Skip to main content
Key Specialties
Cardiology Diabetology Endocrinology Gastroenterology Geriatrics and Gerontology Gynecology and Obstetrics Hematology Infectious Disease Internal Medicine Nephrology Neurology Oncology Pediatrics Respiratory Medicine Rheumatology Surgery
Congress Coverage
2024 ACC Congress 2023 ESMO Congress 2023 EASD Congress 2023 ERS Congress 2023 ESC Congress
Clinical Collections
Advances in Alzheimer’s

At a glance: The ONWARDS insulin icodec trials

A round-up of the ONWARDS phase 3 clinical trials evaluating the novel weekly insulin icodec in people with diabetes.
ADVANCED SEARCH
Log in
Top
Comparative Clinical Pathology
Published in: Comparative Clinical Pathology 4/2018

01-07-2018 | Original Article

Perturbations of erythrocyte membrane integrity by subchronic low-level lead exposure in New Zealand white rabbits

Authors: Victor M. Ahur, Silvanus M. Anika, Samuel C. Udem

Published in: Comparative Clinical Pathology | Issue 4/2018

Login to get access

Abstract

Lead (Pb) poisoning has been recognised as a clinical condition since ancient times. The anaemia frequently observed in Pb poisoning is thought to result from the shortening of erythrocytes, life span and inhibition of key enzymes of haem synthesis [viz. delta aminolevulinic acid dehydratase (ALAD), pyrimidine 5′-nucleotidase type 1 (P5N-1) and ferrochelatase]. However, the exact mechanism by which Pb shortens erythrocyte life span is still debatable. In the present study, the effect of ingested Pb on erythrocyte membrane sialic acid content and osmotic fragility of New Zealand White (NZW) rabbits was studied. Indices of Pb exposure, RBC counts, haemoglobin concentration (Hb), haematocrit (PCV), mean corpuscular volume (MCV), mean corpuscular haemoglobin (MCH) and mean corpuscular haemoglobin concentration (MCHC) of rabbits were investigated. Exposure to Pb significantly decreased (p < 0.05) RBC counts, Hb levels, MCV and MCH. Similarly, exposure to Pb significantly decreased erythrocyte sialic acid content and increased the erythrocyte osmotic fragility of Pb-treated animals. It is speculated that decreases in membrane sialic acid content due to subchronic low-level Pb exposure shortens red cell life span as observed by increases in osmotic fragility.
Literature
Adamu S, Useh NM, Ibrahim ND, Nok AJ, Esievo KAN (2009) Erythrocyte surface sialic acids depletion as predisposing factor to erythrocyte destruction in sheep experimental model of African trypanosomosis: a preliminary report. Slov Vet Res 46(1):19–28
Ahyayauch H, Sansar W, Rendón-Ramírez A, Goñi FM, Bennouna M, Gamrani H (2013) Effects of chronic and acute lead treatments on the biophysical properties of erythrocyte membranes, and a comparison with model membranes. FEBS Open Bio 3:212–217CrossRefPubMedPubMedCentral
Aminoff D (1961) Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem J 81:384–392CrossRefPubMedPubMedCentral
Baker FJ, Silverton RE, Pallister CJ (2001) Baker and Silverton’s introductory to medical laboratory technology (Nigerian edition). Bounty Press, Nigeria, pp 380–381
Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr (2006) Structure of pyrimidine 5′-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning. J Biol Chem 281(29):20521–20529CrossRefPubMed
Bulai T, Bratosin D, Artenie V, Montreuil J (2003) Uptake of sialic acid by human erythrocyte. Characterizatioin of a transport system. Biochemie 85:241–244CrossRef
Buratai LB, Nok AJ, Ibrahim S, Umar IA, Esievo KAN (2006) Characterization of sialidase from bloodstream froms of Trypanosma vivax. Cell Biochem Funct 24:71–77CrossRefPubMed
CDC (Centers for Disease Control and Prevention) (2013) Blood lead levels in children aged 1–5 years, United States 1999-2010. MMWR, 46(7): 141–146
Cheesbrough M (2005) District laboratory practice in tropical countries, 2nd edition (part 2). Cambridge University Press, Cambridge, UK. pp 295–299CrossRef
Chen GY, Chen X, King S, Cavassani KA, Cheng J, Zheng X, Cao H, Qu J, Fang D, Wu W, Bai XF, Liu JQ, Woodiga SA, Chen C, Sun L, Hogaboam CM, Kunkel SL, Zheng P, Liu Y (2012) Amelioration of sepsis by inhibiting sialidase-mediated disruption of the CD24-SiglecG interaction. Nat Biotechnol 29(5):1–8
Coles EH (1986) Veterinary clinical pathology, 2nd edn. W. B. Saunders, Philadelphia US, pp 192–224
Coustou V, Plazolles N, Guegan F, Baltz T (2012) Sialidases play a key role in infection and anaemia in Trypanosoma congolense animal trypanosomiasis. Cellular Microbiol 14(3):431–445CrossRef
Dodge JT, Mitchell C, Hanahan DJ (1963) The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys 100:119–130CrossRefPubMed
Donaldson WE, Knowles SO (1993) Is lead toxicosis a reflection of altered fatty acid composition of membranes. Comp Biochem Physiol 104:377–379CrossRef
Garg SK (2007) Veterinary toxicology. S. K. Jain CBS Publishers and Distributors, New Delhi, pp 24–29
Ghazaei C, Ahmadi M, Jazani NH (2010) Detection of neuraminidase activity in Pseudomonas aeruginosa PAO1. Iranian J Basic Med Sci 13(3):69–75
Griggs RC (1964) Lead poisoning: hematologic aspects. Prog Hematol 4:117–137PubMed
Heuermann D, Roggentin P, Kleineidam RG, Schauer R (1991) Purification and characterization of a sialidase from Clostridium chauvoei NC08596. Glycoconj J 8:95–101CrossRefPubMed
Jang WH, Lin KM, Kim K, Noh JY, Kang S, Chang YK, Chung JH (2011) Low level of lead can induce phosphatidylserine exposure and erythrophagocytosis: a new mechanism underlying lead-associated anaemia. Toxicol Sci 122:177–184CrossRefPubMed
Karai I, Fukumoto K, Kageyama K, Horiguchi S (1982) Effect of lead in vitro on water metabolism and osmotic fragility of human erythrocytes. Br J Ind Med 39(3):295–299PubMedPubMedCentral
Kempe DS, Lang PA, Eisele K, Klarl BA, Weider T, Huber SM, Duranton C, Lang F (2005) Stimulation of erythrocytes phosphatidylserine exposure by lead ions. Am J Physiol Cell Physiol 288:C396–C402CrossRefPubMed
Kahn CM (ed) (2010) The Merck Veterinary Manual. 10th Edn. Merck & Co., Inc. Kenilworth, p 2824
Kim Y, Yoo CI, Lee CR, Lee JH, Lee H, Kim SR, Chang SH, Lee WJ, Hwang CH, Lee YH (2002) Evaluation of activity of erythrocytes pyrimidine 5′-nucleotidase (P5N) in lead exposed workers: with focus on the effect on haemoglobin. Ind Health 40:23–27CrossRefPubMed
Knowles SO, Donaldson WE (1997) Lead disrupts eicosanoid metabolism, macrophage function and diseases resistant in birds. Biol Trace Elem Res 60:13–26CrossRefPubMed
Maiti AK, Saha NC, Paul G (2010) Effect of lead on oxidative stress, Na+K+atpase activity and mitochondrial electron transport chain activity of the brain of Clarias batrachus L. Bull Environ Contam Toxicol 84:672–676CrossRefPubMed
Mally M, Shin H, Paroz C, Landmann R, Cornelis GR (2008) Capnocytophaga canimorsus: a human pathogen feeding at the surface of epithelial cells and phagocytes. PLoS Pathog 4:e1000164CrossRefPubMedPubMedCentral
Mrugesh T, Dipa L, Manishika G (2011) Effect of lead on human erythrocytes: an in vitro study. Acta Pol Pharm Drug Res 68(5):653–656
Mulligan C, Geertsma ER, Severi E, Kelly DJ, Poolman B, Thomas GH (2009) The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proc Natl Acad Sci U S A 106:1778–1783CrossRefPubMedPubMedCentral
Nguyen DB, Wagner-Britz L, Maia S, Steffen P, Wagner C, Kaestner L, Bernhardt I (2011) Regulation of phosphatidylserine exposure in red blood cells. Cell Physiol Biochem 28(5):847–856CrossRefPubMed
Nok AJ, Nzeribe HC, Yako SK (2003) Trypanosoma evansi: surface localization, properties and hydrolysis of ghost red blood cells and brain cells-implications in trypanosomiasis. Z Naturforsch 58c:594–601CrossRef
Patrick L (2006) Lead toxicity, a review of the literature. Part 1: exposure, evaluation and treatment. Altern Med Rev 11:2–22PubMed
PEMM (Perkin-Elmer Inc. Methods Manual) (1996) Analytical methods for atomic absorption spectroscopy. Perkin-Elmer Corp., Norwalk, p 47 132–299
Schalm OW, Jain NC, Caroll EJ (1975) Textbook of veterinary haematology, 2nd edn. Published by Lea and Fabiger, Philadelphia, pp 129–250
Schauer R, Kamerling JP (1997) Chemistry, biochemistry and biology of sialic acids. In: Glycoproteins II (ed) Montreuil J, Vliegenthart JFG, Schachter H. Elsevier, Amsterdam, pp 241–400
Schwerdtfeger SM, Melzig MF (2010) Sialidase in biological systems. Pharmazie 65:551–561PubMed
Severi E, Randle G, Kivlin P, Whitfield K, Young R, Moxon R, Kelly D, Hood D, Thomas GH (2005) Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter. Mol Microbiol 58:1173–1185CrossRefPubMed
Suradkar SG, Ghodasara DJ, Vohol P, Patel J, Jaiswal V, Prajapati KS (2009) Haemato-biochemical alterations induced by lead acetate toxicity in Wistar rats. Vet World 2(11):429–431
Tanner MJ (1993) The major integral proteins of the human red cell. Baillieres Clin Haematol 6:333–356CrossRefPubMed
Terayama K (1993) Effects of lead on electrophoretic mobility, membrane sialic acid, deformability and survival of rat erythrocytes. Ind Health 13(3):113–126CrossRef
Toscano CD, Guilarte TR (2005) Lead neurotoxicity: from exposure to molecular effects. Brain Res Brain Res Rev 49(3):529–554CrossRefPubMed
Useh NM (2002) The production and characterization of neuraminidase (sialidase) from Clostridium chauvoei (Jakari strain). M.Sc. Ahmadu Bello University, Zaria
Useh NM, Ajanusi JO, Esievo KAN, Nok AJ (2006) Characterization of Sialidase (neuraminidase) isolated from Clostridium Chauvoei (Jakari strain). Cell Biochem Funct 24(4):347–352CrossRefPubMed
Useh NM, Arimie DI, Balogun EO, Ibrahim NDG, Nok AJ, Esievo KAN (2012) Desialylation modulates alkaline phosphatase activity in Zebu cattle experiemntaly infected with Clostridium chauvoei: a novel report. Jordan J Biol Sci 5(4):265–268
Valentine WN, Paglia DE, Fink K, Maldokoro G (1976) Lead poisoning: association with haemolytic anaemia, basophilic stippling, erythrocytes pyrimidine 5′- nucleotidase deficiency and intraerythrocytic accumulation of pyrimidine. J Clin Invest 58:926–932CrossRefPubMedPubMedCentral
Varki A (2007) Glycan-based interaction involving vertebrate sialic acid-recognizing proteins. Nature 446:1023–1029CrossRefPubMed
Varki A (2011) Evolutionary forces shaping the golgi glycosylatioin machinery: why cell suface glycans are universal to living cells. Cold Spring Harb Perspect Biol 3:a005462CrossRefPubMedPubMedCentral
Varki A, Schauer R (2009) Sialic acids. In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertoxxi CR, Hart GW, Etzler MM (eds) Essentials of glycobiology. Cold Spring Harbor Laboratory Press, New York, pp 199–218
von Itzstein M (2007) The war against influenza: discovery and development of sialidase inhibitors. Nat Rev Drug Discov 6:967–974CrossRef
Walski T, Chludzińska L, Komorowska M, Witkiewicz W (2014) Individual osmotic fragility distribution: a new parameter for determination of the osmotic properties of human red blood cells. BioMed Res Intern 2014(162102):1–6CrossRef
Warren L (1994) Bound carbohydrates in nature. Cambridge University Press, CambridgeCrossRef
Wesseling MC, Wagner-Britz L, Huppert H, Hanf B, Hertz L, Nguyen DB, Bernhardt I (2016a) Phosphatidylserine exposure in human red blood cells depending on cell age. Cell Physiol Biochem 38:1376–1390CrossRefPubMed
Wesseling MC, Wagner-Britz L, Nguyen DB, Asanidze S, Mutua J, Mohamed N, Hanf B, Ghashghaeinia M, Kaestner L, Bernhardt I (2016b) Novel insights in the regulation of phosphatidylserine exposure in human red blood cells. Cell Physiol Biochem 39:1941–1954CrossRefPubMed
Yangho KIM, Yoo C, Lee CR, Lee JH, Lee H, Kim S, Chang S, Lee W, Hwang C, Lee YH (2002) Evaluation of activity of erythrocytes pyrimidine 5′-nucleotidase (P5N) in lead exposed workers: with focus on the effect on haemoglobin. Ind Health 40:23–27CrossRef
Metadata
Title
Perturbations of erythrocyte membrane integrity by subchronic low-level lead exposure in New Zealand white rabbits
Authors
Victor M. Ahur
Silvanus M. Anika
Samuel C. Udem
Publication date
01-07-2018
Publisher
Springer London
Published in
Comparative Clinical Pathology / Issue 4/2018
Print ISSN: 1618-5641
Electronic ISSN: 1618-565X
DOI
https://doi.org/10.1007/s00580-018-2679-4

Other articles of this Issue 4/2018

Comparative Clinical Pathology 4/2018 Go to the issue

Original Article

Comparative study of oxidative status in blood of asthmatic patients

Original Article

Ovarian morphology and development of 3 to 8 months old African catfish, Clarias gariepinus

Original Article

Methanolic extract of Celosia argentea var. crista leaves modulates glucose homeostasis and abates oxidative hepatic injury in diabetic rats

Original Article

Cultural and immunohistochemical evaluation of bacterial agents in caprine pneumonia in Nigeria

Original Article

Sero-epidemiological study of peste des petits ruminants in small ruminants in Amahara region, Ethiopia

Original Article

Recombinant VP2 expressed in baculovirus and adjuvanted with TIR-TLR7: a vaccine candidate against infectious bursal disease virus