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Lysosomal mucolytic enzymes are a functional group of acid hydrolases, including glycosidases, sulfatases, and proteases, located within the lysosomes of mucus-secreting cells such as bronchial submucosal glands and goblet cells [1, 3]. These enzymes are responsible for the intracellular and extracellular catabolism of complex acidic mucopolysaccharides and glycoproteins that constitute the structural framework of mucus [3, 4]. Pharmacological agents such as bromhexine and its active metabolite ambroxol target these enzymes by stimulating their release from lysosomes into the cytoplasm and mucus granules [1, 4]. This liberation leads to the enzymatic depolymerization of tenacious mucus fibers, effectively reducing mucus viscosity and facilitating clearance via the mucociliary escalator [2, 3]. Beyond respiratory applications, specific enzymes in this class, such as beta-glucocerebrosidase, are targets for pharmacological chaperones like ambroxol in the treatment of lysosomal storage disorders and neurodegenerative diseases [5]. Consequently, these enzymes represent a critical therapeutic target for managing both obstructive airway diseases and certain metabolic or neurological conditions [1, 5]. The activation of these enzymes helps normalize the rheological properties of respiratory secretions, which is vital for patients with chronic bronchitis or cystic fibrosis [2, 4]. Safety profiles for drugs targeting these enzymes are generally favorable, though rare systemic hypersensitivity reactions have been reported [1]. Sources: [1] BenchChem, 2025; [2] MDPI, 2024; [3] IJRAPS, 2017; [4] Takeda H, et al., Japanese Journal of Pharmacology, 1983; [5] NIH/PubMed, 2018.
Stimulation of the release and activity of lysosomal enzymes (such as glycosidases and proteases) from mucus-secreting cells to depolymerize acidic mucopolysaccharide fibers in mucus [1, 4].
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