KLK5 cleaves and activates KLK8

Stable Identifier
Reaction [transition]
Homo sapiens
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In vitro, KLK5 (Kallikrein 5) catalyzes the slow cleavage of a four-residue aminoterminal propeptide from proKLK8 (pro-Kallekrein 8), to generate active KLK8. The abundance of KLK8 in the stratum corneum and its serine endopeptidase activity are consistent with a role for KLK8 in formation of the stratum corneum, desquamation, or both. Physiological substrates for KLK8 remains to be identified, however, as do possible additional activators of it (Eissa et al. 2011). A possible pathogenic role for KLK8 is suggested by the recent demonstration that it can mediate the extracellular cleavage of the L1 capsid protein of human papilloma viruses, facilitating their infection of human host cells (Cerqueira et al. 2015).
Literature References
PubMed ID Title Journal Year
25926655 Kallikrein-8 Proteolytically Processes Human Papillomaviruses in the Extracellular Space To Facilitate Entry into Host Cells

Samperio Ventayol, P, Cerqueira, C, Vogeley, C, Schelhaas, M

J. Virol. 2015
20940292 Kallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade

Eissa, A, Diamandis, EP, Amodeo, V, Smith, CR

J. Biol. Chem. 2011
Catalyst Activity

serine-type endopeptidase activity of KLK5 [extracellular region]

Orthologous Events
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