Protein substrates of bromelain

Bromelain is a complex mixture of thiol-proteases derived from the stem and fruit of the pineapple plant (Ananas comosus). The protein substrates of bromelain represent the diverse group of molecules that these enzymes proteolytically cleave to achieve therapeutic effects (Maurer, 2001). Major substrates include fibrin, which is degraded to promote fibrinolysis and reduce edema, and kininogens, whose cleavage leads to reduced bradykinin production and diminished inflammation (Pavan et al., 2012). Bromelain also targets various cell surface molecules, such as CD44, CD45, and the chemokine receptors CXCR1 and CXCR2, thereby modulating leukocyte migration and immune signaling (Hikisz & Bernasinska-Slomczewska, 2021). In clinical applications, bromelain-based products like NexoBrid are utilized for the enzymatic debridement of burn eschar by selectively digesting necrotic tissue proteins while sparing healthy dermis (NexoBrid Prescribing Information). Because these substrates are involved in critical processes like blood coagulation and immune response, the use of bromelain can lead to increased bleeding risks and potential hypersensitivity reactions in susceptible individuals (Pavan et al., 2012).

Other names

Bromelain targetsBromelain-sensitive proteinsFibrinKininogenCD44CD45CXCR1CXCR2

Proteolytic cleavage and degradation of target proteins leading to functional inactivation or removal