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SM ISO690:2012 COLIN, Mihail, TIMERCAN, Tatiana. Diseases associated with the oxidative decarboxylation of pyruvate. In: Cercetarea în biomedicină și sănătate: calitate, excelență și performanță, Ed. 1, 20-22 octombrie 2021, Chişinău. Chișinău, Republica Moldova: 2021, p. 37. ISBN 978-9975-82-223-7 (PDF).. |
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Cercetarea în biomedicină și sănătate: calitate, excelență și performanță 2021 | ||||||
Conferința "Cercetarea în biomedicină și sănătate: calitate, excelență și performanță" 1, Chişinău, Moldova, 20-22 octombrie 2021 | ||||||
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Pag. 37-37 | ||||||
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Background. The oxidative decarboxylation of pyruvate represents a complex biochemical process. The final product Acetyl-Co-A, is an essential substrate used in various metabolic paths of vital singnificance. Errors in the functioning of this biochemical process generate dangerous patho-metabolic consequences. Objective of the study. Establishing the interdependence between the altered functioning of the dehydrogenase pyruvate complex and the metabolic and tissue manifestations. Material and Methods. Recent publications from electronic journals database as PubMed and ScienceDirectwere selected and examined. Results. The obtained data showed an interrelation between PDHA1 gene mutations that provide instructions for the biosynthesis of the alpha subunit of the PDH enzyme and the decrease in pyruvate oxidative decarboxylation activity. Therefore, the decrease of the functionality of the multienzyme complex PDH, provoke the preferential conversion of pyruvate into lactic acid, which leads to the induction of a pathological state of metabolic acidosis, as well as the decrease of Acetyl-Co-A use in the Krebs' cycle. Lack of PDH causes energy-metabolic deficiencies, distrupting the integrity of nerve tissue, also causing pathological osteo-muscular development of the visceral region of the skull. Conclusion. The multienzyme complex pyruvate dehydrogenase plays a crucial role in the functionality of the oxidative decarboxylation of pyruvate.Thus, PDHA1’s impartial gene expression disrupts pyruvate metabolism, inducing several damages to various tissues. |
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Cuvinte-cheie PyruvateDehydrogenase, pyruvate’smetabolism, PDHA1, Piruvat Dehidrogenaza, metabolismul piruvatului, PDHA1 |
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Cerif XML Export
<?xml version='1.0' encoding='utf-8'?> <CERIF xmlns='urn:xmlns:org:eurocris:cerif-1.5-1' xsi:schemaLocation='urn:xmlns:org:eurocris:cerif-1.5-1 http://www.eurocris.org/Uploads/Web%20pages/CERIF-1.5/CERIF_1.5_1.xsd' xmlns:xsi='http://www.w3.org/2001/XMLSchema-instance' release='1.5' date='2012-10-07' sourceDatabase='Output Profile'> <cfResPubl> <cfResPublId>ibn-ResPubl-144058</cfResPublId> <cfResPublDate>2021</cfResPublDate> <cfStartPage>37</cfStartPage> <cfISBN>978-9975-82-223-7 (PDF).</cfISBN> <cfURI>https://ibn.idsi.md/ro/vizualizare_articol/144058</cfURI> <cfTitle cfLangCode='EN' cfTrans='o'>Diseases associated with the oxidative decarboxylation of pyruvate</cfTitle> <cfKeyw cfLangCode='EN' cfTrans='o'>PyruvateDehydrogenase; pyruvate’smetabolism; PDHA1; Piruvat Dehidrogenaza; metabolismul piruvatului; PDHA1</cfKeyw> <cfAbstr cfLangCode='EN' cfTrans='o'><p>Background. The oxidative decarboxylation of pyruvate represents a complex biochemical process. The final product Acetyl-Co-A, is an essential substrate used in various metabolic paths of vital singnificance. Errors in the functioning of this biochemical process generate dangerous patho-metabolic consequences. Objective of the study. Establishing the interdependence between the altered functioning of the dehydrogenase pyruvate complex and the metabolic and tissue manifestations. Material and Methods. Recent publications from electronic journals database as PubMed and ScienceDirectwere selected and examined. Results. The obtained data showed an interrelation between PDHA1 gene mutations that provide instructions for the biosynthesis of the alpha subunit of the PDH enzyme and the decrease in pyruvate oxidative decarboxylation activity. Therefore, the decrease of the functionality of the multienzyme complex PDH, provoke the preferential conversion of pyruvate into lactic acid, which leads to the induction of a pathological state of metabolic acidosis, as well as the decrease of Acetyl-Co-A use in the Krebs' cycle. Lack of PDH causes energy-metabolic deficiencies, distrupting the integrity of nerve tissue, also causing pathological osteo-muscular development of the visceral region of the skull. Conclusion. The multienzyme complex pyruvate dehydrogenase plays a crucial role in the functionality of the oxidative decarboxylation of pyruvate.Thus, PDHA1’s impartial gene expression disrupts pyruvate metabolism, inducing several damages to various tissues.</p></cfAbstr> <cfAbstr cfLangCode='RO' cfTrans='o'><p>Introducere. Decarboxilarea oxidativă a piruvatului reprezintă un proces biochimic complex. Produsul final Acetil-Co-A este utilizat ca substrat esențial în diverse căi metabolice de importanță vitală. Erorile în funcționarea acestui proces biochimic provoacă consecințe patometabolice periculoase. Scopul lucrării. Analiza și sistematizarea datelor actuale, referitor la deficiența complexului multienzimatic piruvat de hidrogenază, cu evidențierea urmărilor metabolice și tisulare. Material și Metode. Au fost selectate și examinate publicațiile recente din revistele de specialitate, din bazele de date electronice PubMed și ScienceDirect. Rezultate. S-a depistat o interdependență între mutațiile genei PDHA1, care oferă instrucțiuni pentru biosinteza subunității alpha a enzimei PDH și scăderea randamentului decarboxilării oxidative a piruvatului. Prin urmare, scăderea funcționalității complexului multienzimatic PDH, provoacă conversia preferențială a piruvatului în acid lactic, determinând instalarea unei stări patologice de acidoză metabolică, cât și scăderea utilizării Acetil-Co-A în ciclul acizilor tricarboxilici (ciclul Krebs). Deficitiul PDH produce carențe energitico-metabolice, stimulând apariția leziunilor la nivelul țesutului nervos cât și la dezvoltarea patologică osteo-musculară a viscerocraniului. Concluzii. Complexul multienzimatic PDH joacă un rol crucial în derularea corectă a decarboxilării oxidative a piruvatului. Astfel, expresia imparțială a genei PDHA1 dereglează metabolismul piruvatului, inducând leziuni grave la nivelul diferitor țesuturi.</p></cfAbstr> <cfResPubl_Class> <cfClassId>eda2d9e9-34c5-11e1-b86c-0800200c9a66</cfClassId> <cfClassSchemeId>759af938-34ae-11e1-b86c-0800200c9a66</cfClassSchemeId> <cfStartDate>2021T24:00:00</cfStartDate> </cfResPubl_Class> <cfResPubl_Class> <cfClassId>e601872f-4b7e-4d88-929f-7df027b226c9</cfClassId> <cfClassSchemeId>40e90e2f-446d-460a-98e5-5dce57550c48</cfClassSchemeId> <cfStartDate>2021T24:00:00</cfStartDate> </cfResPubl_Class> <cfPers_ResPubl> <cfPersId>ibn-person-94505</cfPersId> <cfClassId>49815870-1cfe-11e1-8bc2-0800200c9a66</cfClassId> <cfClassSchemeId>b7135ad0-1d00-11e1-8bc2-0800200c9a66</cfClassSchemeId> <cfStartDate>2021T24:00:00</cfStartDate> </cfPers_ResPubl> <cfPers_ResPubl> <cfPersId>ibn-person-29289</cfPersId> <cfClassId>49815870-1cfe-11e1-8bc2-0800200c9a66</cfClassId> <cfClassSchemeId>b7135ad0-1d00-11e1-8bc2-0800200c9a66</cfClassSchemeId> <cfStartDate>2021T24:00:00</cfStartDate> </cfPers_ResPubl> </cfResPubl> <cfPers> <cfPersId>ibn-Pers-94505</cfPersId> <cfPersName_Pers> <cfPersNameId>ibn-PersName-94505-3</cfPersNameId> <cfClassId>55f90543-d631-42eb-8d47-d8d9266cbb26</cfClassId> <cfClassSchemeId>7375609d-cfa6-45ce-a803-75de69abe21f</cfClassSchemeId> <cfStartDate>2021T24:00:00</cfStartDate> <cfFamilyNames>Colin</cfFamilyNames> <cfFirstNames>Mihail</cfFirstNames> </cfPersName_Pers> </cfPers> <cfPers> <cfPersId>ibn-Pers-29289</cfPersId> <cfPersName_Pers> <cfPersNameId>ibn-PersName-29289-3</cfPersNameId> <cfClassId>55f90543-d631-42eb-8d47-d8d9266cbb26</cfClassId> <cfClassSchemeId>7375609d-cfa6-45ce-a803-75de69abe21f</cfClassSchemeId> <cfStartDate>2021T24:00:00</cfStartDate> <cfFamilyNames>Timercan</cfFamilyNames> <cfFirstNames>Tatiana</cfFirstNames> </cfPersName_Pers> </cfPers> </CERIF>