsiveness Representing a Novel Target for the Treatment of Asthma
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by De Montfort University Open Research Archive British Journal of British Journal of Pharmacology (2016) 173 1286–1301 1286 BJP Pharmacology RESEARCH PAPER Nociceptin/orphanin FQ (N/OFQ) modulates immunopathology and airway hyperresponsiveness representing a novel target for the treatment of asthma Correspondence Professor David G Lambert, Department of Cardiovascular Sciences, University of Leicester, Division of Anaesthesia, Critical Care and Pain Management, Leicester Royal Infirmary, Leicester, UK. E-mail: [email protected] Received 22 May 2015; Revised 02 December 2015; Accepted 10 December 2015 Shailendra R Singh1,2, Nikol Sullo1,3, Maria Matteis3,GiuseppeSpaziano3, John McDonald1, Ruth Saunders2, Lucy Woodman2, Konrad Urbanek3, Antonella De Angelis3,RaffaeleDePalma6,RachidBerair2,Mitesh Pancholi2,VijayMistry2,FrancescoRossi3, Remo Guerrini5, Girolamo Calò4,BrunoD’Agostino3,ChristopherE Brightling2*andDavidGLambert1,* 1Department of Cardiovascular Sciences, University of Leicester, Division of Anaesthesia, Critical Care and Pain Management, Leicester Royal Infirmary, Leicester LE2 7LX, UK, 2Institute for Lung Health, Department of Infection, Immunity and Inflammation and Health Sciences, University of Leicester, Leicester, UK, 3Department of Experimental Medicine, Section of Pharmacology L Donatelli,, Second University of Naples, Naples, Italy, 4Department of Medical Sciences, Section of Pharmacology, University of Ferrara, Ferrara, Italy, 5Department
    [Show full text]
  • Product List Subcatalog Biochemica
    Product Article Name Package Product Article Name Package number Productsize Listnumber size Subcatalog Biochemica Take the pink Link! www. .com AppliChem gmbH AppliChem Scandinavia AppliChem Inc. Ottoweg 4 Lyngby Storcenter 66, Lejl. 1203 2814 Mary Avenue D-64291 Darmstadt DK-2800 Kongens Lyngby 63144 St. Louis Germany Denmark Missouri, USA Phone +49 6151 9357-0 Phone +45 39 64 46 66 Phone +1 314 968-3331 Fax +49 6151 9357-11 Fax +45 39 64 34 81 Fax +1 314 968-5006 eMail [email protected] eMail [email protected] eMail [email protected] www.applichem.com Article number Name Package Article number Name Package size size A2110,0005 A23187 5 mg A9541,0010 3-Acetyl-9-11-dehydro-beta-boswel- 10 mg lic acid HPLC grade A2110,0010 A23187 10 mg A5269,0020 6-O-Acetylacteoside HPLC grade 20 mg A7847,0005 A23187 calcium magnesium salt 5 mg BioChemica A5269,0050 6-O-Acetylacteoside HPLC grade 50 mg A1088,0001 ABTS® BioChemica 1 g A3753,0010 Acetyl-Coenzym A trilithium salt 10 mg BioChemica A1088,0005 ABTS® BioChemica 5 g ® A3753,0050 Acetyl-Coenzym A trilithium salt 50 mg A1088,0010 ABTS BioChemica 10 g BioChemica A7817,0020 Acacetin HPLC grade 20 mg A3753,0100 Acetyl-Coenzym A trilithium salt 100 mg A7817,0050 Acacetin HPLC grade 50 mg BioChemica A1060,0100 ACES Buffer grade 100 g A8502,0005 3-Acetyldeoxynivalenol 5 mg A1060,0250 ACES Buffer grade 250 g A7451,0001 N-Acetyl-D-galactosamine 1 g A1060,1000 ACES Buffer grade 1 kg A7451,0005 N-Acetyl-D-galactosamine 5 g A3986,0025 ACES Molecular biology grade 25 g A2554,0025 N-Acetyl-D-glucosamine
    [Show full text]
  • The Enhancing Effects of Amastatin, Phosphoramidon and Captopril on the Potency of [Met5]-Enkephalin in Rat Vas Deferens Suying
    The Enhancing Effects of Amastatin, Phosphoramidon and Captopril on the Potency of [Met5]-Enkephalin in Rat Vas Deferens Suying CUI", Midori KAJIWARA,Kaori ISHII, KazukoAOKI, Junshi SAKAMOTO,Teruhiko MATSUMIYAand Tetsuo OKA* Departmentof Pharmacology,School of Medicine,Tokai University, Isehara259-11, Japan AcceptedMay 29, 1986 Abstract-The enkephalin-inactivating enzymes in rat vas deferens were studied by using the relatively specific inhibitor of each enzyme. The results showed that the rat vas deferens, like the other three preparations, guinea-pig ileum, mouse vas deferens and striatal membranes of guinea-pig brain, which had been investigated previously, contained three distinct enkephalin-hydrolyzing peptidases. Additionally, the enkephalin-hydrolyzing aminopeptidase, endopeptidase-24.11 and peptidyl dipeptidase A in rat vas deferens were found to be inhibited maximally with 1 IN of amastatin, 1 iiM of phosphoramidon and 1 ,IM of captopril, respectively. In contrast to these three enzymes, both L-tyrosyl-L-tyrosine-sensitive dipeptidyl aminopeptidase and D-phenylalanine-sensitive carboxypeptidase were suggested not to be involved significantly in the inactivation of exogenously given enkephalin in rat vas deferens. The characteristics of the enkephalin-degradative enzymes in rat vas deferens were discussed in terms of their similarities to and differences from those in the other preparations. Three enzymes, both bestatin and peptidases, since enkephalin remains intact amastatin-sensitive aminopeptidase, both almost totally after
    [Show full text]
  • Discovery of Novel Opioid Medications
    National Institute on Drug Abuse RESEARCH MONOGRAPH SERIES Discovery of Novel Opioid Medications 147 U.S. Department of Health and Human Services • Public Health Service • National Institutes of Health Discovery of Novel Opioid Medications Editors: Rao S. Rapaka, Ph.D. Heinz Sorer, Ph.D. NIDA Research Monograph 147 1995 U.S. DEPARTMENT OF HEALTH AND HUMAN SERVICES Public Health Service National Institutes of Health National Institute on Drug Abuse 5600 Fishers Lane Rockville, MD 20857 ACKNOWLEDGEMENT This monograph is based on the papers from a technical review on “Discovery of Novel Opioid Medications” held on July 28-29, 1993. The review meeting was sponsored by the National Institute on Drug Abuse. COPYRIGHT STATUS The National Institute on Drug Abuse has obtained permission from the copyright holders to reproduce certain previously published material as noted in the text. Further reproduction of this copyrighted material is permitted only as part of a reprinting of the entire publication or chapter. For any other use, the copyright holder’s permission is required. All other material in this volume except quoted passages from copyrighted sources is in the public domain and may be used or reproduced without permission from the Institute or the authors. Citation of the source is appreciated. Opinions expressed in this volume are those of the authors and do not necessarily reflect the opinions or official policy of the National Institute on Drug Abuse or any other part of the U.S. Department of Health and Human Services. The U.S. Government does not endorse or favor any specific commercial product or company.
    [Show full text]
  • Biased Agonism of Endogenous Opioid Peptides at the Mu-Opioid Receptor Georgina L. Thompson, J. Robert Lane, Thomas Coudrat
    Molecular Pharmacology Fast Forward. Published on May 26, 2015 as DOI: 10.1124/mol.115.098848 This article has not been copyedited and formatted. The final version may differ from this version. MOL #99848 Biased agonism of endogenous opioid peptides at the mu-opioid receptor Georgina L. Thompson, J. Robert Lane, Thomas Coudrat, Patrick M. Sexton, Arthur Christopoulos and Meritxell Canals Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia (G.L.T., J.R.L., T.C., P.M.S., A.C., M.C.) Downloaded from Defence Science and Technology Organisation, Department of Defence, Fishermans Bend, VIC 3207, Australia (G.L.T.) molpharm.aspetjournals.org at ASPET Journals on September 24, 2021 1 Molecular Pharmacology Fast Forward. Published on May 26, 2015 as DOI: 10.1124/mol.115.098848 This article has not been copyedited and formatted. The final version may differ from this version. MOL #99848 Running title: Endogenous biased agonism at the mu-opioid receptor Georgina L. Thompson, J. Robert Lane, Thomas Coudrat, Patrick M. Sexton, Arthur Christopoulos* and Meritxell Canals* * Corresponding authors: Meritxell Canals and Arthur Christopoulos, Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia. Telephone: + 61-3-99039094. Email: [email protected], Downloaded from [email protected] molpharm.aspetjournals.org Page number: 38 Figure number: 6 Reference number: 69 at ASPET Journals on September 24, 2021 Abstract
    [Show full text]
  • Information to Users
    INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand corner and continuing from left to right in equal sections with small overlaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book. Photographs included in the original manuscript have been reproduced xerographically in this copy. Higher quality 6" x 9" black and white photographic prints are available for any photographs or illustrations appearing in this copy for an additional charge. Contact UMI directly to order. University Microfilms International A Bell & Howell Information Company 300 North Zeeb Road. Ann Arbor. Ml 48106-1346 USA 313/761-4700 800/521-0600 Order Number 9201617 Metabolism of vasoactive peptides by aminopeptidase M Benter, Ibrahim Fadil, Ph.D. The Ohio State University, 1991 UMI 300 N. Zeeb RA Ann Arbor, MI 48106 METABOLISM OF VASOACTIVE PEPTIDES E« AMTNOPEPTIDASE M DISSERTATION Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of the Ohio State University By Ibrahim Fadil Benter, B.S.
    [Show full text]
  • Neural Mechanism Underlying Acupuncture Analgesia Progress in Neurobiology
    Progress in Neurobiology 85 (2008) 355–375 Contents lists available at ScienceDirect Progress in Neurobiology journal homepage: www.elsevier.com/locate/pneurobio Neural mechanism underlying acupuncture analgesia Zhi-Qi Zhao * Institute of Neurobiology, Institutes of Brain Science and State Key Laboratory of Medical Neurobiology, Fudan University, Shanghai 200032, China ARTICLE INFO ABSTRACT Article history: Acupuncture has been accepted to effectively treat chronic pain by inserting needles into the specific Received 20 December 2007 ‘‘acupuncture points’’ (acupoints) on the patient’s body. During the last decades, our understanding of Received in revised form 19 March 2008 how the brain processes acupuncture analgesia has undergone considerable development. Acupuncture Accepted 30 May 2008 analgesia is manifested only when the intricate feeling (soreness, numbness, heaviness and distension) of acupuncture in patients occurs following acupuncture manipulation. Manual acupuncture (MA) is the Keywords: insertion of an acupuncture needle into acupoint followed by the twisting of the needle up and down by Acupuncture hand. In MA, all types of afferent fibers (Ab,Ad and C) are activated. In electrical acupuncture (EA), a Electrical acupuncture Acupuncture point stimulating current via the inserted needle is delivered to acupoints. Electrical current intense enough to Afferent fibers excite Ab- and part of Ad-fibers can induce an analgesic effect. Acupuncture signals ascend mainly Neural mechanisms through the spinal ventrolateral funiculus to the brain. Many brain nuclei composing a complicated network are involved in processing acupuncture analgesia, including the nucleus raphe magnus (NRM), periaqueductal grey (PAG), locus coeruleus, arcuate nucleus (Arc), preoptic area, nucleus submedius, habenular nucleus, accumbens nucleus, caudate nucleus, septal area, amygdale, etc.
    [Show full text]