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General protein substrates in plasma and inflamed tissues is a broad pharmacological designation for the diverse set of proteins targeted by exogenous proteolytic enzymes used in systemic enzyme therapy (DrugBank Online, DB09031). This category encompasses various plasma-borne proteins, such as fibrin, kininogens, and albumin, as well as specific inflammatory mediators and cellular debris that accumulate at sites of tissue injury (Pavan et al., 2012, Biotechnology Research International). Therapeutic agents like bromelains, serratiopeptidase, and trypsin interact with these substrates by catalyzing the hydrolysis of peptide bonds, thereby facilitating the resolution of edema, reducing inflammation, and promoting tissue repair (Tiwari, 2017, Asian Journal of Pharmaceutical and Clinical Research). By breaking down fibrin deposits and modulating the permeability of the microvasculature, these enzymes help restore normal circulation and accelerate the healing process in conditions such as post-operative swelling or chronic inflammation (Rathnavelu et al., 2016, Biomedical Reports). However, because this term describes a heterogeneous group of molecules rather than a single, well-defined protein or receptor, it is typically used as a placeholder in drug databases to characterize the multi-target activity of non-specific proteases. Consequently, drugs interacting with these substrates often exhibit pleiotropic effects, ranging from anti-inflammatory and anti-edematous actions to the promotion of wound debridement and tissue repair.
Proteolytic cleavage of peptide bonds in various proteins found in plasma and at sites of inflammation, leading to reduced capillary permeability, breakdown of fibrin clots, and resolution of edema.
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