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Peptidylarginine deiminase type 3 (PAD3) is a calcium-dependent enzyme that catalyzes the post-translational conversion (deimination/citrullination) of arginine residues to citrulline in proteins, a critical process in the formation and mechanical strength of hair and skin. PAD3 is predominantly expressed in keratinocytes of the skin and hair follicles, and abnormal enzyme function is linked to hair shaft disorders and certain skin conditions. Recent research implicates PAD3 in cell growth modulation via apoptosis-inducing factors and in neurodegenerative responses, such as those following spinal cord injury. Experimental small molecules have been designed to selectively inhibit PAD3, but no approved drugs currently target this enzyme. PAD3 has also been detected in mammary gland tissue, with emerging evidence suggesting regulation by prolactin and potential involvement in cancer and lactation[1][2][3][4][5][7][8].
Inhibitors block the enzyme’s calcium-dependent deimination of arginine residues, thus preventing protein citrullination
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