Part 3 Metabolism of Proteins and Nucleic Acids Частина 3 Обмін Білків І Нуклеїнових Кислот
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Forensic Medicine
YEREVAN STATE MEDICAL UNIVERSITY AFTER M. HERATSI DEPARTMENT OF Sh. Vardanyan K. Avagyan S. Hakobyan FORENSIC MEDICINE Handout for foreign students YEREVAN 2007 This handbook is adopted by the Methodical Council of Foreign Students of the University DEATH AND ITS CAUSES Thanatology deals with death in all its aspects. Death is of two types: (1) somatic, systemic or clinical, and (2) molecular or cellular. Somatic Death: It is the complete and irreversible stoppage of the circulation, respiration and brain functions, but there is no legal definition of death. THE MOMENT OF DEATH: Historically (medically and legally), the concept of death was that of "heart and respiration death", i.e. stoppage of spontaneous heart and breathing functions. Heart-lung bypass machines, mechanical respirators, and other devices, however have changed this medically in favor of a new concept "brain death", that is, irreversible loss of Cerebral function. Brain death is of three types: (1) Cortical or cerebral death with an intact brain stem. This produces a vegetative state in which respiration continues, but there is total loss of power of perception by the senses. This state of deep coma can be produced by cerebral hypoxia, toxic conditions or widespread brain injury. (2) Brain stem death, where the cerebrum may be intact, though cut off functionally by the stem lesion. The loss of the vital centers that control respiration, and of the ascending reticular activating system that sustains consciousness, cause the victim to be irreversibly comatose and incapable of spontaneous breathing. This can be produced by raised intracranial pressure, cerebral oedema, intracranial haemorrhage, etc.(3) Whole brain death (combination of 1 and 2). -
Amino Acid & Protein
Amino Acid & Protein DR. MD. MAHBUBUR RAHMAN MBBS, M. Phil . MSc.(Biotechnology) DEPT. OF BIOCHEMISTRY RAJSHAHI MEDICAL COLLEGE At the end of the session Student will be able to • Definition of amino acid, formation of peptide bond & its property • Biomedical importance of AA • Protein cycle At the end of the session Student will be able to • Classification of AA, • Isoelectric pH and 2D electrophoresis • Protein – definition, classification & structure, • purification of protein Biomedical Importance • Monomeric unit of Protein/ Polypeptide • Amino acid and their derivatives participate in diverse cellular function • Further discussed in functional classification Biomedical Importance Peptide performs prominent role in neuroendocrine system eg. Hormone , Neurotransmitter, Transporter Human lack of capability to synthesize 10 of the 20 common A-Acid (most of them α amino acid) Diversity of Protein function Enzyme and hormone regulate metabolism muscle movement by protein (contractile protein) Collagen fiber forms bone Ig fights against infectious Bacteria & viruses Bacitracin and gramicidin act a antibiotic Bleomycin act anticancer agent Amino Acid Are organic acid having both carboxyl group and amino group attach to same carbon atom. Peptide Bond In protein, amino acids are joined covalently By peptide Bond which are amide linkage Between the α-carboxyl group of one amino acid and the α- amino group of another Characteristic of peptide bond Net charge of amino acid at neutral pH • At physiologic pH all amino acid have a negatively charged group (- COO-) and positively charged group ( - NH3).----- is called amphoteric( ampholyte) Isoelectric pH The pH at which amino bears no net charge. The pH at which amino acid are electrically neutral that is the sum of positive charge equals the sum of negative charge Optical properties of amino acid α carbon of each amino acid are attached to four different group there fore amino acid have optical isomerism. -
Evidence for a Catabolic Role of Glucagon During an Amino Acid Load
Evidence for a catabolic role of glucagon during an amino acid load. M R Charlton, … , D B Adey, K S Nair J Clin Invest. 1996;98(1):90-99. https://doi.org/10.1172/JCI118782. Research Article Despite the strong association between protein catabolic conditions and hyperglucagonemia, and enhanced glucagon secretion by amino acids (AA), glucagon's effects on protein metabolism remain less clear than on glucose metabolism. To clearly define glucagon's catabolic effect on protein metabolism during AA load, we studied the effects of glucagon on circulating AA and protein dynamics in six healthy subjects. Five protocols were performed in each subject using somatostatin to inhibit the secretion of insulin, glucagon, and growth hormone (GH) and selectively replacing these hormones in different protocols. Total AA concentration was the highest when glucagon, insulin, and GH were low. Selective increase of glucagon levels prevented this increment in AA. Addition of high levels of insulin and GH to high glucagon had no effect on total AA levels, although branched chain AA levels declined. Glucagon mostly decreased glucogenic AA and enhanced glucose production. Endogenous leucine flux, reflecting proteolysis, decreased while leucine oxidation increased in protocols where AA were infused and these changes were unaffected by the hormones. Nonoxidative leucine flux reflecting protein synthesis was stimulated by AA, but high glucagon attenuated this effect. Addition of GH and insulin partially reversed the inhibitory effect of glucagon on protein synthesis. We conclude that glucagon is the pivotal hormone in amino acid disposal during an AA load and, by reducing the availability of AA, […] Find the latest version: https://jci.me/118782/pdf Evidence for a Catabolic Role of Glucagon during an Amino Acid Load Michael R. -
The Role of Polyamine Uptake Transporters on Growth and Development of Arabidopsis Thaliana
THE ROLE OF POLYAMINE UPTAKE TRANSPORTERS ON GROWTH AND DEVELOPMENT OF ARABIDOPSIS THALIANA Jigarkumar Patel A Dissertation Submitted to the Graduate College of Bowling Green State University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY May 2015 Committee: Paul Morris, Advisor Wendy D Manning Graduate Faculty Representative Vipaporn Phuntumart Scott Rogers Ray Larsen © 2015 Jigarkumar Patel All Rights Reserved iii ABSTRACT Paul Morris, Advisor Transgenic manipulation of polyamine levels has provided compelling evidence that polyamines enable plants to respond to environmental cues by activation of stress and developmental pathways. Here we show that the chloroplasts of A. thaliana and soybeans contain both an arginine decarboxylase, and an arginase/agmatinase. These two enzymes combine to synthesize putrescine from arginine. Since the sequences of plant arginases show conservation of key residues and the predicted 3D structures of plant agmatinases overlap the crystal structure of the enzyme from Deinococcus radiodurans, we suggest that these enzymes can synthesize putrescine, whenever they have access to the substrate agmatine. Finally, we show that synthesis of putrescine by ornithine decarboxylase takes place in the ER. Thus A. thaliana has two, and soybeans have three separate pathways for the synthesis of putrescine. This study also describes key changes in plant phenotypes in response to altered transport of polyamines. iv Dedicated to my father, Jayantilal Haribhai Patel v ACKNOWLEDGMENTS I would like to thank my advisor, Dr. Paul F. Morris, for helping me learn and grow during my Ph.D. Dr. Morris has an open door policy, and he was always available to answer my questions and provide helpful suggestions. -
Blood Metabolite Signature of Metabolic Syndrome Implicates
International Journal of Molecular Sciences Article Blood Metabolite Signature of Metabolic Syndrome Implicates Alterations in Amino Acid Metabolism: Findings from the Baltimore Longitudinal Study of Aging (BLSA) and the Tsuruoka Metabolomics Cohort Study (TMCS) Jackson A. Roberts 1 , Vijay R. Varma 1, Chiung-Wei Huang 2, Yang An 2, Anup Oommen 3 , Toshiko Tanaka 4 , Luigi Ferrucci 4, Palchamy Elango 4, Toru Takebayashi 5, Sei Harada 5 , Miho Iida 5 and Madhav Thambisetty 1,* 1 Clinical and Translational Neuroscience Section, Laboratory of Behavioral Neuroscience, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA; [email protected] (J.A.R.); [email protected] (V.R.V.) 2 Brain Aging and Behavior Section, Laboratory of Behavioral Neuroscience, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA; [email protected] (C.-W.H.); [email protected] (Y.A.) 3 Glycoscience Group, National Centre for Biomedical Engineering Science, National University of Ireland Galway, Galway H91-TK33, Ireland; [email protected] 4 Translational Gerontology Branch, National Institute on Aging, NIH, Baltimore, MD 21224, USA; [email protected] (T.T.); [email protected] (L.F.); [email protected] (P.E.) 5 Department of Preventive Medicine and Public Health, Keio University, Tokyo 160-8282, Japan; [email protected] (T.T.); [email protected] (S.H.); [email protected] (M.I.) * Correspondence: [email protected]; Tel.: +1-(410)-558-8572; Fax: +1-(410)-558-8302 Received: 19 December 2019; Accepted: 10 February 2020; Published: 13 February 2020 Abstract: Rapid lifestyle and dietary changes have contributed to a rise in the global prevalence of metabolic syndrome (MetS), which presents a potential healthcare crisis, owing to its association with an increased burden of multiple cardiovascular and neurological diseases. -
RT² Profiler PCR Array (Rotor-Gene® Format) Human Amino Acid Metabolism I
RT² Profiler PCR Array (Rotor-Gene® Format) Human Amino Acid Metabolism I Cat. no. 330231 PAHS-129ZR For pathway expression analysis Format For use with the following real-time cyclers RT² Profiler PCR Array, Rotor-Gene Q, other Rotor-Gene cyclers Format R Description The Human Amino Acid Metabolism I RT² Profiler PCR Array profiles the expression of 84 key genes important in biosynthesis and degradation of functional amino acids. Of the 20 amino acids required for protein synthesis, six of them (arginine, cysteine, glutamine, leucine, proline, and tryptophan), collectively known as the functional amino acids, regulate key metabolic pathways involved in cellular growth, and development, as well as other important biological processes such as immunity and reproduction. For example, leucine activates mTOR signaling and increases protein synthesis, leading to lymphocyte proliferation. Therefore, a lack of leucine can compromise immune function. Metabolic pathways interrelated with the biosynthesis and degradation of these amino acids include vitamin and cofactor biosynthesis (such as SAM or S-Adenosyl Methionine) as well as neurotransmitter metabolism (such as glutamate). This array includes genes for mammalian functional amino acid metabolism as well as genes involved in methionine metabolism, important also for nutrient sensing and sulfur metabolism. Using realtime PCR, you can easily and reliably analyze the expression of a focused panel of genes involved in functional amino acid metabolism with this array. For further details, consult the RT² Profiler PCR Array Handbook. Shipping and storage RT² Profiler PCR Arrays in the Rotor-Gene format are shipped at ambient temperature, on dry ice, or blue ice packs depending on destination and accompanying products. -
Death & Decomposition Part II
Death & Decomposition Part II Review: Why is TSD/PMI so important? Review: What happens in the Fresh (1st) Stage of Decomposition? STAGE 2: Bloat ⦿ 0-10 days ⦿ Putrefaction: bacterially-induced destruction of soft tissue and gas formation › Skin blisters and marbling › Build-up of fluids from ruptured cells and intestines Putrefaction – the gross stuff ➢ Decomposition that occurs as a result of bacteria and other microorganisms ➢ Results in gradual dissolution of solid tissue into gases and liquids, and salts Putrefaction ➢ Characteristics: ○ Greenish discoloration ○ Darkening of the face ○ Bloating and formation of liquid or gas-filled blisters ○ Skin slippage Putrefaction ➢ Begins about 36 hours after death ➢ Further destruction is caused by maggots and insects ➢ Above 40 F, insects will feed until the body is skeletonized Influences of Putrefaction ➢ Heavy clothing and other coverings speed up the process by holding in body heat ➢ Injuries to the body surface promote putrefaction ○ provide portals of entry for bacteria Marbling Stage 3: Active Decay ➢ 10-20 days after death ➢ Body begins to collapse and black surfaces are exposed ➢ Bloated body collapses and leaves a flattened body ➢ Body fluids drain from body Active Decay Active Decay: Destruction of Tissue • Severe decomp can result in complete destruction of soft tissue Active Decay: Advanced Decomposition Stage 4: Dry Decay ➢ 20-365 days after death ➢ Remaining flesh on body is removed and body dries out ➢ Body is dry and continues to decay very slowly due to lack of moisture ➢ -
Three End-Of-Life Cases: Resolving Their Moral Dilemmas
Vol. 33:2 Summer 2017 Three End-of-Life Cases: Resolving Their Moral Dilemmas RENÉ E MIRKES, OSF, PHD An organization of Roman Catholic physicians presented a set of questions to guide moral assessment of three end-of-life cases. The questions for each scenario highlight a corresponding ethical dilemma: (Case #1) the determination of brain death by neurological criteria; (Case #2) the decision to withhold or withdraw artificial nutrition and hydration from an unresponsive wakefulness syndrome (UWS) (formerly referred to as persistent vegetative state, [PVS]) patient; and (Case #3) the administration of pain medication that hastens death. To adjudicate the moral concern raised in each of these clinical cases, the following moral analyses appeal to the natural law perspective summarized in the Ethical & Religious Directives for Catholic Health Care Services1 and in other philosophical resources, both Catholic and secular. CASE #1 An 18-year-old involved in a motorcycle accident was brought to the emergency room with massive head trauma and life support. A brain angiogram showed no blood flow, and a neurological examination revealed no brainstem reflexes as well as persistent apnea. Blood pressure medication was required for heart rate and blood pressure control. Since the patient was an organ donor, the organ recovery team was called in after he was declared brain dead. Discussion (1) When and how do we declare a person dead? What is the difference between theological and scientific definitions of death? (A) A living human being is a substantial union of a (mammalian) body and a rational soul. We are not spiritual beings who use or have bodies. -
Ornithine Decarboxylase Regulates M1 Macrophage Activation And
Ornithine decarboxylase regulates M1 macrophage PNAS PLUS activation and mucosal inflammation via histone modifications Dana M. Hardbowera,b, Mohammad Asimb, Paula B. Luisc, Kshipra Singhb, Daniel P. Barryb, Chunying Yangd,e, Meredith A. Steevese, John L. Clevelandd,e, Claus Schneiderc, M. Blanca Piazuelob, Alain P. Gobertb, and Keith T. Wilsona,b,f,g,h,1 aDepartment of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232; bDivision of Gastroenterology, Hepatology and Nutrition, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232; cDepartment of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232; dDepartment of Tumor Biology, Moffitt Cancer Center and Research Institute, Tampa, FL 33612; eDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, FL 33458; fDepartment of Cancer Biology, Vanderbilt University School of Medicine, Nashville, TN 37232; gCenter for Mucosal Inflammation and Cancer, Vanderbilt University Medical Center, Nashville, TN 37232; and hVeterans Affairs Tennessee Valley Healthcare System, Nashville, TN 37232 Edited by Carl F. Nathan, Weill Medical College of Cornell University, New York, NY, and approved December 20, 2016 (received for review September 6, 2016) Macrophage activation is a critical step in host responses during pathogens is macrophage activation. Macrophages have the ca- bacterial infections. Ornithine decarboxylase (ODC), the rate-limiting pacity to alter cytokine/chemokine production and various other enzyme in polyamine metabolism, has been well studied in epithelial functions along the spectrum of M1 or M2 activation based on the cells and is known to have essential roles in many different cellular stimulus detected (12–14). M1 macrophages represent a highly functions. However, its role in regulating macrophage function during proinflammatory and antimicrobial subset of macrophages (12–14). -
Biochemistry - Problem Drill 20: Amino Acid Metabolism
Biochemistry - Problem Drill 20: Amino Acid Metabolism Question No. 1 of 10 Instructions: (1) Read the problem and answer choices carefully (2) Work the problems on paper as needed (3) Pick the answer (4) Go back to review the core concept tutorial as needed. 1. ________ is the reaction between an amino acid and an alpha keto acid. (A) Ketogenic (B) Aminogenic (C) Transamination Question (D) Carboxylation (E) Glucogenic A. Incorrect! No, consider the amino acid and keto acid structure when answering this question. B. Incorrect! No, consider the amino acid and keto acid structure when answering this question. C. Correct! Yes, Transamination is the reaction between an amino acid and an alpha keto acid. Feedback D. Incorrect! No, consider the amino acid and keto acid structure when answering this question. E. Incorrect! No, consider the amino acid and keto acid structure when answering this question. Transamination is the reaction between an amino acid and an alpha keto acid. The correct answer is (C). Solution RapidLearningCenter.com © Rapid Learning Inc. All Rights Reserved Question No. 2 of 10 Instructions: (1) Read the problem statement and answer choices carefully (2) Work the problems on paper as needed (3) Pick the answer (4) Go back to review the core concept tutorial as needed. 2. Lysine and leucine are examples of what? (A) Ketogenic amino acids. (B) Nonessential amino acids. (C) Non-ketogenic amino acids. (D) Glucogenic amino acids. Question (E) None of the above A. Correct! Yes, lysine and leucine are examples of ketogenic amino acids. B. Incorrect No, this is not a correct response. -
Fermentation of Non-Digestible Oligosaccharides by Human Colonic Bacteria
Proceedings of the Nutrition Society ( 1996), 55,899-9 12 899 Symposium 2 Fermentation of non-digestible oligosaccharides by human colonic bacteria BY GLENN R. GIBSON, ANNE WILLEMS, SALLY READING AND M. DAVID COLLINS Department of Microbiology, Institute of Food Research, Earley Gate, Reading RG6 6BZ The principal substrates for colonic bacterial growth are dietary carbohydrates which have escaped digestion in the upper gastrointestinal tract. These may be starches, dietary fibres, other non-absorbable sugars, sugar alcohols and oligosaccharides. In the large intestine, saccharolytic bacteria are able to metabolize carbohydrates for increased energy and growth with short-chain fatty acids (SCFA) and a variety of other metabolites, such as the electron-sink products lactate, pyruvate, ethanol, H, and succinate, being produced. The majority of human large intestinal micro-organisms, have a strictly anaerobic metabolism, whilst numbers of facultative anaerobes are many orders of magnitude lower than those of the obligate anaerobes. Of the culturable flora, numerically predominant anaerobes are Gram-negative rods belonging to the genus Bacteroides. Other groups which have hitherto been identified as quantitatively significant include bifidobacteria, clostridia, eubacteria, lactobacilli, Gram-positive cocci, coliforms, methanogens and dissimilatory sulphate- reducing bacteria. Generally, the various components of the large intestinal microbiota may be considered as exerting either pathogenic effects or they may have potential health- promoting values. Bifidobacteria and lactobacilli are considered to belong to the latter group. Bacteria in the colon respond largely to the available fermentable substrate, and there is currently some interest in the use of diet to specifically increase groups perceived as health promoting. Non-digestible oligosaccharides seem to have this (prebiotic) potential. -
Supplementary Informations SI2. Supplementary Table 1
Supplementary Informations SI2. Supplementary Table 1. M9, soil, and rhizosphere media composition. LB in Compound Name Exchange Reaction LB in soil LBin M9 rhizosphere H2O EX_cpd00001_e0 -15 -15 -10 O2 EX_cpd00007_e0 -15 -15 -10 Phosphate EX_cpd00009_e0 -15 -15 -10 CO2 EX_cpd00011_e0 -15 -15 0 Ammonia EX_cpd00013_e0 -7.5 -7.5 -10 L-glutamate EX_cpd00023_e0 0 -0.0283302 0 D-glucose EX_cpd00027_e0 -0.61972444 -0.04098397 0 Mn2 EX_cpd00030_e0 -15 -15 -10 Glycine EX_cpd00033_e0 -0.0068175 -0.00693094 0 Zn2 EX_cpd00034_e0 -15 -15 -10 L-alanine EX_cpd00035_e0 -0.02780553 -0.00823049 0 Succinate EX_cpd00036_e0 -0.0056245 -0.12240603 0 L-lysine EX_cpd00039_e0 0 -10 0 L-aspartate EX_cpd00041_e0 0 -0.03205557 0 Sulfate EX_cpd00048_e0 -15 -15 -10 L-arginine EX_cpd00051_e0 -0.0068175 -0.00948672 0 L-serine EX_cpd00054_e0 0 -0.01004986 0 Cu2+ EX_cpd00058_e0 -15 -15 -10 Ca2+ EX_cpd00063_e0 -15 -100 -10 L-ornithine EX_cpd00064_e0 -0.0068175 -0.00831712 0 H+ EX_cpd00067_e0 -15 -15 -10 L-tyrosine EX_cpd00069_e0 -0.0068175 -0.00233919 0 Sucrose EX_cpd00076_e0 0 -0.02049199 0 L-cysteine EX_cpd00084_e0 -0.0068175 0 0 Cl- EX_cpd00099_e0 -15 -15 -10 Glycerol EX_cpd00100_e0 0 0 -10 Biotin EX_cpd00104_e0 -15 -15 0 D-ribose EX_cpd00105_e0 -0.01862144 0 0 L-leucine EX_cpd00107_e0 -0.03596182 -0.00303228 0 D-galactose EX_cpd00108_e0 -0.25290619 -0.18317325 0 L-histidine EX_cpd00119_e0 -0.0068175 -0.00506825 0 L-proline EX_cpd00129_e0 -0.01102953 0 0 L-malate EX_cpd00130_e0 -0.03649016 -0.79413596 0 D-mannose EX_cpd00138_e0 -0.2540567 -0.05436649 0 Co2 EX_cpd00149_e0