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Expression of lactate dehydrogenase A and B isoforms in the mouse kidney
Cellular metabolic rates in the kidney are critical for maintaining normal renal function. In a hypoxic milieu, cells rely on glycolysis to meet energy needs, resulting in the generation of pyruvate and NADH. In the absence of oxidative phosphorylation, the continuation of glycolysis is dependent on...
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Published in: | American journal of physiology. Renal physiology 2021-05, Vol.320 (5), p.F706-F718 |
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description | Cellular metabolic rates in the kidney are critical for maintaining normal renal function. In a hypoxic milieu, cells rely on glycolysis to meet energy needs, resulting in the generation of pyruvate and NADH. In the absence of oxidative phosphorylation, the continuation of glycolysis is dependent on the regeneration of NAD
from NADH accompanied by the fermentation of pyruvate to lactate. This reaction is catalyzed by lactate dehydrogenase (LDH) isoform A (LDHA), whereas LDH isoform B (LDHB) catalyzes the opposite reaction. LDH is widely used as a potential injury marker as it is released from damaged cells into the urine and serum; however, the precise isoform-specific cellular localization of the enzyme along the nephron has not been characterized. By combining immunohistochemistry results and single-cell RNA-sequencing data on healthy mouse kidneys, we identified that LDHA is primarily expressed in proximal segments, whereas LDHB is expressed in the distal parts of the nephron. In vitro experiments in mouse and human renal proximal tubule cells showed an increase in LDHA following hypoxia with no change in LDHB. Using immunofluorescence, we observed that the overall expression of both LDHA and LDHB proteins decreased following renal ischemia-reperfusion injury as well as in the adenine-diet-induced model of chronic kidney disease. Single-nucleus RNA-sequencing analyses of kidneys following ischemia-reperfusion injury revealed a significant decline in the number of cells expressing detectable levels of
and
; however, cells that were positive showed increased average expression postinjury, which subsided during the recovery phase. These data provide information on the cell-specific expression of LDHA and LDHB in the normal kidney as well as following acute and chronic kidney disease.
Cellular release of lactate dehydrogenase (LDH) is being used as an injury marker; however, the exact localization of LDH within the nephron remains unclear. We show that LDH isoform A is expressed proximally, whereas isoform B is expressed distally. Both subunit expressions were significantly altered in models of acute kidney injury and chronic kidney disease. Our study provides new insights into basal and postinjury renal lactate metabolism. |
doi_str_mv | 10.1152/ajprenal.00628.2020 |
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from NADH accompanied by the fermentation of pyruvate to lactate. This reaction is catalyzed by lactate dehydrogenase (LDH) isoform A (LDHA), whereas LDH isoform B (LDHB) catalyzes the opposite reaction. LDH is widely used as a potential injury marker as it is released from damaged cells into the urine and serum; however, the precise isoform-specific cellular localization of the enzyme along the nephron has not been characterized. By combining immunohistochemistry results and single-cell RNA-sequencing data on healthy mouse kidneys, we identified that LDHA is primarily expressed in proximal segments, whereas LDHB is expressed in the distal parts of the nephron. In vitro experiments in mouse and human renal proximal tubule cells showed an increase in LDHA following hypoxia with no change in LDHB. Using immunofluorescence, we observed that the overall expression of both LDHA and LDHB proteins decreased following renal ischemia-reperfusion injury as well as in the adenine-diet-induced model of chronic kidney disease. Single-nucleus RNA-sequencing analyses of kidneys following ischemia-reperfusion injury revealed a significant decline in the number of cells expressing detectable levels of
and
; however, cells that were positive showed increased average expression postinjury, which subsided during the recovery phase. These data provide information on the cell-specific expression of LDHA and LDHB in the normal kidney as well as following acute and chronic kidney disease.
Cellular release of lactate dehydrogenase (LDH) is being used as an injury marker; however, the exact localization of LDH within the nephron remains unclear. We show that LDH isoform A is expressed proximally, whereas isoform B is expressed distally. Both subunit expressions were significantly altered in models of acute kidney injury and chronic kidney disease. Our study provides new insights into basal and postinjury renal lactate metabolism.</description><identifier>ISSN: 1931-857X</identifier><identifier>EISSN: 1522-1466</identifier><identifier>DOI: 10.1152/ajprenal.00628.2020</identifier><identifier>PMID: 33719570</identifier><language>eng</language><publisher>United States: American Physiological Society</publisher><subject>Acute Kidney Injury - enzymology ; Acute Kidney Injury - genetics ; Acute Kidney Injury - pathology ; Adenine ; Animals ; Biomarkers - metabolism ; Cell Hypoxia ; Cells, Cultured ; Dehydrogenases ; Disease Models, Animal ; Fermentation ; Gene Expression Regulation, Enzymologic ; Glycolysis ; Humans ; Hypoxia ; Immunofluorescence ; Immunohistochemistry ; Ischemia ; Isoenzymes ; Isoforms ; Kidney - enzymology ; Kidney - pathology ; Kidney diseases ; L-Lactate dehydrogenase ; L-Lactate Dehydrogenase - genetics ; L-Lactate Dehydrogenase - metabolism ; Lactic acid ; Localization ; Male ; Metabolic rate ; Mice ; Mice, Inbred C57BL ; NAD ; NADH ; Oxidative phosphorylation ; Phosphorylation ; Pyruvic acid ; Renal function ; Renal Insufficiency, Chronic - enzymology ; Renal Insufficiency, Chronic - genetics ; Renal Insufficiency, Chronic - pathology ; Reperfusion ; Time Factors</subject><ispartof>American journal of physiology. Renal physiology, 2021-05, Vol.320 (5), p.F706-F718</ispartof><rights>Copyright American Physiological Society May 2021</rights><rights>Published by the American Physiological Society 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-4719392d9759508007a6cbfa5b57c81f717b9dc5f4538f3f9714c30682390c43</citedby><cites>FETCH-LOGICAL-c499t-4719392d9759508007a6cbfa5b57c81f717b9dc5f4538f3f9714c30682390c43</cites><orcidid>0000-0003-4276-5186 ; 0000-0002-0613-737X ; 0000-0002-4096-4897</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,786,790,891,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33719570$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Osis, Gunars</creatorcontrib><creatorcontrib>Traylor, Amie M</creatorcontrib><creatorcontrib>Black, Laurence M</creatorcontrib><creatorcontrib>Spangler, Daryll</creatorcontrib><creatorcontrib>George, James F</creatorcontrib><creatorcontrib>Zarjou, Abolfazl</creatorcontrib><creatorcontrib>Verlander, Jill W</creatorcontrib><creatorcontrib>Agarwal, Anupam</creatorcontrib><title>Expression of lactate dehydrogenase A and B isoforms in the mouse kidney</title><title>American journal of physiology. Renal physiology</title><addtitle>Am J Physiol Renal Physiol</addtitle><description>Cellular metabolic rates in the kidney are critical for maintaining normal renal function. In a hypoxic milieu, cells rely on glycolysis to meet energy needs, resulting in the generation of pyruvate and NADH. In the absence of oxidative phosphorylation, the continuation of glycolysis is dependent on the regeneration of NAD
from NADH accompanied by the fermentation of pyruvate to lactate. This reaction is catalyzed by lactate dehydrogenase (LDH) isoform A (LDHA), whereas LDH isoform B (LDHB) catalyzes the opposite reaction. LDH is widely used as a potential injury marker as it is released from damaged cells into the urine and serum; however, the precise isoform-specific cellular localization of the enzyme along the nephron has not been characterized. By combining immunohistochemistry results and single-cell RNA-sequencing data on healthy mouse kidneys, we identified that LDHA is primarily expressed in proximal segments, whereas LDHB is expressed in the distal parts of the nephron. In vitro experiments in mouse and human renal proximal tubule cells showed an increase in LDHA following hypoxia with no change in LDHB. Using immunofluorescence, we observed that the overall expression of both LDHA and LDHB proteins decreased following renal ischemia-reperfusion injury as well as in the adenine-diet-induced model of chronic kidney disease. Single-nucleus RNA-sequencing analyses of kidneys following ischemia-reperfusion injury revealed a significant decline in the number of cells expressing detectable levels of
and
; however, cells that were positive showed increased average expression postinjury, which subsided during the recovery phase. These data provide information on the cell-specific expression of LDHA and LDHB in the normal kidney as well as following acute and chronic kidney disease.
Cellular release of lactate dehydrogenase (LDH) is being used as an injury marker; however, the exact localization of LDH within the nephron remains unclear. We show that LDH isoform A is expressed proximally, whereas isoform B is expressed distally. Both subunit expressions were significantly altered in models of acute kidney injury and chronic kidney disease. Our study provides new insights into basal and postinjury renal lactate metabolism.</description><subject>Acute Kidney Injury - enzymology</subject><subject>Acute Kidney Injury - genetics</subject><subject>Acute Kidney Injury - pathology</subject><subject>Adenine</subject><subject>Animals</subject><subject>Biomarkers - metabolism</subject><subject>Cell Hypoxia</subject><subject>Cells, Cultured</subject><subject>Dehydrogenases</subject><subject>Disease Models, Animal</subject><subject>Fermentation</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Glycolysis</subject><subject>Humans</subject><subject>Hypoxia</subject><subject>Immunofluorescence</subject><subject>Immunohistochemistry</subject><subject>Ischemia</subject><subject>Isoenzymes</subject><subject>Isoforms</subject><subject>Kidney - enzymology</subject><subject>Kidney - pathology</subject><subject>Kidney diseases</subject><subject>L-Lactate dehydrogenase</subject><subject>L-Lactate Dehydrogenase - genetics</subject><subject>L-Lactate Dehydrogenase - metabolism</subject><subject>Lactic acid</subject><subject>Localization</subject><subject>Male</subject><subject>Metabolic rate</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>NAD</subject><subject>NADH</subject><subject>Oxidative phosphorylation</subject><subject>Phosphorylation</subject><subject>Pyruvic acid</subject><subject>Renal function</subject><subject>Renal Insufficiency, Chronic - enzymology</subject><subject>Renal Insufficiency, Chronic - genetics</subject><subject>Renal Insufficiency, Chronic - pathology</subject><subject>Reperfusion</subject><subject>Time Factors</subject><issn>1931-857X</issn><issn>1522-1466</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNpdkUtrGzEUhUVJiJ3HLygUQTbZjHv1GkmbQhKSphDIJovshKyR7HFnRq40DvG_j5yHabu6gvPdc3XvQegrgRkhgn63q3Xyg-1mADVVMwoUvqBpUWhFeF0flLdmpFJCPk3Qcc4rACCEkiM0YUwSLSRM0d3NS3HJuY0DjgF31o129Ljxy22T4qL4Z48vsR0afIXbHENMfcbtgMelx33cFPV32wx-e4oOg-2yP_uoJ-jx9ubx-q66f_j56_ryvnJc67HiZTDTtNFSaAEKQNrazYMVcyGdIkESOdeNE4ELpgILWhLuGNSKMg2OsxP04912vZn3vnF-GJPtzDq1vU1bE21r_lWGdmkW8dkoTrkQO4OLD4MU_2x8Hk3fZue7zg6-rGOoAMJlXau6oOf_oau4SeXiO4qBKMfUqlDsnXIp5px82H-GgNkFZT6DMm9BmV1Qpevb33vsez6TYa9JJo_9</recordid><startdate>20210501</startdate><enddate>20210501</enddate><creator>Osis, Gunars</creator><creator>Traylor, Amie M</creator><creator>Black, Laurence M</creator><creator>Spangler, Daryll</creator><creator>George, James F</creator><creator>Zarjou, Abolfazl</creator><creator>Verlander, Jill W</creator><creator>Agarwal, Anupam</creator><general>American Physiological Society</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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4276-5186</orcidid><orcidid>https://orcid.org/0000-0002-0613-737X</orcidid><orcidid>https://orcid.org/0000-0002-4096-4897</orcidid></search><sort><creationdate>20210501</creationdate><title>Expression of lactate dehydrogenase A and B isoforms in the mouse kidney</title><author>Osis, Gunars ; Traylor, Amie M ; Black, Laurence M ; Spangler, Daryll ; George, James F ; Zarjou, Abolfazl ; Verlander, Jill W ; Agarwal, Anupam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-4719392d9759508007a6cbfa5b57c81f717b9dc5f4538f3f9714c30682390c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Acute Kidney Injury - enzymology</topic><topic>Acute Kidney Injury - genetics</topic><topic>Acute Kidney Injury - pathology</topic><topic>Adenine</topic><topic>Animals</topic><topic>Biomarkers - metabolism</topic><topic>Cell Hypoxia</topic><topic>Cells, Cultured</topic><topic>Dehydrogenases</topic><topic>Disease Models, Animal</topic><topic>Fermentation</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Glycolysis</topic><topic>Humans</topic><topic>Hypoxia</topic><topic>Immunofluorescence</topic><topic>Immunohistochemistry</topic><topic>Ischemia</topic><topic>Isoenzymes</topic><topic>Isoforms</topic><topic>Kidney - enzymology</topic><topic>Kidney - pathology</topic><topic>Kidney diseases</topic><topic>L-Lactate dehydrogenase</topic><topic>L-Lactate Dehydrogenase - genetics</topic><topic>L-Lactate Dehydrogenase - metabolism</topic><topic>Lactic acid</topic><topic>Localization</topic><topic>Male</topic><topic>Metabolic rate</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>NAD</topic><topic>NADH</topic><topic>Oxidative phosphorylation</topic><topic>Phosphorylation</topic><topic>Pyruvic acid</topic><topic>Renal function</topic><topic>Renal Insufficiency, Chronic - enzymology</topic><topic>Renal Insufficiency, Chronic - genetics</topic><topic>Renal Insufficiency, Chronic - pathology</topic><topic>Reperfusion</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Osis, Gunars</creatorcontrib><creatorcontrib>Traylor, Amie M</creatorcontrib><creatorcontrib>Black, Laurence M</creatorcontrib><creatorcontrib>Spangler, Daryll</creatorcontrib><creatorcontrib>George, James F</creatorcontrib><creatorcontrib>Zarjou, Abolfazl</creatorcontrib><creatorcontrib>Verlander, Jill W</creatorcontrib><creatorcontrib>Agarwal, Anupam</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>American journal of physiology. Renal physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Osis, Gunars</au><au>Traylor, Amie M</au><au>Black, Laurence M</au><au>Spangler, Daryll</au><au>George, James F</au><au>Zarjou, Abolfazl</au><au>Verlander, Jill W</au><au>Agarwal, Anupam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of lactate dehydrogenase A and B isoforms in the mouse kidney</atitle><jtitle>American journal of physiology. Renal physiology</jtitle><addtitle>Am J Physiol Renal Physiol</addtitle><date>2021-05-01</date><risdate>2021</risdate><volume>320</volume><issue>5</issue><spage>F706</spage><epage>F718</epage><pages>F706-F718</pages><issn>1931-857X</issn><eissn>1522-1466</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><abstract>Cellular metabolic rates in the kidney are critical for maintaining normal renal function. In a hypoxic milieu, cells rely on glycolysis to meet energy needs, resulting in the generation of pyruvate and NADH. In the absence of oxidative phosphorylation, the continuation of glycolysis is dependent on the regeneration of NAD
from NADH accompanied by the fermentation of pyruvate to lactate. This reaction is catalyzed by lactate dehydrogenase (LDH) isoform A (LDHA), whereas LDH isoform B (LDHB) catalyzes the opposite reaction. LDH is widely used as a potential injury marker as it is released from damaged cells into the urine and serum; however, the precise isoform-specific cellular localization of the enzyme along the nephron has not been characterized. By combining immunohistochemistry results and single-cell RNA-sequencing data on healthy mouse kidneys, we identified that LDHA is primarily expressed in proximal segments, whereas LDHB is expressed in the distal parts of the nephron. In vitro experiments in mouse and human renal proximal tubule cells showed an increase in LDHA following hypoxia with no change in LDHB. Using immunofluorescence, we observed that the overall expression of both LDHA and LDHB proteins decreased following renal ischemia-reperfusion injury as well as in the adenine-diet-induced model of chronic kidney disease. Single-nucleus RNA-sequencing analyses of kidneys following ischemia-reperfusion injury revealed a significant decline in the number of cells expressing detectable levels of
and
; however, cells that were positive showed increased average expression postinjury, which subsided during the recovery phase. These data provide information on the cell-specific expression of LDHA and LDHB in the normal kidney as well as following acute and chronic kidney disease.
Cellular release of lactate dehydrogenase (LDH) is being used as an injury marker; however, the exact localization of LDH within the nephron remains unclear. We show that LDH isoform A is expressed proximally, whereas isoform B is expressed distally. Both subunit expressions were significantly altered in models of acute kidney injury and chronic kidney disease. Our study provides new insights into basal and postinjury renal lactate metabolism.</abstract><cop>United States</cop><pub>American Physiological Society</pub><pmid>33719570</pmid><doi>10.1152/ajprenal.00628.2020</doi><orcidid>https://orcid.org/0000-0003-4276-5186</orcidid><orcidid>https://orcid.org/0000-0002-0613-737X</orcidid><orcidid>https://orcid.org/0000-0002-4096-4897</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Acute Kidney Injury - enzymology Acute Kidney Injury - genetics Acute Kidney Injury - pathology Adenine Animals Biomarkers - metabolism Cell Hypoxia Cells, Cultured Dehydrogenases Disease Models, Animal Fermentation Gene Expression Regulation, Enzymologic Glycolysis Humans Hypoxia Immunofluorescence Immunohistochemistry Ischemia Isoenzymes Isoforms Kidney - enzymology Kidney - pathology Kidney diseases L-Lactate dehydrogenase L-Lactate Dehydrogenase - genetics L-Lactate Dehydrogenase - metabolism Lactic acid Localization Male Metabolic rate Mice Mice, Inbred C57BL NAD NADH Oxidative phosphorylation Phosphorylation Pyruvic acid Renal function Renal Insufficiency, Chronic - enzymology Renal Insufficiency, Chronic - genetics Renal Insufficiency, Chronic - pathology Reperfusion Time Factors |
title | Expression of lactate dehydrogenase A and B isoforms in the mouse kidney |
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