In biology, collagen-biomaterial regulates several signaling mechanisms of bone and immune cells involved in tissue repair and any imbalance in collagen turnover may affect the homeostasis of cells, becoming a major cause of several complications. In this case, the administration of oral collagen may play a potential role in returning cells to their normal function. For several decades, the beneficial effects of collagen have been explored widely, and thus many commercial products are available in cosmetics, food, and biomedical fields. For instance, collagen-based-products have been widely used to treat the complications of cartilage-related-disorders. Many researchers are reporting the anti-arthritogenic properties of collagen-based materials. In contrast, collagen, especially type-II collagen (CII), has been widely used to induce arthritis by immunization in an animal-model with or without adjuvants, and the potentially immunogenic-properties of collagen have been continuously reported for a long time. Additionally, the immune tolerance of collagen is mainly regulated by the T-lymphocytes and B-cells. This controversial hypothesis is getting more and more evidence nowadays from both sides to support its mechanism. Therefore, this review links the gap between the arthritogenic and anti-arthritogenic effects of collagen and explored the actual mechanism to understand the fundamental concept of collagen in arthritis. Accordingly, this review opens-up several unrevealed scientific knots of collagen and arthritis and helps the researchers understand the potential use of collagen in therapeutic applications.

Fibrin clot structure and function are major determinants of venous and arterial thromboembolic diseases, as well as the key determinants of the efficiency of clot lysis. Studies have revealed that fungi fibrinolytic compound 1 (FGFC1) is a novel marine pyranisoindolone natural product with fibrinolytic activity. Here, we explore the impacts of FGFC1 on clot structure, lysis, and plasminogen activation in vitro using turbidimetric, enzyme-linked immunosorbent assay, confocal and electron microscopy, urokinase, or plasmin chromogenic substrate. Clots formed in the presence of FGFC1 expressed reduced fibrin polymerization rate and maximum turbidity; however, they did not influence the lag phase of fibrin polymerization. In the absence of scu-PA (single-chain urokinase plasminogen activator), microscopy revealed that FGFC1 increased the number of protofibrils within fibrin fiber and the pore diameter between protofibrils, inducing clots to form a region of thinner and looser networks separated by large pores. The effects of FGFC1 on scu-PA-mediated plasma clot structure were similar to those in the absence of scu-PA. In addition, FGFC1 promoted the lysis of clots and increased the D-dimer concentration in lysate. FGFC1 increased the generation rate of p-nitroaniline in plasma. These results show that FGFC1 has fibrinolytic activity in plasma, leading to interference with the release of fibrinopeptide B to affect lateral aggregation of protofibrils and increase clot susceptibility to fibrinolysis by altering its structure.

Due to environmental pollution, unhealthy lifestyles, and autoimmunity, many individuals frequently encounter skin problems, such as sensitive skin, caused by the activation of the TRPV1 pathway and immune-inflammatory reactions. This study aims to synthesize compounds with soothing effects using β-chitooligosaccharides (COS) derived from marine Sargassum, which is investigated for its regulating inflammatory responses and activating of TRPV1 pathways. Dopamine is used as the hydroxyl donor in this process. COS-diDA, a compound that binds two dopamine amines, is synthesized using Michael additions and Schiff base reactions under alkaline circumstances, with a pH of 8.5. This work investigates the soothing effects of COS-diDA using a HaCaT cell model activated with capsaicin (CAP). ELISA and immunofluorescence experiments provide evidence that COS-diDA efficiently inhibits the activation of the TRPV1 protein in HaCaT cells by reducing its levels when stimulated with CAP. In addition, ELISA analysis demonstrates that COS-diDA reduces the secretion of IL-1α, IL-6, and IL-8 from HaCaT cells stimulated with CAP, indicating an interaction between the TRPV1 protein and interleukins. Additional research on in vitro pain models generated by CAP confirms the anti-inflammatory and soothing properties of COS-diDA. The study indicates that COS-diDA exhibits favorable adhesion qualities and possesses anti-inflammatory action, making it a viable candidate for inclusion as an anti-inflammatory component of cosmetic formulations.