The presence of pyruvate carboxylase in the human brain and its role in the survival of cultured human astrocytes
Pyruvate carboxylase (PC) is a mitochondrial, biotin-containing enzyme catalyzing the ATP-dependent synthesis of oxaloacetate from pyruvate and bicarbonate, with a critical anaplerotic role in sustaining the brain metabolism. Based on the studies performed on animal models, PC expression was assigne...
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| Veröffentlicht in: | Physiological research 2023-07, Vol.72 (3), p.403-414 |
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| creator | Gondáš, E Kráľová Trančíková, A Šofranko, J Majerová, P Lučanský, V Dohál, M Kováč, A Murín, R |
| description | Pyruvate carboxylase (PC) is a mitochondrial, biotin-containing enzyme catalyzing the ATP-dependent synthesis of oxaloacetate from pyruvate and bicarbonate, with a critical anaplerotic role in sustaining the brain metabolism. Based on the studies performed on animal models, PC expression was assigned to be glia-specific. To study PC distribution among human neural cells, we probed the cultured human astrocytes and brain sections with antibodies against PC. Additionally, we tested the importance of PC for the viability of cultured human astrocytes by applying the PC inhibitor 3-chloropropane-1,2-diol (CPD). Our results establish the expression of PC in mitochondria of human astrocytes in culture and brain tissue and also into a subpopulation of the neurons in situ. CPD negatively affected the viability of astrocytes in culture, which could be partially reversed by supplementing media with malate, 2-oxoglutarate, citrate, or pyruvate. The provided data estimates PC expression in human astrocytes and neurons in human brain parenchyma. Furthermore, the enzymatic activity of PC is vital for sustaining the viability of cultured astrocytes. |
| doi_str_mv | 10.33549/physiolres.935026 |
| format | Article |
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Based on the studies performed on animal models, PC expression was assigned to be glia-specific. To study PC distribution among human neural cells, we probed the cultured human astrocytes and brain sections with antibodies against PC. Additionally, we tested the importance of PC for the viability of cultured human astrocytes by applying the PC inhibitor 3-chloropropane-1,2-diol (CPD). Our results establish the expression of PC in mitochondria of human astrocytes in culture and brain tissue and also into a subpopulation of the neurons in situ. CPD negatively affected the viability of astrocytes in culture, which could be partially reversed by supplementing media with malate, 2-oxoglutarate, citrate, or pyruvate. The provided data estimates PC expression in human astrocytes and neurons in human brain parenchyma. Furthermore, the enzymatic activity of PC is vital for sustaining the viability of cultured astrocytes.</description><identifier>ISSN: 0862-8408</identifier><identifier>EISSN: 1802-9973</identifier><identifier>DOI: 10.33549/physiolres.935026</identifier><identifier>PMID: 37449752</identifier><language>eng</language><publisher>Czech Republic: Institute of Physiology</publisher><subject>Animal models ; Animals ; Antibodies ; Astrocytes ; Astrocytes - metabolism ; Bicarbonates ; Biotin ; Brain ; Brain - metabolism ; Carbon ; Cell culture ; Dehydrogenases ; Enzymatic activity ; Enzymes ; Glucose ; Humans ; Hypotheses ; Ketoglutaric acid ; Laboratories ; Metabolism ; Metabolites ; Neuronal-glial interactions ; Neurons ; Neurons - metabolism ; Parenchyma ; Proteins ; Pyruvate carboxylase ; Pyruvate Carboxylase - metabolism ; Pyruvic acid ; Pyruvic Acid - metabolism ; Tissue culture ; Viability</subject><ispartof>Physiological research, 2023-07, Vol.72 (3), p.403-414</ispartof><rights>Copyright Institute of Physiology 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c342t-82742107d6ab045fef5cbd5a77b105a315523459b3eedd82e0542ac635cc8fca3</citedby><cites>FETCH-LOGICAL-c342t-82742107d6ab045fef5cbd5a77b105a315523459b3eedd82e0542ac635cc8fca3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,865,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37449752$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gondáš, E</creatorcontrib><creatorcontrib>Kráľová Trančíková, A</creatorcontrib><creatorcontrib>Šofranko, J</creatorcontrib><creatorcontrib>Majerová, P</creatorcontrib><creatorcontrib>Lučanský, V</creatorcontrib><creatorcontrib>Dohál, M</creatorcontrib><creatorcontrib>Kováč, A</creatorcontrib><creatorcontrib>Murín, R</creatorcontrib><title>The presence of pyruvate carboxylase in the human brain and its role in the survival of cultured human astrocytes</title><title>Physiological research</title><addtitle>Physiol Res</addtitle><description>Pyruvate carboxylase (PC) is a mitochondrial, biotin-containing enzyme catalyzing the ATP-dependent synthesis of oxaloacetate from pyruvate and bicarbonate, with a critical anaplerotic role in sustaining the brain metabolism. Based on the studies performed on animal models, PC expression was assigned to be glia-specific. To study PC distribution among human neural cells, we probed the cultured human astrocytes and brain sections with antibodies against PC. Additionally, we tested the importance of PC for the viability of cultured human astrocytes by applying the PC inhibitor 3-chloropropane-1,2-diol (CPD). Our results establish the expression of PC in mitochondria of human astrocytes in culture and brain tissue and also into a subpopulation of the neurons in situ. CPD negatively affected the viability of astrocytes in culture, which could be partially reversed by supplementing media with malate, 2-oxoglutarate, citrate, or pyruvate. The provided data estimates PC expression in human astrocytes and neurons in human brain parenchyma. Furthermore, the enzymatic activity of PC is vital for sustaining the viability of cultured astrocytes.</description><subject>Animal models</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Astrocytes</subject><subject>Astrocytes - metabolism</subject><subject>Bicarbonates</subject><subject>Biotin</subject><subject>Brain</subject><subject>Brain - metabolism</subject><subject>Carbon</subject><subject>Cell culture</subject><subject>Dehydrogenases</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Glucose</subject><subject>Humans</subject><subject>Hypotheses</subject><subject>Ketoglutaric acid</subject><subject>Laboratories</subject><subject>Metabolism</subject><subject>Metabolites</subject><subject>Neuronal-glial interactions</subject><subject>Neurons</subject><subject>Neurons - metabolism</subject><subject>Parenchyma</subject><subject>Proteins</subject><subject>Pyruvate carboxylase</subject><subject>Pyruvate Carboxylase - metabolism</subject><subject>Pyruvic acid</subject><subject>Pyruvic Acid - metabolism</subject><subject>Tissue culture</subject><subject>Viability</subject><issn>0862-8408</issn><issn>1802-9973</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpFkMtOwzAQRS0EoqXwAyyQJdYBx4_aXqKKl1SJTVlHjjNRU6Vx6kdF_p5AS1mNRnPvGekgdJuTB8YE14_9egiNaz2EB80EofMzNM0VoZnWkp2jKVFzmilO1ARdhbAhhEoi2SWaMMm5loJO0W61BtyPBOgsYFfjfvBpbyJga3zpvobWBMBNh-OYW6et6XDpzbibrsJNDNi79nQPye-bvWl_ODa1MXmojiUTond2iBCu0UVt2gA3xzlDny_Pq8Vbtvx4fV88LTPLOI2ZopLTnMhqbkrCRQ21sGUljJRlToRhuRCUcaFLBlBVigIRnBo7Z8JaVVvDZuj-wO292yUIsdi45LvxZUEV1znVQusxRQ8p610IHuqi983W-KHISfFrufi3XBwsj6W7IzqVW6hOlT-t7BsEqX1J</recordid><startdate>20230714</startdate><enddate>20230714</enddate><creator>Gondáš, E</creator><creator>Kráľová Trančíková, A</creator><creator>Šofranko, J</creator><creator>Majerová, P</creator><creator>Lučanský, V</creator><creator>Dohál, M</creator><creator>Kováč, A</creator><creator>Murín, R</creator><general>Institute of Physiology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>4T-</scope><scope>4U-</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BYOGL</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20230714</creationdate><title>The presence of pyruvate carboxylase in the human brain and its role in the survival of cultured human astrocytes</title><author>Gondáš, E ; Kráľová Trančíková, A ; Šofranko, J ; Majerová, P ; Lučanský, V ; Dohál, M ; Kováč, A ; Murín, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c342t-82742107d6ab045fef5cbd5a77b105a315523459b3eedd82e0542ac635cc8fca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Animal models</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Astrocytes</topic><topic>Astrocytes - metabolism</topic><topic>Bicarbonates</topic><topic>Biotin</topic><topic>Brain</topic><topic>Brain - metabolism</topic><topic>Carbon</topic><topic>Cell culture</topic><topic>Dehydrogenases</topic><topic>Enzymatic activity</topic><topic>Enzymes</topic><topic>Glucose</topic><topic>Humans</topic><topic>Hypotheses</topic><topic>Ketoglutaric acid</topic><topic>Laboratories</topic><topic>Metabolism</topic><topic>Metabolites</topic><topic>Neuronal-glial interactions</topic><topic>Neurons</topic><topic>Neurons - metabolism</topic><topic>Parenchyma</topic><topic>Proteins</topic><topic>Pyruvate carboxylase</topic><topic>Pyruvate Carboxylase - metabolism</topic><topic>Pyruvic acid</topic><topic>Pyruvic Acid - metabolism</topic><topic>Tissue culture</topic><topic>Viability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gondáš, E</creatorcontrib><creatorcontrib>Kráľová Trančíková, A</creatorcontrib><creatorcontrib>Šofranko, J</creatorcontrib><creatorcontrib>Majerová, P</creatorcontrib><creatorcontrib>Lučanský, V</creatorcontrib><creatorcontrib>Dohál, M</creatorcontrib><creatorcontrib>Kováč, A</creatorcontrib><creatorcontrib>Murín, R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Docstoc</collection><collection>University Readers</collection><collection>Nursing & Allied Health Database</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>East Europe, Central Europe Database</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Physiological research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gondáš, E</au><au>Kráľová Trančíková, A</au><au>Šofranko, J</au><au>Majerová, P</au><au>Lučanský, V</au><au>Dohál, M</au><au>Kováč, A</au><au>Murín, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The presence of pyruvate carboxylase in the human brain and its role in the survival of cultured human astrocytes</atitle><jtitle>Physiological research</jtitle><addtitle>Physiol Res</addtitle><date>2023-07-14</date><risdate>2023</risdate><volume>72</volume><issue>3</issue><spage>403</spage><epage>414</epage><pages>403-414</pages><issn>0862-8408</issn><eissn>1802-9973</eissn><abstract>Pyruvate carboxylase (PC) is a mitochondrial, biotin-containing enzyme catalyzing the ATP-dependent synthesis of oxaloacetate from pyruvate and bicarbonate, with a critical anaplerotic role in sustaining the brain metabolism. Based on the studies performed on animal models, PC expression was assigned to be glia-specific. To study PC distribution among human neural cells, we probed the cultured human astrocytes and brain sections with antibodies against PC. Additionally, we tested the importance of PC for the viability of cultured human astrocytes by applying the PC inhibitor 3-chloropropane-1,2-diol (CPD). Our results establish the expression of PC in mitochondria of human astrocytes in culture and brain tissue and also into a subpopulation of the neurons in situ. CPD negatively affected the viability of astrocytes in culture, which could be partially reversed by supplementing media with malate, 2-oxoglutarate, citrate, or pyruvate. The provided data estimates PC expression in human astrocytes and neurons in human brain parenchyma. Furthermore, the enzymatic activity of PC is vital for sustaining the viability of cultured astrocytes.</abstract><cop>Czech Republic</cop><pub>Institute of Physiology</pub><pmid>37449752</pmid><doi>10.33549/physiolres.935026</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Animal models Animals Antibodies Astrocytes Astrocytes - metabolism Bicarbonates Biotin Brain Brain - metabolism Carbon Cell culture Dehydrogenases Enzymatic activity Enzymes Glucose Humans Hypotheses Ketoglutaric acid Laboratories Metabolism Metabolites Neuronal-glial interactions Neurons Neurons - metabolism Parenchyma Proteins Pyruvate carboxylase Pyruvate Carboxylase - metabolism Pyruvic acid Pyruvic Acid - metabolism Tissue culture Viability |
| title | The presence of pyruvate carboxylase in the human brain and its role in the survival of cultured human astrocytes |
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