Association between alcohol-induced erythrocyte membrane alterations and hemolysis in chronic alcoholics
The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35–45 years with a drinking history of 8–10 years. Results showed that plasma marker enzymes AST, ALT, ALP and...
Saved in:
| Published in | Journal of Clinical Biochemistry and Nutrition Vol. 60; no. 1; pp. 63 - 69 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Japan
SOCIETY FOR FREE RADICAL RESEARCH JAPAN
01.01.2017
Japan Science and Technology Agency the Society for Free Radical Research Japan |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35–45 years with a drinking history of 8–10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation (r = 0.703, p<0.05), protein carbonyls (r = 0.754, p<0.05), lysate NOx (r = 0.654, p<0.05) and weak association with C/P ratio (r = 0.240, p<0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics. |
|---|---|
| AbstractList | The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35-45 years with a drinking history of 8-10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation (r = 0.703, p<0.05), protein carbonyls (r = 0.754, p<0.05), lysate NOx (r = 0.654, p<0.05) and weak association with C/P ratio (r = 0.240, p<0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics.The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35-45 years with a drinking history of 8-10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation (r = 0.703, p<0.05), protein carbonyls (r = 0.754, p<0.05), lysate NOx (r = 0.654, p<0.05) and weak association with C/P ratio (r = 0.240, p<0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics. The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35-45 years with a drinking history of 8-10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation ( = 0.703, <0.05), protein carbonyls ( = 0.754, <0.05), lysate NOx ( = 0.654, <0.05) and weak association with C/P ratio ( = 0.240, <0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics. The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35–45 years with a drinking history of 8–10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation ( r = 0.703, p <0.05), protein carbonyls ( r = 0.754, p <0.05), lysate NOx ( r = 0.654, p <0.05) and weak association with C/P ratio ( r = 0.240, p <0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics. The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35–45 years with a drinking history of 8–10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation (r = 0.703, p<0.05), protein carbonyls (r = 0.754, p<0.05), lysate NOx (r = 0.654, p<0.05) and weak association with C/P ratio (r = 0.240, p<0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics. The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on human male volunteers aged between 35–45 years with a drinking history of 8–10 years. Results showed that plasma marker enzymes AST, ALT, ALP and γGT were increased in alcoholic subjects. Plasma and erythrocyte membrane lipid peroxidation, erythrocyte lysate nitric oxide (NOx) levels were also increased significantly in alcoholics. Furthermore, erythrocyte membrane protein carbonyls, total cholesterol, phospholipid and cholesterol/phospholipid (C/P) ratio were increased in alcoholics. SDS-PAGE analysis of erythrocyte membrane proteins revealed that increased density of band 3, protein 4.2, 4.9, actin and glycophorins, whereas glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and glycophorin A showed slight increase, however, decreased ankyrin with no change in spectrins (α and β) and protein 4.1 densities were observed in alcoholics. Moreover, alcoholics red blood cells showed altered morphology with decreased resistance to osmotic hemolysis. Increased hemolysis showed strong positive association with lipid peroxidation (r = 0.703, p<0.05), protein carbonyls (r = 0.754, p<0.05), lysate NOx (r = 0.654, p<0.05) and weak association with C/P ratio (r = 0.240, p<0.05). Bottom line, increased lipid and protein oxidation, altered membrane C/P ratio and membrane cytoskeletal protein profile might be responsible for the increased hemolysis in alcoholics. |
| Author | Padmavathi, Pannuru Bulle, Saradamma Puvvada, Pavan Kumar Maturu, Paramahamsa Nallanchakravarthula, Varadacharyulu Reddy, Vaddi Damodara |
| AuthorAffiliation | 4 DR Biosciences, Research and Development Institute, Jayanagar, Bengaluru, Karnataka - 560 011, India 2 Oil Technological Research Institute, Jawaharlal Nehru Technological University, Anantapur - 515 001, AP, India 1 Department of Biochemistry, Sri Krishnadevaraya University, Anantapur - 515 003, AP, India 3 Department of Pediatrics, Texas Children’s Hospital, Baylor College of Medicine, Houston, TX-77030, USA |
| AuthorAffiliation_xml | – name: 2 Oil Technological Research Institute, Jawaharlal Nehru Technological University, Anantapur - 515 001, AP, India – name: 1 Department of Biochemistry, Sri Krishnadevaraya University, Anantapur - 515 003, AP, India – name: 4 DR Biosciences, Research and Development Institute, Jayanagar, Bengaluru, Karnataka - 560 011, India – name: 3 Department of Pediatrics, Texas Children’s Hospital, Baylor College of Medicine, Houston, TX-77030, USA |
| Author_xml | – sequence: 1 fullname: Bulle, Saradamma organization: Department of Biochemistry, Sri Krishnadevaraya University – sequence: 1 fullname: Reddy, Vaddi Damodara organization: Department of Biochemistry, Sri Krishnadevaraya University – sequence: 1 fullname: Maturu, Paramahamsa organization: Department of Pediatrics, Texas Children’s Hospital, Baylor College of Medicine – sequence: 1 fullname: Puvvada, Pavan Kumar organization: DR Biosciences, Research and Development Institute – sequence: 1 fullname: Padmavathi, Pannuru organization: Oil Technological Research Institute, Jawaharlal Nehru Technological University – sequence: 1 fullname: Nallanchakravarthula, Varadacharyulu organization: Department of Biochemistry, Sri Krishnadevaraya University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28163384$$D View this record in MEDLINE/PubMed |
| BookMark | eNptkU1r3DAQhkVJaTbbXvoDiqGXUHCiL8vSpTSEfkGgl_QsZHkca7GlVJIb9t9Xu5ssbSiI0WGe92Vm3jN04oMHhN4SfMGI4Jcb2_kLImoiXqAVkRLXDZbiBK2wIrTGGKtTdJbSBmMuGsFfoVMqiWBM8hUar1IK1pnsgq86yA8AvjKTDWOYauf7xUJfQdzmMQa7zVDNMHfReChQhrjXpcr4vhphDtM2uVQ5X9mCe2efnJxNr9HLwUwJ3jz-a_Tzy-fb62_1zY-v36-vbmorGp5ryehAKGdGGKuo5aKVxjSUdsYSLnvKWzUoyVivREugg34omBywbVQrMRNsjT4efO-Xbobegs_RTPo-utnErQ7G6X873o36LvzWTTlKQ9ticP5oEMOvBVLWs0sWpqksHZakiRRNQ7HiqqDvn6GbsERf1tO0nFcp1ZZZ1-jd3xMdR3kKoQAfDoCNIaUIwxEhWO8S1ruENRHlFRg_g63L-xjKNm76v-TTQbJJ2dzB0d3E7OwEB1RgTfZlJzm27GiiBs_-APC5wxY |
| CitedBy_id | crossref_primary_10_1007_s10620_018_4938_2 crossref_primary_10_3390_ijms241713124 crossref_primary_10_2174_1568026622666220803151814 crossref_primary_10_22416_1382_4376_2024_1215_3218 crossref_primary_10_3390_ijms22083943 crossref_primary_10_1080_15376516_2023_2290071 crossref_primary_10_1097_MCG_0000000000001383 crossref_primary_10_1007_s00232_020_00147_w crossref_primary_10_1155_2019_5172480 crossref_primary_10_3390_membranes11030189 crossref_primary_10_1111_trf_15811 crossref_primary_10_3390_nu16203541 crossref_primary_10_2169_internalmedicine_0710_17 crossref_primary_10_1016_j_puhip_2025_100604 crossref_primary_10_21518_ms2024_397 crossref_primary_10_3390_ijms232112738 crossref_primary_10_3390_antiox11101919 crossref_primary_10_3164_jcbn_17_96 crossref_primary_10_1007_s00580_022_03400_x |
| Cites_doi | 10.1172/JCI25040 10.4161/oxim.3.1.10476 10.1016/S0735-1097(99)00531-8 10.1016/j.autrev.2008.03.017 10.3109/00365519109091621 10.2215/CJN.06920810 10.1038/227680a0 10.1152/physrev.00029.2006 10.1016/S0301-0082(98)00032-X 10.1155/2013/781050 10.1016/j.bbadis.2006.03.003 10.1006/abio.2002.5676 10.1016/j.alcohol.2011.09.024 10.1146/annurev.pharmtox.39.1.127 10.1016/j.pathophys.2013.12.001 10.1182/blood-2007-07-100180 10.1007/s12192-013-0472-5 10.1177/0960327110396527 10.1182/blood-2006-11-056101 10.1016/j.fct.2009.05.014 10.1016/S0895-7061(02)03261-2 10.1155/2015/682054 10.1016/S0925-4439(00)00086-7 10.1089/ars.2012.4884 10.1007/s10867-005-6472-7 10.1080/10715760601090305 10.1182/blood-2010-11-317024 10.1016/j.clinbiochem.2009.03.005 10.1097/01.ALC.0000148112.92525.AC 10.1016/0003-2697(80)90470-4 10.1002/hep.20957 10.1182/blood-2005-10-3992 10.1093/alcalc/37.4.327 10.1016/j.alcohol.2007.10.006 10.1159/000342229 10.1111/j.1582-4934.2008.00281.x 10.2337/diacare.29.04.06.dc05-1782 10.1155/2013/432616 10.1016/j.etp.2011.01.002 10.1016/j.chemphyslip.2008.09.004 10.1093/alcalc/agt071 10.1002/jat.922 10.1007/s11010-009-0367-z 10.1093/aje/kwg184 10.2174/157488407780598135 |
| ContentType | Journal Article |
| Copyright | 2017 JCBN Copyright Japan Science and Technology Agency 2017 Copyright © 2017 JCBN 2017 |
| Copyright_xml | – notice: 2017 JCBN – notice: Copyright Japan Science and Technology Agency 2017 – notice: Copyright © 2017 JCBN 2017 |
| DBID | AAYXX CITATION NPM 7QL 7QP 7TK 7U9 C1K H94 K9. NAPCQ 7X8 5PM |
| DOI | 10.3164/jcbn.16-16 |
| DatabaseName | CrossRef PubMed Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Virology and AIDS Abstracts Environmental Sciences and Pollution Management AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Nursing & Allied Health Premium MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef PubMed Nursing & Allied Health Premium Virology and AIDS Abstracts Bacteriology Abstracts (Microbiology B) AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Environmental Sciences and Pollution Management MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic PubMed Nursing & Allied Health Premium |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Medicine Diet & Clinical Nutrition |
| EISSN | 1880-5086 |
| EndPage | 69 |
| ExternalDocumentID | PMC5281527 28163384 10_3164_jcbn_16_16 article_jcbn_60_1_60_16_16_article_char_en |
| Genre | Journal Article |
| GroupedDBID | --- .GJ 29K 2WC 5GY ACGFO ACPRK ADBBV ADRAZ AENEX AFRAH AHMBA ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL CS3 D-I DIK DU5 E3Z F5P GX1 HH5 HYE JSF JSH KQ8 M48 O5R O5S OK1 P6G PQQKQ RJT RPM RZJ TKC TR2 AAYXX CITATION NPM 7QL 7QP 7TK 7U9 C1K H94 K9. NAPCQ 7X8 5PM |
| ID | FETCH-LOGICAL-c654t-832f1243a6ac92c4678aa522bac148d2479f9833d9671ebedfc928f0c59780363 |
| IEDL.DBID | M48 |
| ISSN | 0912-0009 |
| IngestDate | Thu Aug 21 18:18:27 EDT 2025 Thu Jul 10 17:43:55 EDT 2025 Mon Jun 30 08:24:55 EDT 2025 Thu Jan 02 22:30:43 EST 2025 Tue Jul 01 00:55:43 EDT 2025 Thu Apr 24 23:09:07 EDT 2025 Wed Sep 03 06:30:03 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | alcohol SDS-PAGE oxidative/nitrosative stress erythrocyte membrane hemolysis |
| Language | English |
| License | This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c654t-832f1243a6ac92c4678aa522bac148d2479f9833d9671ebedfc928f0c59780363 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| OpenAccessLink | http://journals.scholarsportal.info/openUrl.xqy?doi=10.3164/jcbn.16-16 |
| PMID | 28163384 |
| PQID | 2338999798 |
| PQPubID | 1996339 |
| PageCount | 7 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_5281527 proquest_miscellaneous_1865520949 proquest_journals_2338999798 pubmed_primary_28163384 crossref_primary_10_3164_jcbn_16_16 crossref_citationtrail_10_3164_jcbn_16_16 jstage_primary_article_jcbn_60_1_60_16_16_article_char_en |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2017-01-01 |
| PublicationDateYYYYMMDD | 2017-01-01 |
| PublicationDate_xml | – month: 01 year: 2017 text: 2017-01-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Japan |
| PublicationPlace_xml | – name: Japan – name: Gifu – name: Kyoto, Japan |
| PublicationTitle | Journal of Clinical Biochemistry and Nutrition |
| PublicationTitleAlternate | J. Clin. Biochem. Nutr. |
| PublicationYear | 2017 |
| Publisher | SOCIETY FOR FREE RADICAL RESEARCH JAPAN Japan Science and Technology Agency the Society for Free Radical Research Japan |
| Publisher_xml | – name: SOCIETY FOR FREE RADICAL RESEARCH JAPAN – name: Japan Science and Technology Agency – name: the Society for Free Radical Research Japan |
| References | 7 Song BJ, Abdelmegeed MA, Henderson LE, et al. Increased nitroxidative stress promotes mitochondrial dysfunction in alcoholic and non-alcoholic fatty liver disease. Oxid Med Cell Longev 2013; 2013: 781050. 26 Padmavathi P, Damodara Reddy V, Narendra M, Varadacharyulu N. Bidis--hand-rolled, Indian cigarettes: induced biochemical changes in plasma and red membranes of human male volunteers. Clin Biochem 2009; 42: 1041–1045. 22 Tóth ME, Vigh L, Sántha M. Alcohol stress, membranes and chaperones. Cell Stress Chaperones 2014; 19: 299–309. 24 Gallagher PG, Jarolim P. Red blood cell membrane disorders. In: Hoffman R, Benz EJ Jr., Shattil SJ, et al, eds. Hematology: Basic Principles and Practice. Philadelphia, PA: Churchill Livingstone, 2009; 623–643. 28 Reddy VD, Padmavathi P, Hymavathi R, Maturu P, Varadacharyulu NCh. Alcohol-induced oxidative stress in rat liver microsomes: protective effect of Emblica officinalis. Pathophysiology 2014; 21: 153–159. 32 Oakley BR, Kirsch DR, Morris NR. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 1980; 105: 361–363. 45 Ferru E, Giger K, Pantaleo A, et al. Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3. Blood 2011; 117: 5998–6006. 39 Maturu P, Vaddi DR, Pannuru P, Nallanchakravarthula V. Modifications of erythrocyte membrane proteins, enzymes and transport mechanisms in chronic alcoholics: an in vivo and in vitro study. Alcohol Alcohol 2013; 48: 679–686. 27 Sastry KV, Moudgal RP, Mohan J, Tyagi JS, Rao GS. Spectrophotometric determination of serum nitrite and nitrate by copper-cadmium alloy. Anal Biochem 2002; 306: 79–82. 9 Straat M, van Bruggen R, de Korte D, Juffermans NP. Red blood cell clearance in inflammation. Trandus Med Hemother 2012; 39: 353–361. 43 Tyulina OV, Prokopieva VD, Boldyrev AA, Johnson P. Erythrocyte and plasma protein modification in alcoholism: a possible role of acetaldehyde. Biochim Biophys Acta 2006; 1762: 558–563. 31 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685. 42 Stibler H, Beaugé F, Leguicher A, Borg S. Biophysical and biochemical alterations in erythrocyte membranes from chronic alcoholics. Scand J Clin Lab Invest 1991; 51: 309–319. 21 Fadda F, Rossetti ZL. Chronic ethanol consumption: from neuroadaptation to neurodegeneration. Prog Neurobiol 1998; 56: 385–431. 33 Dey A, Cederbaum AI. Alcohol and oxidative liver injury. Hepatology 2006; 43 (2 Suppl 1): S63–S74. 37 Pandey KB, Rizvi SI. Markers of oxidative stress in erythrocytes and plasma during aging in humans. Oxid Med Cell Longev 2012; 3: 2–12. 11 Maio R, Siacqua A, Bruni R, et al. Association between hemoglobin level and endothelial function in uncomplicated untreated hypertensive patients. Clin J Am Sco Nephrol 2011; 6: 648–655. 48 Chu H, Breite A, Ciraolo P, Franco RS, Low PS. Characterization of the deoxyhemoglobin binding site on human erythrocyte band 3: implications for O2 regulation of erythrocyte properties. Blood 2008; 111: 932–938. 36 Catalá A. Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem Phys Lipids 2009; 157: 1–11. 13 Ballard HS. The haematological complications of alcoholism. Alcohol Health Res World 1997; 21: 42–52. 40 Deng XS, Deitrich RA. Ethanol metabolism and effects: nitric oxide and its interaction. Curr Clin Pharmacol 2007; 2: 145–153. 38 Tsuda K, Kinoshita-Shimamoto Y, Kimura K, Nishio I. Nitric oxide is a determinant of membrane fluidity of erythrocytes in postmenopausal woman: an electron paramagnetic resonance investigation. Am J Hypertens 2003; 16: 244–248. 20 Escribá PV, González-Ros JM, Goñi FM, et al. Membranes: a meeting point for lipids, proteins and therapies. J Cell Mol Med 2008; 12: 829–875. 17 Pacher P, Beckman JS, Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 2007; 87: 315–424. 30 Pannuru P, Vaddi DR, Kindinti RR, Varadacharyulu N. Increased erythrocyte antioxidant status protects against smoking induced hemolysis in moderate smokers. Hum Exp Toxicol 2011; 30: 1475–1481. 29 Kavitha G, Damodara Reddy V, Paramahamsa M, Akhtar PM, Varadacharyulu NC. Role of nitric oxide in alcohol-induced changes in lipid profile of moderate and heavy alcoholics. Alcohol 2008; 42: 47–53. 10 Tyulina OV, Huentelman MJ, Prokopieva VD, Boldyrev AA, Johnson P. Does ethanol metabolism affect erythrocyte hemolysis? Biochem Biophys Act 2000; 1535: 69–77. 15 Minneci PC, Deans KJ, Zhi H, et al. Hemolysis-associated endothelial dysfunction mediated by acceleration NO inactivation by decompartmentalized oxyhemoglobin. J Clin Invest 2005; 115: 3409–3417. 44 Zennadi R, Moeller BJ, Whalen EJ, et al. Epinephrine-induced activation of LW-mediated sickle cell adhesion and vaso-occlusion in vivo. Blood 2007; 110: 2708–2717. 18 Owusu BY, Stapley R, Honavar J, Patel RP. Effects of erythrocyte aging on nitric oxide and nitrite metabolism. Antioxid Redox Signal 2013; 19: 1198–1208. 35 Maturu P, Vaddi DR, Pannuru P, Nallanchakravarthula V. Alterations in erythrocyte membrane fluidity and Na+/K+-ATPase activity in chronic alcoholics. Mol Cell Biochem 2010; 339: 35–42. 47 Pantaleo A, Giribaldi G, Mannu F, Arese P, Turrini F. Naturally occurring anti-band 3 antibodies and red blood cell removal under physiological and pathological conditions. Autoimmun Rev 2008; 7: 457–462. 16 Kleinbongard P, Schulz R, Rassaf T, et al. Red blood cells express a functional endothelial nitric oxide synthase. Blood 2006; 107: 2943–2951. 23 Alimi H, Hfaeidh N, Bouoni Z, Sakly M, Ben Rhouma K. Protective effect of Opuntia ficus indica f. Inermis prickly pear juice upon ethanol-induced damages in rat erythrocytes. Alcohol 2012; 46: 235–243. 3 Englund Ogge L, Brohall G, Behre CJ, Schmidt C, Fagerberg B. Alcohol consumption in relation to metabolic regulation, inflammation and adiponectin in 64-year-old Caucasian women: a population-based study with a focus on impaired glucose regulation. Diabetes Care 2006; 29: 908–913. 12 Mozos I. Mechanisms linking red blood cell disorders and cardiovascular diseases. BioMed Res Int 2015; 2015: 682054. 19 Gov N, Safran SA. Red blood cell shape and fluctuations: cytoskeleton confinement and ATP activity. J Biolgic Phys 2005; 31: 453–464. 34 Reddy VD, Padmavathi P, Paramahamsa M, Varadacharyulu N. Modulatory role of Emblica officinalis against alcohol induced biochemical and biophysical changes in rat erythrocyte membranes. Food Chem Toxicol 2009; 47: 1958–1963. 14 Büyükokuroğlu ME, Altikat S, Ciftçi M. The effect of ethanol on glucose-6-phosphate dehydrogenase enzyme activity from human erythrocytes in vitro and rat erythrocytes in vivo. Alcohol Alcoholism 2002; 37: 327–329. 6 Baker RC, Kramer RE. Cytotoxicity of short-chain alcohols. Annu Rev Pharmacol Toxicol 1999; 39: 127–150. 1 Maturu P, Reddy VD, Padmavathi P, Varadacharyulu N. Ethanol induced adaptive changes in blood for the pathological and toxicological effects of chronic ethanol consumption in humans. Exp Taxicol Pathol 2012; 64: 697–703. 4 Klatsky AL, Friedman GD, Armstrong MA, Kipp H. Wine, liquor, beer and mortality. Am J Epidemol 2003; 158: 585–595. 25 Ciccoli L, De Felice C, Paccagnini E, et al. Erythrocyte shape abnormalities, membrane oxidative damage and β-actin alterations: an unrecognised triad in classical autism. Mediators Inflamm 2013; 2013: 432616. 41 Muriel P, Castañeda G, Ortega M, Noël F. Insights into the mechanism of erythrocyte Na+/K+-ATPase inhibition by nitric oxide and peroxynitrite anion. J Appl Toxicol 2003; 23: 275–278. 5 Durazzo TC, Gazdzinski S, Banys P, Meyerhoff DJ. Cigarette smoking exacerbates chronic alcohol-induced brain damage: a preliminary metabolic imaging study. Alcohol Clin Exp Res 2004; 28: 1849–1860. 8 Reddy KR, Reddy VD, Padmavathi P, Kavitha G, Saradamma B, Varadacharyulu NC. Gender differences in alcohol-induced oxidative stress and altered membrane properties in erythrocytes of rats. Indian J Biochem Biophys 2013; 50: 32–39. 2 Gaziano JM, Gaziano TA, Gynn RJ, et al. Light to moderate alcohol consumption and mortality in the Physicians’ Health Study enrolment cohort. J Am Coll Cardiol 2000; 35: 96–105. 46 Celedón G, González G, Pino J, Lissi EA. Peroxynitrite oxidizes erythrocyte membrane band 3 protein and diminishes its anion transport capacity. Free Radic Res 2007; 41: 316–323. 22 44 23 45 24 46 25 47 26 48 27 28 29 30 31 10 32 11 33 12 34 13 35 14 36 15 37 16 38 17 39 18 19 1 2 3 4 5 6 7 8 9 40 41 20 42 21 43 20047071 - Mol Cell Biochem. 2010 Jun;339(1-2):35-42 24122554 - Cell Stress Chaperones. 2014 May;19(3):299-309 17942752 - Blood. 2008 Jan 15;111(2):932-8 18690862 - Curr Clin Pharmacol. 2007 May;2(2):145-53 17237348 - Physiol Rev. 2007 Jan;87(1):315-424 12965884 - Am J Epidemiol. 2003 Sep 15;158(6):585-95 23345910 - J Biol Phys. 2005 Dec;31(3-4):453-64 21071519 - Clin J Am Soc Nephrol. 2011 Mar;6(3):648-55 21262864 - Hum Exp Toxicol. 2011 Oct;30(10):1475-81 22445806 - Alcohol. 2012 May;46(3):235-43 15706762 - Alcohol Health Res World. 1997;21(1):42-52 16294219 - J Clin Invest. 2005 Dec;115(12):3409-17 15608601 - Alcohol Clin Exp Res. 2004 Dec;28(12):1849-60 17364960 - Free Radic Res. 2007 Mar;41(3):316-23 10636266 - J Am Coll Cardiol. 2000 Jan;35(1):96-105 25710019 - Biomed Res Int. 2015;2015:682054 23966453 - Alcohol Alcohol. 2013 Nov-Dec;48(6):679-86 23801928 - Transfus Med Hemother. 2012 Oct;39(5):353-61 20716923 - Oxid Med Cell Longev. 2010 Jan-Feb;3(1):2-12 18249269 - Alcohol. 2008 Feb;42(1):47-53 19454300 - Food Chem Toxicol. 2009 Aug;47(8):1958-63 16447273 - Hepatology. 2006 Feb;43(2 Suppl 1):S63-74 18558362 - Autoimmun Rev. 2008 Jun;7(6):457-62 24453417 - Mediators Inflamm. 2013;2013:432616 17609430 - Blood. 2007 Oct 1;110(7):2708-17 21474668 - Blood. 2011 Jun 2;117(22):5998-6006 21282047 - Exp Toxicol Pathol. 2012 Nov;64(7-8):697-703 19303001 - Clin Biochem. 2009 Jul;42(10-11):1041-5 12107033 - Alcohol Alcohol. 2002 Jul-Aug;37(4):327-9 23617072 - Indian J Biochem Biophys. 2013 Feb;50(1):32-9 10331079 - Annu Rev Pharmacol Toxicol. 1999;39:127-50 12069417 - Anal Biochem. 2002 Jul 1;306(1):79-82 16630710 - Biochim Biophys Acta. 2006 May;1762(5):558-63 5432063 - Nature. 1970 Aug 15;227(5259):680-5 24393670 - Pathophysiology. 2014 Jun;21(2):153-9 12884412 - J Appl Toxicol. 2003 Jul-Aug;23(4):275-8 1947716 - Scand J Clin Lab Invest. 1991 Jun;51(4):309-19 23691267 - Oxid Med Cell Longev. 2013;2013:781050 11113633 - Biochim Biophys Acta. 2000 Dec 15;1535(1):69-77 9775400 - Prog Neurobiol. 1998 Nov;56(4):385-431 16567836 - Diabetes Care. 2006 Apr;29(4):908-13 6161559 - Anal Biochem. 1980 Jul 1;105(2):361-3 23311696 - Antioxid Redox Signal. 2013 Oct 10;19(11):1198-208 18977338 - Chem Phys Lipids. 2009 Jan;157(1):1-11 16368881 - Blood. 2006 Apr 1;107(7):2943-51 18266954 - J Cell Mol Med. 2008 Jun;12(3):829-75 12620706 - Am J Hypertens. 2003 Mar;16(3):244-8 |
| References_xml | – reference: 14 Büyükokuroğlu ME, Altikat S, Ciftçi M. The effect of ethanol on glucose-6-phosphate dehydrogenase enzyme activity from human erythrocytes in vitro and rat erythrocytes in vivo. Alcohol Alcoholism 2002; 37: 327–329. – reference: 2 Gaziano JM, Gaziano TA, Gynn RJ, et al. Light to moderate alcohol consumption and mortality in the Physicians’ Health Study enrolment cohort. J Am Coll Cardiol 2000; 35: 96–105. – reference: 37 Pandey KB, Rizvi SI. Markers of oxidative stress in erythrocytes and plasma during aging in humans. Oxid Med Cell Longev 2012; 3: 2–12. – reference: 46 Celedón G, González G, Pino J, Lissi EA. Peroxynitrite oxidizes erythrocyte membrane band 3 protein and diminishes its anion transport capacity. Free Radic Res 2007; 41: 316–323. – reference: 24 Gallagher PG, Jarolim P. Red blood cell membrane disorders. In: Hoffman R, Benz EJ Jr., Shattil SJ, et al, eds. Hematology: Basic Principles and Practice. Philadelphia, PA: Churchill Livingstone, 2009; 623–643. – reference: 44 Zennadi R, Moeller BJ, Whalen EJ, et al. Epinephrine-induced activation of LW-mediated sickle cell adhesion and vaso-occlusion in vivo. Blood 2007; 110: 2708–2717. – reference: 1 Maturu P, Reddy VD, Padmavathi P, Varadacharyulu N. Ethanol induced adaptive changes in blood for the pathological and toxicological effects of chronic ethanol consumption in humans. Exp Taxicol Pathol 2012; 64: 697–703. – reference: 17 Pacher P, Beckman JS, Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 2007; 87: 315–424. – reference: 36 Catalá A. Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem Phys Lipids 2009; 157: 1–11. – reference: 21 Fadda F, Rossetti ZL. Chronic ethanol consumption: from neuroadaptation to neurodegeneration. Prog Neurobiol 1998; 56: 385–431. – reference: 42 Stibler H, Beaugé F, Leguicher A, Borg S. Biophysical and biochemical alterations in erythrocyte membranes from chronic alcoholics. Scand J Clin Lab Invest 1991; 51: 309–319. – reference: 7 Song BJ, Abdelmegeed MA, Henderson LE, et al. Increased nitroxidative stress promotes mitochondrial dysfunction in alcoholic and non-alcoholic fatty liver disease. Oxid Med Cell Longev 2013; 2013: 781050. – reference: 32 Oakley BR, Kirsch DR, Morris NR. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 1980; 105: 361–363. – reference: 26 Padmavathi P, Damodara Reddy V, Narendra M, Varadacharyulu N. Bidis--hand-rolled, Indian cigarettes: induced biochemical changes in plasma and red membranes of human male volunteers. Clin Biochem 2009; 42: 1041–1045. – reference: 45 Ferru E, Giger K, Pantaleo A, et al. Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3. Blood 2011; 117: 5998–6006. – reference: 4 Klatsky AL, Friedman GD, Armstrong MA, Kipp H. Wine, liquor, beer and mortality. Am J Epidemol 2003; 158: 585–595. – reference: 19 Gov N, Safran SA. Red blood cell shape and fluctuations: cytoskeleton confinement and ATP activity. J Biolgic Phys 2005; 31: 453–464. – reference: 22 Tóth ME, Vigh L, Sántha M. Alcohol stress, membranes and chaperones. Cell Stress Chaperones 2014; 19: 299–309. – reference: 3 Englund Ogge L, Brohall G, Behre CJ, Schmidt C, Fagerberg B. Alcohol consumption in relation to metabolic regulation, inflammation and adiponectin in 64-year-old Caucasian women: a population-based study with a focus on impaired glucose regulation. Diabetes Care 2006; 29: 908–913. – reference: 28 Reddy VD, Padmavathi P, Hymavathi R, Maturu P, Varadacharyulu NCh. Alcohol-induced oxidative stress in rat liver microsomes: protective effect of Emblica officinalis. Pathophysiology 2014; 21: 153–159. – reference: 15 Minneci PC, Deans KJ, Zhi H, et al. Hemolysis-associated endothelial dysfunction mediated by acceleration NO inactivation by decompartmentalized oxyhemoglobin. J Clin Invest 2005; 115: 3409–3417. – reference: 31 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685. – reference: 41 Muriel P, Castañeda G, Ortega M, Noël F. Insights into the mechanism of erythrocyte Na+/K+-ATPase inhibition by nitric oxide and peroxynitrite anion. J Appl Toxicol 2003; 23: 275–278. – reference: 5 Durazzo TC, Gazdzinski S, Banys P, Meyerhoff DJ. Cigarette smoking exacerbates chronic alcohol-induced brain damage: a preliminary metabolic imaging study. Alcohol Clin Exp Res 2004; 28: 1849–1860. – reference: 35 Maturu P, Vaddi DR, Pannuru P, Nallanchakravarthula V. Alterations in erythrocyte membrane fluidity and Na+/K+-ATPase activity in chronic alcoholics. Mol Cell Biochem 2010; 339: 35–42. – reference: 38 Tsuda K, Kinoshita-Shimamoto Y, Kimura K, Nishio I. Nitric oxide is a determinant of membrane fluidity of erythrocytes in postmenopausal woman: an electron paramagnetic resonance investigation. Am J Hypertens 2003; 16: 244–248. – reference: 13 Ballard HS. The haematological complications of alcoholism. Alcohol Health Res World 1997; 21: 42–52. – reference: 29 Kavitha G, Damodara Reddy V, Paramahamsa M, Akhtar PM, Varadacharyulu NC. Role of nitric oxide in alcohol-induced changes in lipid profile of moderate and heavy alcoholics. Alcohol 2008; 42: 47–53. – reference: 43 Tyulina OV, Prokopieva VD, Boldyrev AA, Johnson P. Erythrocyte and plasma protein modification in alcoholism: a possible role of acetaldehyde. Biochim Biophys Acta 2006; 1762: 558–563. – reference: 23 Alimi H, Hfaeidh N, Bouoni Z, Sakly M, Ben Rhouma K. Protective effect of Opuntia ficus indica f. Inermis prickly pear juice upon ethanol-induced damages in rat erythrocytes. Alcohol 2012; 46: 235–243. – reference: 11 Maio R, Siacqua A, Bruni R, et al. Association between hemoglobin level and endothelial function in uncomplicated untreated hypertensive patients. Clin J Am Sco Nephrol 2011; 6: 648–655. – reference: 10 Tyulina OV, Huentelman MJ, Prokopieva VD, Boldyrev AA, Johnson P. Does ethanol metabolism affect erythrocyte hemolysis? Biochem Biophys Act 2000; 1535: 69–77. – reference: 33 Dey A, Cederbaum AI. Alcohol and oxidative liver injury. Hepatology 2006; 43 (2 Suppl 1): S63–S74. – reference: 16 Kleinbongard P, Schulz R, Rassaf T, et al. Red blood cells express a functional endothelial nitric oxide synthase. Blood 2006; 107: 2943–2951. – reference: 48 Chu H, Breite A, Ciraolo P, Franco RS, Low PS. Characterization of the deoxyhemoglobin binding site on human erythrocyte band 3: implications for O2 regulation of erythrocyte properties. Blood 2008; 111: 932–938. – reference: 27 Sastry KV, Moudgal RP, Mohan J, Tyagi JS, Rao GS. Spectrophotometric determination of serum nitrite and nitrate by copper-cadmium alloy. Anal Biochem 2002; 306: 79–82. – reference: 39 Maturu P, Vaddi DR, Pannuru P, Nallanchakravarthula V. Modifications of erythrocyte membrane proteins, enzymes and transport mechanisms in chronic alcoholics: an in vivo and in vitro study. Alcohol Alcohol 2013; 48: 679–686. – reference: 18 Owusu BY, Stapley R, Honavar J, Patel RP. Effects of erythrocyte aging on nitric oxide and nitrite metabolism. Antioxid Redox Signal 2013; 19: 1198–1208. – reference: 20 Escribá PV, González-Ros JM, Goñi FM, et al. Membranes: a meeting point for lipids, proteins and therapies. J Cell Mol Med 2008; 12: 829–875. – reference: 30 Pannuru P, Vaddi DR, Kindinti RR, Varadacharyulu N. Increased erythrocyte antioxidant status protects against smoking induced hemolysis in moderate smokers. Hum Exp Toxicol 2011; 30: 1475–1481. – reference: 6 Baker RC, Kramer RE. Cytotoxicity of short-chain alcohols. Annu Rev Pharmacol Toxicol 1999; 39: 127–150. – reference: 9 Straat M, van Bruggen R, de Korte D, Juffermans NP. Red blood cell clearance in inflammation. Trandus Med Hemother 2012; 39: 353–361. – reference: 47 Pantaleo A, Giribaldi G, Mannu F, Arese P, Turrini F. Naturally occurring anti-band 3 antibodies and red blood cell removal under physiological and pathological conditions. Autoimmun Rev 2008; 7: 457–462. – reference: 12 Mozos I. Mechanisms linking red blood cell disorders and cardiovascular diseases. BioMed Res Int 2015; 2015: 682054. – reference: 25 Ciccoli L, De Felice C, Paccagnini E, et al. Erythrocyte shape abnormalities, membrane oxidative damage and β-actin alterations: an unrecognised triad in classical autism. Mediators Inflamm 2013; 2013: 432616. – reference: 40 Deng XS, Deitrich RA. Ethanol metabolism and effects: nitric oxide and its interaction. Curr Clin Pharmacol 2007; 2: 145–153. – reference: 34 Reddy VD, Padmavathi P, Paramahamsa M, Varadacharyulu N. Modulatory role of Emblica officinalis against alcohol induced biochemical and biophysical changes in rat erythrocyte membranes. Food Chem Toxicol 2009; 47: 1958–1963. – reference: 8 Reddy KR, Reddy VD, Padmavathi P, Kavitha G, Saradamma B, Varadacharyulu NC. Gender differences in alcohol-induced oxidative stress and altered membrane properties in erythrocytes of rats. Indian J Biochem Biophys 2013; 50: 32–39. – ident: 15 doi: 10.1172/JCI25040 – ident: 37 doi: 10.4161/oxim.3.1.10476 – ident: 2 doi: 10.1016/S0735-1097(99)00531-8 – ident: 47 doi: 10.1016/j.autrev.2008.03.017 – ident: 42 doi: 10.3109/00365519109091621 – ident: 11 doi: 10.2215/CJN.06920810 – ident: 31 doi: 10.1038/227680a0 – ident: 17 doi: 10.1152/physrev.00029.2006 – ident: 21 doi: 10.1016/S0301-0082(98)00032-X – ident: 7 doi: 10.1155/2013/781050 – ident: 43 doi: 10.1016/j.bbadis.2006.03.003 – ident: 27 doi: 10.1006/abio.2002.5676 – ident: 23 doi: 10.1016/j.alcohol.2011.09.024 – ident: 6 doi: 10.1146/annurev.pharmtox.39.1.127 – ident: 28 doi: 10.1016/j.pathophys.2013.12.001 – ident: 48 doi: 10.1182/blood-2007-07-100180 – ident: 22 doi: 10.1007/s12192-013-0472-5 – ident: 30 doi: 10.1177/0960327110396527 – ident: 44 doi: 10.1182/blood-2006-11-056101 – ident: 34 doi: 10.1016/j.fct.2009.05.014 – ident: 38 doi: 10.1016/S0895-7061(02)03261-2 – ident: 12 doi: 10.1155/2015/682054 – ident: 10 doi: 10.1016/S0925-4439(00)00086-7 – ident: 18 doi: 10.1089/ars.2012.4884 – ident: 19 doi: 10.1007/s10867-005-6472-7 – ident: 24 – ident: 46 doi: 10.1080/10715760601090305 – ident: 45 doi: 10.1182/blood-2010-11-317024 – ident: 26 doi: 10.1016/j.clinbiochem.2009.03.005 – ident: 5 doi: 10.1097/01.ALC.0000148112.92525.AC – ident: 32 doi: 10.1016/0003-2697(80)90470-4 – ident: 33 doi: 10.1002/hep.20957 – ident: 16 doi: 10.1182/blood-2005-10-3992 – ident: 14 doi: 10.1093/alcalc/37.4.327 – ident: 29 doi: 10.1016/j.alcohol.2007.10.006 – ident: 13 – ident: 9 doi: 10.1159/000342229 – ident: 20 doi: 10.1111/j.1582-4934.2008.00281.x – ident: 3 doi: 10.2337/diacare.29.04.06.dc05-1782 – ident: 25 doi: 10.1155/2013/432616 – ident: 1 doi: 10.1016/j.etp.2011.01.002 – ident: 36 doi: 10.1016/j.chemphyslip.2008.09.004 – ident: 39 doi: 10.1093/alcalc/agt071 – ident: 41 doi: 10.1002/jat.922 – ident: 8 – ident: 35 doi: 10.1007/s11010-009-0367-z – ident: 4 doi: 10.1093/aje/kwg184 – ident: 40 doi: 10.2174/157488407780598135 – reference: 17364960 - Free Radic Res. 2007 Mar;41(3):316-23 – reference: 23801928 - Transfus Med Hemother. 2012 Oct;39(5):353-61 – reference: 23311696 - Antioxid Redox Signal. 2013 Oct 10;19(11):1198-208 – reference: 21282047 - Exp Toxicol Pathol. 2012 Nov;64(7-8):697-703 – reference: 22445806 - Alcohol. 2012 May;46(3):235-43 – reference: 12107033 - Alcohol Alcohol. 2002 Jul-Aug;37(4):327-9 – reference: 24453417 - Mediators Inflamm. 2013;2013:432616 – reference: 17609430 - Blood. 2007 Oct 1;110(7):2708-17 – reference: 16630710 - Biochim Biophys Acta. 2006 May;1762(5):558-63 – reference: 17237348 - Physiol Rev. 2007 Jan;87(1):315-424 – reference: 15608601 - Alcohol Clin Exp Res. 2004 Dec;28(12):1849-60 – reference: 12620706 - Am J Hypertens. 2003 Mar;16(3):244-8 – reference: 11113633 - Biochim Biophys Acta. 2000 Dec 15;1535(1):69-77 – reference: 18266954 - J Cell Mol Med. 2008 Jun;12(3):829-75 – reference: 21474668 - Blood. 2011 Jun 2;117(22):5998-6006 – reference: 5432063 - Nature. 1970 Aug 15;227(5259):680-5 – reference: 9775400 - Prog Neurobiol. 1998 Nov;56(4):385-431 – reference: 23617072 - Indian J Biochem Biophys. 2013 Feb;50(1):32-9 – reference: 16368881 - Blood. 2006 Apr 1;107(7):2943-51 – reference: 17942752 - Blood. 2008 Jan 15;111(2):932-8 – reference: 23966453 - Alcohol Alcohol. 2013 Nov-Dec;48(6):679-86 – reference: 10331079 - Annu Rev Pharmacol Toxicol. 1999;39:127-50 – reference: 21071519 - Clin J Am Soc Nephrol. 2011 Mar;6(3):648-55 – reference: 24122554 - Cell Stress Chaperones. 2014 May;19(3):299-309 – reference: 20047071 - Mol Cell Biochem. 2010 Jun;339(1-2):35-42 – reference: 21262864 - Hum Exp Toxicol. 2011 Oct;30(10):1475-81 – reference: 10636266 - J Am Coll Cardiol. 2000 Jan;35(1):96-105 – reference: 18558362 - Autoimmun Rev. 2008 Jun;7(6):457-62 – reference: 16567836 - Diabetes Care. 2006 Apr;29(4):908-13 – reference: 12884412 - J Appl Toxicol. 2003 Jul-Aug;23(4):275-8 – reference: 1947716 - Scand J Clin Lab Invest. 1991 Jun;51(4):309-19 – reference: 16447273 - Hepatology. 2006 Feb;43(2 Suppl 1):S63-74 – reference: 18690862 - Curr Clin Pharmacol. 2007 May;2(2):145-53 – reference: 20716923 - Oxid Med Cell Longev. 2010 Jan-Feb;3(1):2-12 – reference: 25710019 - Biomed Res Int. 2015;2015:682054 – reference: 12069417 - Anal Biochem. 2002 Jul 1;306(1):79-82 – reference: 19303001 - Clin Biochem. 2009 Jul;42(10-11):1041-5 – reference: 18249269 - Alcohol. 2008 Feb;42(1):47-53 – reference: 19454300 - Food Chem Toxicol. 2009 Aug;47(8):1958-63 – reference: 16294219 - J Clin Invest. 2005 Dec;115(12):3409-17 – reference: 15706762 - Alcohol Health Res World. 1997;21(1):42-52 – reference: 6161559 - Anal Biochem. 1980 Jul 1;105(2):361-3 – reference: 12965884 - Am J Epidemiol. 2003 Sep 15;158(6):585-95 – reference: 24393670 - Pathophysiology. 2014 Jun;21(2):153-9 – reference: 18977338 - Chem Phys Lipids. 2009 Jan;157(1):1-11 – reference: 23345910 - J Biol Phys. 2005 Dec;31(3-4):453-64 – reference: 23691267 - Oxid Med Cell Longev. 2013;2013:781050 |
| SSID | ssj0046564 |
| Score | 2.2354612 |
| Snippet | The present study aimed to understand the association between erythrocyte membrane alterations and hemolysis in chronic alcoholics. Study was conducted on... |
| SourceID | pubmedcentral proquest pubmed crossref jstage |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 63 |
| SubjectTerms | Actin alcohol Alcoholics Alcoholism Ankyrins Carbonyl compounds Carbonyls Cholesterol Cytology Cytoskeleton Drinking behavior erythrocyte membrane Erythrocytes Gel electrophoresis Glyceraldehyde Glyceraldehyde 3-phosphate Glyceraldehyde-3-phosphate dehydrogenase Hemolysis Lipid peroxidation Lipids Membrane proteins Membranes Morphology Nitric oxide Nitrogen oxides Original Oxidation oxidative/nitrosative stress Peroxidation Phospholipids Protein 4.1 Proteins SDS-PAGE Sodium lauryl sulfate |
| Title | Association between alcohol-induced erythrocyte membrane alterations and hemolysis in chronic alcoholics |
| URI | https://www.jstage.jst.go.jp/article/jcbn/60/1/60_16-16/_article/-char/en https://www.ncbi.nlm.nih.gov/pubmed/28163384 https://www.proquest.com/docview/2338999798 https://www.proquest.com/docview/1865520949 https://pubmed.ncbi.nlm.nih.gov/PMC5281527 |
| Volume | 60 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| ispartofPNX | Journal of Clinical Biochemistry and Nutrition, 2017, Vol.60(1), pp.63-69 |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fa9swED7aboy9jK775a0tGhuDPbi1LVmyHkYp20rZSGGwQN-MJMtLSuJsiQvLf7-TZJum5Glg_GCdbNDdWd_ppO8A3osskUbrKhZJYmJGbR4XmWSxNjbFJ7YWvlrD6Ipfjtm36_x6B_r6nd0ArraGdq6e1Hg5O_n7Z32GDv_JR5ycnd4Y3ZykPE75LjzAGUk4Bx2xIZvgKME8jZR02xAQVASa0nt9HS1wgeiEFmxjjnp4gzDtl92GQO9vpLwzM13sw5MOUpLzYANPYcc2BxB9mdqWfCAd7-eMXPW0-wfwaNQl1J_B5I56SLdni6hQNjfGcB0VXxG7XLtqCmbdWjK3c4yvG0t8mj0s9xHVVGRi5wtPb0KmDTGBcrd_09SsnsP44uvPz5dxV3whNjxnbYyeXuPcTxVXRmYG_6eFUgjWtDIYQVUZE7KWBaWV5CJFS6hqFCvqxOSO04hy-gL2mkVjXwGRUmtNqcgc-59OjEIxqfLK1lwjAqsi-NgPd2k6ZnJXIGNWYoTitFQ6LZUpxyuCd4Ps78DHsVVKBq0NMp0fBhmOgY-_OdmhyR1zw39FBIe9osveHMuMOh5CKWQRwduhGT3RpVdw0Be3qzJ1Z3zR9JmM4GWwi-HzvWVFIDYsZhBwLN-bLc104tm-c-ybZ-L1f_d8A48zh0X8utEh7LXLW3uESKrVx7D7_Udx7J3lHw-II0M |
| linkProvider | Scholars Portal |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Association+between+alcohol-induced+erythrocyte+membrane+alterations+and+hemolysis+in+chronic+alcoholics&rft.jtitle=Journal+of+clinical+biochemistry+and+nutrition&rft.au=Bulle%2C+Saradamma&rft.au=Reddy%2C+Vaddi+Damodara&rft.au=Padmavathi%2C+Pannuru&rft.au=Maturu%2C+Paramahamsa&rft.date=2017-01-01&rft.pub=the+Society+for+Free+Radical+Research+Japan&rft.issn=0912-0009&rft.eissn=1880-5086&rft.volume=60&rft.issue=1&rft.spage=63&rft.epage=69&rft_id=info:doi/10.3164%2Fjcbn.16-16&rft_id=info%3Apmid%2F28163384&rft.externalDocID=PMC5281527 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0912-0009&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0912-0009&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0912-0009&client=summon |