Larynx proteomics after jellyfish collagen IL: Increased ECM/collagen and suppressed inflammation

Abstract

Objectives/Hypothesis Compare proteomic profiles of rabbit vocal folds (VFs) injected with micronized cross‐linked jellyfish collagen “collagen Type 0” (MX‐JC) against two clinical products for injection medialization laryngoplasty (IL). Study Design Animal model. Methods Left recurrent laryngeal nerve sectioning and IL were performed in New Zealand White rabbits ( N = 6/group). Group 1 received (MX‐JC) and adipose‐derived stem cells (ADSCs), Group 2, MX‐JC alone; Group 3, cross‐linked hyaluronic acid; and Group 4, micronized acellular dermis. Animals were sacrificed at 4 and 12 weeks. Proteomic profiling of injected versus noninjected VFs by nano‐liquid chromatography, tandem mass spectrometry, and reactome gene ontology analysis was performed. Results Overall, 37–61 proteins were found to be upregulated and 60–284 downregulated in injected versus non‐injected VFs (>1.5 fold, false discovery rate‐adjusted p < .05). Over‐representation analysis (% of total) revealed top up‐regulated pathways at 4 and 12 weeks, respectively: Group 1, keratan sulfate metabolism (46%) and cellular processes (29%); Group 2, extracellular matrix (ECM)/collagen processes (33%) and beta oxidation (39%); Group 3, cellular processes (50%) and energy metabolism (100%); and Group 4, keratan sulfate metabolism (31%) and inflammation (50%). Top downregulated pathways were: Group 1, Inflammation (36%) and glucose/citric acid metabolism (42%); Group 2, cell signaling (38%) and glucose/citric acid metabolism (35%); Group 3, keratan sulfate metabolism (31%) and ECM/collagen processes (48%); and Group 4, glucose/citric acid metabolism (33%) and ECM/collagen processes (43%). Conclusions MX‐JC “collagen Type 0” upregulates pathways related to ECM/collagen formation and downregulates pathways related to inflammation suggesting that it is promising biomaterial for IL. Level of Evidence NA

Structural and biofunctional evaluation of decellularized jellyfish matrices

“…Nevertheless, compared to the numerous terrestrial (e.g., bovine, porcine, human) and aquatic (e.g., tilapia, squid) animals for tissue decellularization, jellyfish are primitive animals. Their early form of collagen was thought to have similarities to different types of mammalian collagen, 26,27 providing the decellularized jellyfish ECM a potential to be widely used to regenerate different tissues, including skin, cartilage, and cornea. Jellyfish are abundant marine animals, which are also easy to farm; their quick growth can even cause This journal is © The Royal Society of Chemistry 2023 natural ecological incidents occasionally.…”

“…, I, II, III, IV, V) and may be applied to engineer various tissues. 26,27 The risk of transmitting pathogens from jellyfish to humans is low due to the vast interspecies differences. Finally, there are minimal religious restrictions for jellyfish products.…”

“…Unlike mammalian matrices that are often tissue-specific, the jellyfish's primitive collagen was considered similar to multiple mammalian collagen types (e.g., I, II, III, IV, V) and may be applied to engineer various tissues. 26,27 The risk of transmitting pathogens from jellyfish to humans is low due to the vast interspecies differences. Finally, there are minimal religious restrictions for jellyfish products.…”

Extracellular matrix type 0: From ancient collagen lineage to a versatile product pipeline – JellaGel™

“…Therefore, this matrix can be viewed as a stem of all collagen matrices: a precursor for all the matrices of higher animals. Although this matrix exhibits essential fibrillar properties of other collagen matrices, e.g., collagen type I, and can be considered as collagen type I-like [ 36 ], it demonstrates unique behaviours and amino-acid fingerprints reflective of its undifferentiated, evolutionary primitive form which precedes type I [ [34] , [35] , [36] ]. Without belonging to one particular type and due to its ancient biochemical lineage, compositional simplicity, and resemblance to multiple collagen types (e.g., I, II, III, V, IX), this matrix lends itself as a matrix type 0 [ [34] , [35] , [36] , [37] , [38] , [39] , [40] , [41] ].…”