{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m36.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m27.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m23.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m33.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m41.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m34.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m28.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m37.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m40.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m35.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m29.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m42.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m31.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m30.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m38.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m22.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m26.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ib_m43.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m32.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/WT_m15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/Ia_m39.raw"],"Xls":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066807/20220722_mouse_GSD_Ia_Ib_proteomics_Report_input.xls"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["j.c.wolters@umcg.nl"],"submitter":["Justina Clarinda Wolters"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Mouse","Liver","Proteomics","Gsd i"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066807"],"tissue":["Liver"],"sample_protocol":["Liver homogenization 10% lysis buffer (w/v, mg/mL) was added into liver tissues, and used a mechanical agitator at 700 for 20 times to make liver homogenate. The lysis buffer was made by 48.45 mL 0.1% Nonidet P-40 buffer, 0.5 mL phosphatase inhibitors cocktail 2, 0.5 mL phosphatase inhibitors cocktail 3, 50 μL 1M DL-Dithiothreitol, and one complete protease inhibitor cocktail tablet (Roche, 11836145001). 0.1% Nonidet P-40 buffer was made by 0.4 M sodium chloride, 1:1000 Nonidet P-40, 10 mM Tris(hydroxymethyl)aminomethane, and 1 mM ethylenediaminetetraacetic acid. The primary liver homogenate was collected into 1.5 mL tubes and sonicated on ice by a sonicator two times for 10 seconds each, with pulse on/off 1 second. After sonicating, samples were centrifuged at 3000 rpm, 4 ºC for 10 mins, and the supernatants were collected into new tubes as 10% liver homogenates.  Delipidation 90 μL liver homogenates and 20 μL serum/plasma were delipidated using 4 mL MeOH and 4 mL cold diethyl ether (-20 ºC), followed by centrifugation for 30 minutes at 1,500 xg at 4 ºC. After discarding the supernatant, 4 mL cold diethyl ether was added to each sample and centrifuged for 30 minutes at 1,500 xg at 4 ºC. Samples were dried under N2 after discarding the supernatant, and then resuspended with 100 μL 1× lithium dodecyl sulfate (LDS) sample loading buffer (Abcam PH=8.5, diluted with RIPA buffer). After sonicating, vortexing, pipetting up and down several times, and centrifugation at 1,500 xg for 1 min, the supernatants were taken and diluted 5 times using 1×LDS sample buffer. In-gel digestion The in-gel digestion protocol was based on the 'In-Gel Digestion and Sample Cleanup' protocol, as described previously in Wolters et al (PMID: 27447838). Briefly, 20 μL of delipidated samples were loaded on a precast polyacrylamide gel (Bolt™ Bis-Tris Plus Mini Protein Gels, 4‐12%, 1.0 mm, Thermo Scientific) and ran for 5 minutes at 100V. The gels were stained for one hour with InstantBlue® Coomassie Protein Stain, and after destaining by MiliQ water, the blue gel bands were cut into small squares of 2 mm×2 mm and collected separately. They were washed and shaken at 500 rpm on Thermomixer comfort with 300 μL 30% v/v acetonitrile (ACN) in 100 mM ammonium bicarbonate (ABC) until they were completely destained, followed by 300 μL 50% ACN in ABC, and lastly with 300 μL 100% ACN for 5 min, after which they were dried in the oven (Melag, brutschrank incubat) at 37 ºC. Next, the proteins were reduced with 30 μL 10 mM dithiothreitol (30 minutes, 55 ºC) and alkylated with 30 μL 55 mM iodoacetamide (30 min, RT, in the dark), after which they were shaken with 300 μL 100% ACN for 30 minutes, after which removed the solution and dried in the oven at 37 ºC. Subsequently, the gel pieces were rehydrated with 30 μL trypsin (1:100 g/g, Sequencing Grade Modified Trypsin, V5111, Promega), and incubated overnight at 37 ºC. After collecting the residual liquid to a new tube the next day, the residual liquid was collected in a new tube and the peptides in the gel plugs were extracted in 30 μL 75% v/v ACN plus 5% v/v formic acid (FA) (20 min, 25 ºC, mixing 500 rpm). After combining these two liquid fractions, peptides were dried in a vacuum concentrator. The residues were resuspended in 0.1% FA and diluted to 25 ng/μL. Further analysis was standardized based on the protein concentration before delipidation. Untargeted proteomics 20 μL peptide solutions (25 ng/μL) were loaded onto the Evotips following the sample loading protocol. All samples were analyzed by the Evosep One HPLC  using a C18 column with length/ID/C18 bead size of 15 cm/150 μm/1.9 μm (EV-1106, Evosep Biosystems). The pre-programmed gradient (30 samples per day, 0.5 μL/min flow rate, 48 minutes cycle time, 44 minutes gradient length) was applied. The column temperature was maintained at 40 ºC by a column heater controller and interfaced online with a FAIMS Pro, and then to the Orbitrap Exploris 480."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The raw data obtained from mass spectrometry were processed in Spectronaut v.16 (SN16) using a library-free approach (directDIA). Data was aligned with mouse protein sequences based on the Mouse UniProt reviewed sequences (17021 entries)."],"omics_type":["Proteomics"],"labhead":["Dr. JC Wolters"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Laboratory of Pediatrics, UMCG, The Netherlands"],"species":["Mus Musculus (mouse)"],"publication":["42270039 Krishnamurthy KA, Xiao R, Rutten MGS, Bos T, Bleeker A, Zhang M, de Vries HI, Koster M, Huijkman N, Smit M, Kloosterhuis N, Boer T, Schomakers B, van Weeghel M, van de Sluis B, Wolters JC, Bakker BM, Oosterveer MH. Hepatocyte-specific Cas9-mediated editing of G6pc and Slc37a4 elicits comparable biochemical and regulatory responses between glycogen storage disease (GSD) type Ia and Ib mice. Mol Metab. 2026 110:102393 10.1016/j.molmet.2026.102393"],"submitter_mail":["j.c.wolters@umcg.nl"],"submitter_affiliation":["UMCG"],"submitter_country":["Netherlands"],"pubmed_abstract":["<h4>Background/objective</h4>Glycogen storage disease type I (GSD I) is an autosomal recessive inborn error of carbohydrate metabolism. Patients with GSD type Ia and Ib exhibit overlapping and distinct symptoms and complications. Notably, GSD Ia patients show more severe hypertriglyceridemia and higher risk of hepatic tumors than GSD Ib patients.<h4>Methods</h4>Given the liver's pivotal role in these processes, this study utilized hepatocyte-specific CRISPR/Cas9-mediated somatic gene editing to explore the pathophysiological and biochemical adaptations in hepatic GSD Ia and Ib side-by-side. Additionally, hepatic histology, transcriptomics, and proteomics analysis was performed.<h4>Results</h4>Compared to controls, hepatic GSD Ia and Ib mice showed hepatomegaly, fasting hypoglycemia, hyperlactatemia, and increased uric acid in plasma, which was somewhat more pronounced in GSD Ia than Ib. Both GSD I subtypes showed similar reductions in hepatic acetyl-CoA precursor pool enrichment and increases in de novo biosynthesis of hepatic stearate and oleate. Interestingly, only GSD Ia mice showed mildly elevated plasma triglyceride and hepatic phosphate sugars. Metabolic changes were reflected at the transcriptomic and proteomic levels, with largely similar responses between GSD Ia and Ib livers. Moreover, altered mRNAs and protein levels related to nucleotide-binding oligomerization domain (NOD) signaling pathways, infection and inflammation, liver disease, and chemical carcinogenesis were somewhat more pronounced in hepatic GSD Ia than in GSD Ib mice.<h4>Conclusions</h4>Overall, the metabolic disturbance was more severe in hepatocyte-specific GSD Ia than in GSD Ib mice, consistent with the clinical phenotype in patients. The metabolic disorders and specific metabolites, genes, and proteins identified in this study provided new insights into the pathophysiological and biochemical phenotypes of GSD I subtypes in the liver."],"pubmed_title":["Hepatocyte-specific Cas9-mediated editing of G6pc and Slc37a4 elicits comparable biochemical and regulatory responses between glycogen storage disease (GSD) type Ia and Ib mice."],"pubmed_authors":["Krishnamurthy Kishore A KA, Xiao Ruiqi R, Rutten Martijn G S MGS, Bos Trijnie T, Bleeker Aycha A, Zhang Mingjia M, de Vries Hilda I HI, Koster Mirjam M, Huijkman Nicolette N, Smit Marieke M, Kloosterhuis Niels N, Boer Theo T, Schomakers Bauke B, van Weeghel Michel M, van de Sluis Bart B, Wolters Justina C JC, Bakker Barbara M BM, Oosterveer Maaike H MH"],"additional_accession":[]},"is_claimable":false,"name":"Hepatocyte-specific Cas9-mediated editing of G6pc and Slc37a4 elicits comparable biochemical and regulatory responses between glycogen storage disease (GSD) type Ia and Ib mice","description":"Glycogen storage disease type I (GSD I) is an autosomal recessive inborn error of carbohydrate metabolism. Patients with GSD type Ia and Ib exhibit overlapping and distinct symptoms and complications. Notably, GSD Ia patients show more severe hypertriglyceridemia and higher risk of hepatic tumors than GSD Ib patients. Given the liver's pivotal role in these processes, this study utilized hepatocyte-specific CRISPR/Cas9-mediated gene editing to explore the pathophysiological and biochemical differences between hepatic GSD Ia and Ib. Additionally, hepatic histology, transcriptomics, and proteomics analysis was performed. Compared to controls, GSD Ia and Ib mice showed hepatomegaly, fasting hypoglycemia, hyperlactatemia, and increased uric acid in plasma, which was more pronounced in GSD Ia than Ib. Both GSD I subtypes showed similar reductions in hepatic acetyl-CoA precursor pool enrichment and inceases in de novo biosynthesis of hepatic stearate and oleate. Interestingly, only GSD Ia mice showed significantly elevated plasma triglyceride, uric acid, and hepatic phosphate sugars. These metabolic changes were reflected at the level of transcriptomics and proteomics results. Moreover, altered mRNAs and protein levels related to nucleotide-binding oligomerization domain (NOD) signaling pathways, infection and inflammation, liver disease, and chemical carcinogenesis were more pronounced in GSD Ia mice. Overall, the metabolic disturbance was more severe in hepatocyte-specific GSD Ia than Ib mice, consistent with the clinical phenotype on patients. The metabolic disorders and specific metabolites, genes, and proteins identified in this study provided new insights into the potential therapeutic targets for GSD I patients, highlighting the need for subtype-specific treatment strategies.","dates":{"publication":"2026-07-02","submission":"2025-07-31"},"accession":"PXD066807","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:265619","NEWT:11294","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922",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