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Proteomic Identification of Novel Proteins in Primary and Secondary Membranous Nephropathy Using Laser Microdissection and Mass Spectrometry

ABSTRACT: Membranous nephropathy (MN) is a major cause of nephrotic syndrome in adults and is defined by subepithelial immune complex deposits along the glomerular basement membrane. While primary (or idiopathic) MN often involves known autoantigens such as PLA2R and THSD7A, secondary MN can be associated with autoimmune diseases, infections (for example, hepatitis B or C), malignancies, and certain medications. Despite these discoveries, the detailed mechanisms underlying both primary and secondary MN remain insufficiently understood.　Recently, advances in liquid chromatography–mass spectrometry (LC-MS) have facilitated more extensive proteomic analyses, enabling the identification of potential novel proteins tied to MN pathogenesis. Such findings may not only enhance our understanding of the disease mechanisms involved in both primary and secondary MN but also guide future diagnostic and therapeutic innovations.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dedong Kang

PROVIDER: PXD060136 | JPOST Repository | Sat Jan 24 00:00:00 GMT 2026

REPOSITORIES: jPOST

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Laser microdissection and mass spectrometry shows loss of podocyte proteins in minimal change disease and focal segmental glomerulosclerosis.

Project description:Minimal change disease and primary focal segmental glomerulosclerosis (FSGS) are common causes of nephrotic syndrome. Both diseases present with massive proteinuria and widespread foot process effacement on electron microscopy examination. On the other hand, secondary FSGS can also present with significant proteinuria, although the extent of foot process effacement can be variable. In this study, we performed laser microdissection of glomeruli followed by mass spectrometry to study podocyte proteins and compare the differences between the 3 diseases. Our study shows significant decrease in total spectral counts of nephrin, podocin, CD2-associated protein, alpha actinin 4, inverted formin 2 and dystroglycan 1 in all 3 diseases compared to time zero kidney transplant controls and membranous nephropathy biopsies (p <0.001). On the other hand, the decrease in the podocyte proteins in minimal change disease, primary FSGS and secondary FSGS was comparable and there was no significant difference. Surprisingly, there was no significant decrease in the podocyte proteins in membranous nephropathy compared to time zero kidney transplant control biopsies. In conclusion, our study shows significant decrease in major podocyte proteins in minimal change disease, primary and secondary FSGS, but not in time zero kidney transplant controls and in membranous nephropathy.

2025-12-29 | PXD057165 | Pride

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Fat1 is atarget antigen in de novo allograft membranous nephropoathy associated with antibody mediated rejection.

Project description:Membranous nephropathy (MN) occurs either as recurrent or de novo MN in the kidney allograft. Recurrent MN is most often associated with antibodies to the target antigen M-type phospholipase A2 receptor (PLA2R). 1-3 Most cases of de novo MN are PLA2R-negative and the target antigen in unknown.2 We have previously used the laser microdissection and mass spectrometry (LMD/MS) to search for target antigens in PLA2R-negative MN. In this study, we used LMD/MS to search for the target antigen(s) in de novo MN. Our studies identified target antigen FAT1 in de novo MN when it is associated with concurrent antibody mediated rejection.

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Identification of Novel Proteins in Membranous Nephropathy Using LC-MS

Project description:Membranous nephropathy (MN) is a primary cause of nephrotic syndrome in adults, characterized by the formation of immune complexes on the podocyte side of the glomerular basement membrane. Despite the identification of several target antigens (such as PLA2R and THSD7A), the underlying pathophysiology of MN remains incompletely understood. Recent advances in liquid chromatography–mass spectrometry (LC-MS) technology have enabled more comprehensive proteomic analyses, providing opportunities to discover novel disease-associated proteins. Identifying these proteins may enhance our understanding of MN pathogenesis and offer new diagnostic and therapeutic targets.

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Project description:Membranous nephropathy (MN) is an autoimmune kidney disease with the clinical hallmark of causing high level proteinuria. MN is caused by circulating antibodies binding to targeting antigens on the surface of podocytes â€“ specialized endothelial cells contributing to the formation of the glomerular filtration barrier. Histomorphologically MN is characterized by a deposition of IgG along the glomerular basement membrane (GBM) â€“ predominantly IgG4 in primary MN â€“ as well as an accumulation of the respective target antigen, thickening of the GBM and effacement of podocyte foot processes. The predominant MN target antigen in 70-80% of MN patients is the phospholipase A2 receptor 1. Additional target antigens, which occur with lower frequencies, have recently been described. The aim of the study was the identification of a novel MN target antigen, which fulfills the typical criteria of MN target antigen: being a podocytic membrane protein, which is recognized by IgG4 subclass specific autoantibodies. Performing a mass spectrometry analysis based on a TMT-based relative quantification approach of immunoprecipitated samples resulted in the identification of Netrin G1 (NTNG1) as a novel MN target antigen. The results were validated using immunohistochemistry, Western Blot and ELISA. The molecular characterization of patients with MN will allow a better diagnosis and clinical management of these patients in the future.

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Minor Antigens in Membranous Nephropathy Identified by Mass Spectrometry

Project description:Background: Multiple autoantigens have been identified in membranous nephropathy (MN) by tissue-based proteomics. However, the antigenic targets of disease are unknown for >10% of MN and >50% of membranous lupus nephritis (MLN) cases. We identified multiple new targets in PLA2R-/THSD7A-/EXT-/NELL1-quadruple negative MN biopsies through mass spectrometry (MS) of immune complexes recovered from biopsy tissue of patients with MN. Methods: MN cases negative for PLA2R, THSD7A, EXT1/2, and NELL1 were identified from a biopsy database. Protein G immunoprecipitation was used to recover immune complexes from frozen biopsy tissue, followed by interrogation by mass spectrometry (MS). Potential antigens were confirmed through paraffin immunofluorescence of protein targets, followed by co-localization with IgG within immune deposits. Consecutive series of 165 cases of PLA2R-negative MN biopsies and 95 MLN biopsies was screened to determine the frequency for each potential antigen. Results: Seven protein targets were discovered within immune complexes from MN biopsies including FCN3, CD206, EEA1, SEZ6L2, NPR3, MST1, and VASN. Peptides from these proteins on MS were not enriched in PLA2R (n=86), THSD7A (n=64), NELL1 (n=64), or EXT1/2 (n=60) controls. Between 3-30 unique peptides were detected for each target. Frequencies of each antigen, determined by staining consecutive case series, were SEZ6L2 (1/165 idiopathic; 0/95 MLN), VASN (8/165 idiopathic; 2/95 MLN), EEA1 (6/165 idiopathic; 7/95 MLN), MST1 (6/165 idiopathic; 2/95 MLN), and FCN3 (0/165 idiopathic, 6/95 MLN), NPR3 and CD206 were positive in index cases. All cases showed co-localization of IgG within immune deposits. Conclusion: Seven novel protein targets were identified in MN and MLN.

2023-04-06 | PXD035853 | Pride

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