ArticleEuropean spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society2026
Proteomic signature of human annulus fibrosus and cartilage endplate: divergent matrisomal architectures reveal complementary roles in intervertebral disc homeostasis.
Article in European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
purposeThe baseline proteomic architecture of healthy human annulus fibrosus (AF) and cartilage endplate (CEP) is poorly defined. A rigorous healthy-tissue reference is essential for identifying the early molecular deviations that drive degenerative disc disease (DDD).
methodsAF (n = 20) and CEP (n = 21) tissues were harvested from healthy brain-dead organ donors (Pfirrmann Grade I). After 8 M urea/TEAB extraction, proteins were reduced, alkylated, and digested with sequencing-grade trypsin. Tryptic peptides were analysed in triplicate by nano-LC-MS/MS (Q-Exactive Plus Orbitrap) and processed with Proteome Discoverer 2.5 against UniProt Homo sapiens (FDR < 1%). Matrisome annotation used Human MatrisomeDB. GO and KEGG enrichment were used with DAVID and ShinyGO v0.82. Proteome overlap was quantified by Jaccard similarity; intra-tissue variability by Kruskal-Wallis analysis of log₂-normalised NSAF values.
results470 proteins were identified in AF and 1,899 in CEP. The AF proteome was enriched in ECM glycoproteins (57% of matrisome), ECM regulators-notably serine protease inhibitors and matrix metalloproteinases (48%)-and glycolytic enzymes reflecting adaptation to hypoxia and tensile load. The CEP proteome featured higher collagen density (30%), ECM-affiliated proteins (48%), and extensive mitochondrial pathway enrichment (TCA cycle, oxidative phosphorylation), establishing it as a metabolically active interface for nutrient transport and proteostasis. AF-CEP proteome overlap was the lowest pairwise compartment comparison (≈ 20%), and CEP exhibited significantly greater intra-tissue variability than AF or NP (p = 2 × 10⁻³²).
conclusionThis study delivers the first comprehensive paired proteomic atlas of healthy human AF and CEP. The AF emerges as a mechanically adaptive, ECM-remodelling tissue; the CEP as a metabolically specialised cartilage-bone interface. Integrated with the published healthy NP proteome, these data constitute a three-compartment human IVD molecular reference baseline for degeneration research and therapeutic target discovery.
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