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Targeteted quantification of RORDEPs in fasting plasma of healthy adult men

ABSTRACT: In this study, we investigated two bacterially derived polypeptides, RORDEP1 and RORDEP2, previously identified in human plasma through data-independent acquisition (DIA) mass spectrometry. To accurately measure the concentrations of these peptides in fasting plasma samples obtained from 59 healthy adult men, we utilized a targeted mass spectrometry approach based on the SUREQuant method.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Michael Wierer

LAB HEAD: Oluf Pedersen

PROVIDER: PXD057146 | Pride | 2025-06-04

REPOSITORIES: Pride

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Source:

			Action	DRS
	20240820_ASC2_EVO1_PRI_P132_R468_15cmPepSep_SQ_1to16_1.raw	Raw
	20240820_ASC2_EVO1_PRI_P132_R468_15cmPepSep_SQ_1to16_2.raw	Raw
	20240820_ASC2_EVO1_PRI_P132_R468_15cmPepSep_SQ_1to2_1.raw	Raw
	20240820_ASC2_EVO1_PRI_P132_R468_15cmPepSep_SQ_1to2_2.raw	Raw
	20240820_ASC2_EVO1_PRI_P132_R468_15cmPepSep_SQ_1to4_1.raw	Raw

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Project description:The biology and physiology of Siberian sturgeon reproduction differ substantially from teleost fish. Seminal plasma support and protect the viability, motility and fertilizing capacity of spermatozoa by creating the optimal environment for the storage. The present study for the first time described in-depth proteomic characterization of Siberian sturgeon seminal plasma using gel based and gel-free proteomic approaches: LC-MS/MS, 2DE and 2D blue native (BN)/SDS-PAGE. LC-MS/MS allowed to identify 657 proteins, which were classified according to their functions and pathways. 2DE visualized 339 spots corresponding to 76 unique proteins (almost 60% were present in various proteoforms). For the first time we demonstrated interactions between seminal proteins; four (C1-C4) multiprotein complexes were identified after 2D BN/SDS-PAGE; composed of (C1) serotransferrin-2 (TF) and fish-egg lectin (FEL); (C2) serum albumin 2 (ALB) and retinol-binding protein 4 (RBP4); (C3) ALB and TF (C3) and (C4) apolipoprotein A-I (APOA1), riboflavin-binding protein (RfBP) and myoglobin (MB). BN-SDS-PAGE also revealed that immunoglobulin and TF formed homomultimeric (dimer, trimer, tetramer and pentamer) complexes in seminal plasma. ALB, TF, Beta-Ala-His dipeptidase, glyceraldehyde-3-phosphate dehydrogenase, IGH, APOA1, hemopexin, type-4 ice-structuring protein, FEL, RfBP and glycogen phosphorylase, liver form-like were selected as major seminal plasma proteins. The functional analysis of identified proteins indicated their involvement mainly in immune system process and response to stimulus, metabolism, vesicle-mediated transport, proteolysis, and catherin binding involved in cell-cell adhesion. Moreover, 67 proteins were associated with reproductive processes, including spermatogenesis, fertilization, acrosomal reaction and sperm motility. Comparative proteomic analysis of sturgeon seminal plasma showed common proteins with fish and human and 150 proteins specific for sturgeon which may reflect the specificity of sturgeon reproduction. To conclude, this integrative proteomic view lead to deeper insight into physiological function of seminal plasma and processes occurred in sturgeon reproductive tract.

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Targeteted quantification of RORDEPs in fasting plasma of healthy adult men

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