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Oglesbee, Devin

0000-0002-7147-5527

Mayo Clinic

Biochemical Genetics Laboratory, Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN 55905, USA; lacey.jean@mayo.edu (J.M.L.); white.amy1@mayo.edu (A.L.W.); pino.gisele@mayo.edu (G.P.); studinski.april@mayo.edu (A.L.S.); gavrilov.di

Citations 36

Clinical Heterogeneity of Neuronal Ceroid Lipofuscinosis Type 13
Ghayal, Nikhil B , Roemer, Shanu F. , Tipton, Philip W. , Jiang, Peizhou , Selner, Elizabeth M., Peck, Dawn , Murakami, Aya , Oglesbee, Devin , Graff‐Radford, Neill R. , Dickson, Dennis W. , Peck, Dawn S, Dickson, Dennis W , Graff-Radford, Neill R , Oglesbee, Devin , Tipton, Philip W , Ghayal, Nikhil B

Neurology Genetics | December 23, 2024 | Volume: 11 | Issue: 1 | Pages: No page available

10.1212/nxg.0000000000200227 Get It

The clinical utility in hospital‐wide use of growth differentiation factor 15 as a biomarker for mitochondrial DNA‐related disorders
Fernández, Andrea Cortés , Estrella, Jane , Oglesbee, Devin , Larson, Austin , Hove, Johan L.K. Van , Larson, Austin A , Van Hove, Johan L K , Oglesbee, Devin

Journal of Inherited Metabolic Disease | November 25, 2024 | Volume: 48 | Issue: 1 | Pages: No page available

10.1002/jimd.12821 Get It

AbstractClinical recognition of primary mitochondrial disorders (PMD) is difficult due to the clinical and genetic heterogeneity. Whereas lactate has low sensitivity and specificity, in structured clinical studies growth differentiation factor 15 (GDF15) has shown promise with elevations in mitochondrial DNA (mtDNA)‐related PMD, but its specificity has been questioned. In a tertiary care hospital‐wide study, medical records were retrospectively reviewed from 418 cases where GDF15 levels were obtained by clinicians. Patients were classified into patients with PMD due to mtDNA‐related defects (mtDNA maintenance, mtDNA deletions, and mtDNA‐encoded tRNA variants), PMD due to structural defects or other nuclear causes, and in non‐mitochondrial disease. Patients with liver disease or systemic critical illness were excluded. GDF15 was assayed in a clinical laboratory with a cutoff of 750 ng/L. There were 38 mtDNA‐related PMD (GDF15 >750 pg/mL in 76%), 35 other nuclear DNA‐encoded PMD or structural subunits (31% elevated GDF15), 309 non‐mitochondrial disorders (13% elevated GDF15). Based on the highest Youden J‐index, the optimal cut‐off value to identify these target mtDNA‐related disorders was 815 pg/mL, with sensitivity 76%, specificity 88%, positive predictive value of 41% and negative predictive value of 97%. At this optimized cutoff level, mtDNA‐encoded PMD patients had elevated GDF15 in 76%, nuclear DNA‐encoded PMD in 26%, and non‐mitochondrial disorders in 11% of patients. Thus, in a real‐life clinical setting, after excluding abnormal liver function and critical illness, GDF15 had good clinical utility increasing the odds at predicting mtDNA‐related primary mitochondrial disorders 14‐fold, but not for structural or other nuclear‐encoded primary mitochondrial disorders.
A Review of Multiple Diagnostic Approaches in the Undiagnosed Diseases Network to Identify Inherited Metabolic Diseases
Furuta, Yutaka , Tinker, Rory J. , Hamid, Rizwan , Ezell, Kimberly , Oglesbee, Devin , DeBerardinis, Ralph J., Phillips, John A., Oglesbee, Devin , Tinker, R J , Cogan, Joy D. , DeBerardinis, Ralph J. , Phillips, John A., Network, the Undiagnosed Diseases

No container title available | October 11, 2024 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.21203/rs.3.rs-4588411/v1 Get It

Abstract Background The number of known inherited metabolic diseases (IMDs) has been expanding, and the rate of diagnosis is improving with the development of innovative approaches including next generation sequencing (NGS). However, a substantial proportion of IMDs remain undetected by traditional diagnostic approaches. We aim to highlight the spectrum of IMDs diagnosed by the Undiagnosed Diseases Network (UDN) and to learn from the UDN diagnostic processes that were able to detect IMDs. Methods We conducted a retrospective analysis of 757 UDN participants diagnosed from 2015 until 2023 using the cohort database, which were divided into a cohort with IMDs (n = 194; 27%) and a cohort whose phenotypes were not explained by an IMD (n = 563; 73%), based on the International Classification of Inherited Metabolic Disorders (ICIMD). Then, we divided the causes of the metabolic 194 diagnoses into seven groups that included all the ICIMD categories. We inspected which clinical and laboratory approaches contributed to a final UDN diagnosis. We also present a UDN case example from each group to highlight the diagnostic yields that resulted from combining newer diagnostic approaches in the UDN and illustrate potential pitfalls of current NGS methods. Results These 194 cases of IMDs included examples from 21/25 (84%) of the ICIMD categories. Of the UDN subjects 164/194 (85%) were diagnosed with IMDs through NGS. Conclusion The spectrum of IMDs detected in the UDN cohort is large and growing and appropriate use of newer multiple diagnostic approaches should further increase diagnosis of IMDs that are presently missed by the traditional laboratory screening methods.
Case Report of Friedreich's Ataxia and ALG1‐Related Biochemical Abnormalities in a Patient With Progressive Spastic Paraplegia
Quinlan, Aisling , Rodan, Lance H. , Barkoudah, Elizabeth, Tam, Amy , Saffari, Afshin , Shammas, Ibrahim , Ranatunga, Wasantha , Morava‐Kozicz, Eva, Oglesbee, Devin , Ebrahimi‐Fakhari, Darius , Srivastava, Siddharth , Rodan, Lance , Ebrahimi-Fakhari, Darius , Srivastava, Siddharth , Oglesbee, Devin , Berry, Gerald J.

American Journal of Medical Genetics Part A | September 26, 2024 | Volume: 197 | Issue: 2 | Pages: No page available

10.1002/ajmg.a.63890 Get It

ABSTRACTFrataxin is an evolutionarily conserved mitochondrial protein responsible for iron homeostasis and metabolism. A deficiency of frataxin (encoded by FXN) leads to Friedreich's ataxia (FRDA), a progressive disorder that affects both the central and peripheral nervous systems, most commonly via a pathogenic GAA trinucleotide expansion. In contrast, pathogenic variants in ALG1 in humans cause a form of congenital disorder of glycosylation. Here, we present a 15‐year‐old boy with a clinical presentation that raised concern for complex hereditary spastic paraplegia (HSP), with motor features including progressive spastic paraparesis, cervical dystonia, cerebellar dysfunction, and diminished lower extremity reflexes. The proband was initially found to have a novel compound heterozygous variant in ALG1 on exome sequencing, along with N‐glycan profiling revealing evidence of defective mannosylation and Western blot analysis demonstrating an 84% reduction in ALG1 expression. Although several of his clinical features could be explained by the ALG1 variant specifically or considered as part of the presentation of CDGs in general, there were additional phenotypes that suggested an alternative, or additional, genetic diagnosis. Subsequently, he was found to have biallelic pathogenic GAA repeat expansions in FXN on genome sequencing, leading to a diagnosis of FRDA. Given that FRDA explained all his clinical features, the ALG1 variant may have been a hypomorphic form and/or a biochemical phenotype. Our findings underscore the importance of considering FRDA as a differential diagnosis in cases of complex HSP and demonstrate the utility of unbiased genome sequencing approaches that include detection of trinucleotide repeat expansions for progressive motor disorders.
Development of a Multiplexed Sphingolipids Method for Diagnosis of Inborn Errors of Ceramide Metabolism
Byeon, Seul Kee , Wegwerth, Peter Jared, George, John Phillip, Oglesbee, Devin , Matern, Dietrich , Pandey, Akhilesh , Kim, Jinyong, Zenka, Roman, George, John P, Vairo, Filippo , Pandey, Akhilesh , Oglesbee, Devin , Byeon, Seul Kee , Kim, Jin Yong , Zenka, Roman M. , Vairo, Filippo Pinto e , Schultz, Matthew

Clinical Chemistry | August 29, 2024 | Volume: 70 | Issue: 11 | Pages: 1366-1374

10.1093/clinchem/hvae115 Get It

Abstract Background Sphingolipids play a crucial role in cellular functions and are essential components of cell membranes, signaling molecules, and lipid metabolism. In particular, ceramide is a key intermediate in sphingolipid metabolism and defects in ceramide metabolism can lead to various inborn errors of metabolism, making ceramides important targets for clinical screening and diagnosis. Detecting altered concentration patterns of sphingolipids is desirable for distinguishing related inborn errors of metabolism for diagnosis and treatment monitoring. Methods We developed a liquid chromatography-tandem mass spectrometry method with a pathway-oriented approach to focus on sphingolipids involved in ceramide metabolism. A total of 47 sphingolipids bearing different head groups and side chains were targeted. Precision/reproducibility, linearity, and spike recovery extraction efficiency tests were performed on plasma and serum samples from confirmed cases of sphingolipidosis. Results Linearity of the method showed the coefficient of determination (r2) for all standards to be >0.99 with a slope of 1.00 ± 0.01. Intra- and interday reproducibility of standards spiked into plasma and serum revealed a coefficient of variation <20%. Spike and recovery assessment showed recovery values of 80%–120% for all standards. Altered levels of sphingolipids from patients with hereditary sensory and autonomic neuropathy caused by pathogenic variants in SPTLC2 and hypomyelinating leukodystrophy related to variants in DEGS1 were detected, in agreement with trends reported in earlier studies confirming the utility of this pathway-centric method. Conclusions This method can serve as a useful tool to simultaneously monitor sphingolipids, enabling screening and diagnosis of inborn errors of ceramide metabolism.
A new test method for biochemical analysis of plasmalogens in dried blood spots and erythrocytes from patients with peroxisomal disorders
Wegwerth, Peter J, White, Amy , Stoway, Stephanie D., Loken, Perry R , Oglesbee, Devin , Matern, Dietrich , Tortorelli, Silvia , Raymond, Kimiyo , Gavrilov, Dimitar K. , White, Amy L , Raymond, Kimiyo M, Oglesbee, Devin , Braverman, Nancy

Journal of Inherited Metabolic Disease | September 25, 2023 | Volume: 46 | Issue: 6 | Pages: 1159-1169

10.1002/jimd.12682 Get It

AbstractMeasurement of plasmalogens is useful for the biochemical diagnosis of rhizomelic chondrodysplasia punctata (RCDP) and is also informative for Zellweger spectrum disorders (ZSD). We have developed a test method for the simultaneous quantitation of C16:0, C18:0, and C018:1 plasmalogen (PG) species and their corresponding fatty acids (FAs) in dried blood spots (DBS) and erythrocytes (RBC) by using capillary gas chromatography–mass spectrometry. Normal reference ranges for measured markers and 10 calculated ratios were established by the analysis of 720 and 473 unaffected DBS and RBC samples, respectively. Determination of preliminary disease ranges was made by using 45 samples from 43 unique patients: RCDP type 1 (DBS: 1 mild, 17 severe; RBC: 1 mild, 6 severe), RCDP type 2 (DBS: 2 mild, 1 severe; RBC: 2 severe), RCDP type 3 (DBS: 1 severe), RCDP type 4 (RBC: 2 severe), and ZSD (DBS: 3 severe; RBC: 2 mild, 7 severe). Postanalytical interpretive tools in Collaborative Laboratory Integrated Reports (CLIR) were used to generate an integrated score and a likelihood of disease. In conjunction with a review of clinical phenotype, phytanic acid, and very long‐chain FA test results, the CLIR analysis allowed for differentiation between RCDP and ZSD. Data will continue to be gathered to improve CLIR analysis as more samples from affected patients with variable disease severity are analyzed. The addition of DBS analysis of PGs may allow for at‐home specimen collection and second‐tier testing for newborn screening programs.
Genetic therapy in a mitochondrial disease model suggests a critical role for liver dysfunction in mortality
Sabharwal, Ankit , Wishman, Mark , Cervera, Roberto Lopez , Serres, MaKayla R., Anderson, Jennifer L. , Holmberg, Shannon R. , Treichel, Anthony J. , Ichino, Noriko , Liu, Weibin , Yang, Jingchun , Deng, Yun , Lacey, Jean M., Laxen, William , Loken, Perry R , Oglesbee, Devin , Wishman, Mark D, Treichel, Anthony J , Ichino, Noriko , Ding, Yonghe , Laxen, William J, Farber, Steven Arthur , Clark, Karl J , Lin, Xueying , Ekker, Stephen C , Oglesbee, Devin , Sabharwal, Ankit , Kar, Bibekananda , Kar, Bibekananda , Farber, Steven , Clark, Karl J. , Xu, Xiaolei , Ekker, Stephen C.

eLife | November 21, 2022 | Volume: 11 | Issue: No issue available | Pages: No page available

10.7554/elife.65488 Get It

The clinical and largely unpredictable heterogeneity of phenotypes in patients with mitochondrial disorders demonstrates the ongoing challenges in the understanding of this semi-autonomous organelle in biology and disease. Previously, we used the gene-breaking transposon to create 1200 transgenic zebrafish strains tagging protein-coding genes (Ichino et al., 2020), including the lrpprc locus. Here, we present and characterize a new genetic revertible animal model that recapitulates components of Leigh Syndrome French Canadian Type (LSFC), a mitochondrial disorder that includes diagnostic liver dysfunction. LSFC is caused by allelic variations in the LRPPRC gene, involved in mitochondrial mRNA polyadenylation and translation. lrpprc zebrafish homozygous mutants displayed biochemical and mitochondrial phenotypes similar to clinical manifestations observed in patients, including dysfunction in lipid homeostasis. We were able to rescue these phenotypes in the disease model using a liver-specific genetic model therapy, functionally demonstrating a previously under-recognized critical role for the liver in the pathophysiology of this disease.
Sorbitol Is a Severity Biomarker for PMM2‐CDG with Therapeutic Implications
Ligezka, Anna N. , Radenkovic, Silvia , Saraswat, Mayank , Garapati, Kishore , Ranatunga, Wasantha , Yanaihara, Hitoshi, Preston, Graeme , Brucker, William , McGovern, Renee M., Cassiman, David , Johnsen, Christin , Lam, Christina , Edmondson, Andrew C. , Raymond, Kimiyo , Oglesbee, Devin , Pandey, Akhilesh , Reid, Joel M. , Muthusamy, Karthik , Morava, Eva , Pandey, Akhilesh , Oglesbee, Devin , Edmondson, Andrew C , Garapati, Kishore , Krzyściak, Wirginia , Muthusamy, Karthik , Mercimek‐Andrews, Saadet , Larson, Austin , Ghesquière, Bart , Witters, Peter , Perlstein, Ethan , Kozicz, Tamás , Morava, Éva

Annals of Neurology | October 20, 2021 | Volume: 90 | Issue: 6 | Pages: 887-900

10.1002/ana.26245 Get It

ObjectiveEpalrestat, an aldose reductase inhibitor increases phosphomannomutase (PMM) enzyme activity in a PMM2‐congenital disorders of glycosylation (CDG) worm model. Epalrestat also decreases sorbitol level in diabetic neuropathy. We evaluated the genetic, biochemical, and clinical characteristics, including the Nijmegen Progression CDG Rating Scale (NPCRS), urine polyol levels and fibroblast glycoproteomics in patients with PMM2‐CDG.MethodsWe performed PMM enzyme measurements, multiplexed proteomics, and glycoproteomics in PMM2‐deficient fibroblasts before and after epalrestat treatment. Safety and efficacy of 0.8 mg/kg/day oral epalrestat were studied in a child with PMM2‐CDG for 12 months.ResultsPMM enzyme activity increased post‐epalrestat treatment. Compared with controls, 24% of glycopeptides had reduced abundance in PMM2‐deficient fibroblasts, 46% of which improved upon treatment. Total protein N‐glycosylation improved upon epalrestat treatment bringing overall glycosylation toward the control fibroblasts’ glycosylation profile. Sorbitol levels were increased in the urine of 74% of patients with PMM2‐CDG and correlated with the presence of peripheral neuropathy, and CDG severity rating scale. In the child with PMM2‐CDG on epalrestat treatment, ataxia scores improved together with significant growth improvement. Urinary sorbitol levels nearly normalized in 3 months and blood transferrin glycosylation normalized in 6 months.InterpretationEpalrestat improved PMM enzyme activity, N‐glycosylation, and glycosylation biomarkers in vitro. Leveraging cellular glycoproteome assessment, we provided a systems‐level view of treatment efficacy and discovered potential novel biosignatures of therapy response. Epalrestat was well‐tolerated and led to significant clinical improvements in the first pediatric patient with PMM2‐CDG treated with epalrestat. We also propose urinary sorbitol as a novel biomarker for disease severity and treatment response in future clinical trials in PMM2‐CDG. ANN NEUROL 20219999:n/a–n/a
A new D‐galactose treatment monitoring index for PGM1‐CDG
Perales‐Clemente, Ester , Liedtke, Kristen, Studinski, April, Radenkovic, Silvia , Gavrilov, Dimitar , Oglesbee, Devin , Matern, Dietrich , Rinaldo, Piero, Tortorelli, Silvia , Raymond, Kimiyo , Oglesbee, Devin , Morava, Éva

Journal of Inherited Metabolic Disease | May 27, 2021 | Volume: 44 | Issue: 5 | Pages: 1263-1271

10.1002/jimd.12406 Get It

AbstractPhosphoglucomutase 1 (PGM1) catalyzes the interconversion of glucose‐6‐phosphate to glucose‐1‐phosphate and is a key enzyme of glycolysis, glycogenesis, and glycogenolysis. PGM1 deficiency (OMIM: 614921) was initially defined as a glycogen storage disorder (type XIV), and later re‐classified as a PGM1‐congenital disorder of glycosylation (PGM1‐CDG). Serum transferrin (Tf) glycan isoform analysis by liquid chromatography‐mass spectrometry (LC‐MS) is used as a primary diagnostic screen tool, and reveals a very unique CDG profile described as a mixture of CDG‐type I and CDG‐type II patterns. Oral d‐galactose supplementation shows significant clinical and metabolic improvements, which are indicated by the Tf glycan isoform normalization over time in patients with PGM1‐CDG. Thus, there is a need for biomarkers to guide d‐galactose dosage in patients in order to maintain effective and safe drug levels. Here, we present a simplified algorithm called PGM1‐CDG Treatment Monitoring Index (PGM1‐TMI) for assessing the response of PGM1‐CDG patients to d‐galactose supplementation. For our single‐center cohort of 16 PGM1‐CDG patients, the Tf glycan profile analysis provided the biochemical diagnosis in all of them. In addition, the PGM1‐TMI was reduced in PGM1‐CDG patients under d‐galactose supplementation as compared with their corresponding values before treatment, indicating that glycosylation proceeds towards normalization. PGM1‐TMI allows tracking Tf glycan isoform normalization over time when the patients are on d‐galactose supplementation.