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Modifier Genes in 21-hydroxylase Deficiency - GSD 5607

ABSTRACT: Modifier Genes in 21-hydroxylase Deficiency - GSD 5607

PROVIDER: PRJNA377375 | ENA |

REPOSITORIES: ENA

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Potential Modulatory Role of Osteoprotegerin in Bone Metabolism of Patients with 21-Hydroxylase Deficiency - GSD 5611

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Reduced expression of Semaphorin3A derived from osteoclasts cause lymphatic expansion in GSD mouse model

Project description:Gorham-Stout disease (GSD) is a sporadic chronic disease characterized by progressive bone dissolution, absorption, disappearance, and lymphatic vessel infiltration in bone marrow cavities. Although the osteolytic mechanism of GSD has been widely studied, the cause of lymphatic hyperplasia of GSD is rarely touched. In this study, Through comparing RNA expression profile in Osteoclast (OC) with Osteoclast precursors (OCP) by RNA sequencing, we identified a new factor, Semaphorin 3A (Sema3A), as an osteoprotective factor, which is involved in the lymphatic expansion of GSD. Compared to OCP, OC enhanced the growth, migration, and tube formation of lymphatic endothelial cells (LECs), in which the expression of Sema3A is low compared to OCP. In the presence of recombinant Sema3A, the growth, migration, and tube formation of LECs were inhibited, further comfirmed the effect of Sema3A on LECs. Using LEC-induced GSD mouse model, the effect of Sema3A was examined by injecting lentiviral expressing Sema3A into the tibiae. We found that the overexpression of Sema3A in tibiea suppressed the expansion of LECs and alleviated the bone loss, whereas the injection with lentiviral expressing Sema3A shRNA into the tibiae caused GSD-like phenotypes. Histological staining further demonstratsed the Osteoclasts decreased and osteocalcin were increased after the Seme3A treatment with lentiviral of Sema3A compared with the control. Combined with the role of Seme3A on osteoprotection, we propose that reduced Sema3A in OCs is one of pathogenesis of GSD and expressing Sema3A represents a new approach for treatment of GSD.

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The common P450 oxidoreductase variant A503V is not a modifier gene for 21-hydroxylase deficiency.

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Proteomics profiling of serum and liver in GSD Ia and Ib patients: insights into complication mechanisms and circulation biomarkers

Project description:Background: Glycogen Storage Disease (GSD) Type Ia and Ib are rare metabolic diseases caused by gene variants in G6PC and SLC37A4 respectively. Patients often suffer from multiple metabolic abnormalities and severe long-term complications. Methods: In this study, we employed comprehensive untargeted proteomics on retrospectively registered samples: 26 serum/plasma samples (18 GSD Ia and 8 GSD Ib) from patients with 21 matched healthy controls, complemented by 4 liver samples from 3 patients who received liver transplantation (3 from GSD Ia including 1 with hepatocellular carcinoma tissue and 1 from GSD Ib), compared to 10 donor liver samples, to investigate the pathological mechanisms of disease complications and identify potential biomarkers. Results: Pathway analysis of the differentially regulated proteins revealed distinct changes in the serum/plasma of GSD Ia and Ib. Coagulation was the most significantly changed biological process in the GSD Ia patients. Immune response-associated proteins, especially a large number of immunoglobulins, increased in GSD Ib specifically. Proteins related to liver injury, cholesterol, and amyloidosis were altered in two subtypes, though more pronounced in GSD Ia. Potential biomarkers with significant alterations both in the circulation as well as in the liver were identified specifically for monitoring and prognosing GSD Ia (COL163 and PROC), GSD Ib (F11 and CD163), and hepatocellular carcinoma (HCC) in GSD Ia patients (ALDOB and CFHR5). Conclusions: These findings provide new insights into the pathogenesis of GSD I-related complications and highlighted the potential of protein circulating biomarkers for monitoring complication progression in GSD Ia and Ib, as well as for assessing HCC risk in GSD Ia patients.

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Project description:Potential Modulatory Role of Osteoprotegerin in Bone Metabolism of Patients with 21-Hydroxylase Deficiency - GSD 5611

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