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The Probable serine carboxypeptidase CPVL is an enzyme encoded by the CPVL gene, predominantly expressed in human monocytes and macrophages, with high mRNA levels in the heart and kidney[1][3][4][5]. Structurally, CPVL possesses features typical of serine carboxypeptidases, although its enzymatic activity has not yet been confirmed experimentally[1][3]. It is localized to the endoplasmic reticulum and endosomal/lysosomal compartments, and is found in lamellipodia and membrane ruffles of macrophages associated with the secretory pathway and actin cytoskeleton remodeling[3]. CPVL is hypothesized to function in the processing of antigens for MHC class I and II presentation, in peptide trimming within lysosomes, and possibly in regulating cytokine and chemokine secretion, though precise biological roles remain to be clarified[1][3][4][5]. Genetic deletion is linked to Wilms tumor, and variants are associated with diabetic nephropathy susceptibility; it is also down-regulated in response to inflammation and may serve as a biomarker for infectious disease severity[1][3][5]. No approved pharmaceuticals are known to directly modulate CPVL function currently.
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