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Kallikrein‐related peptidases are activators of the CC chemokine CCL14
Author(s) -
Grünberg Mario,
Quandt Dagmar,
Cynis Holger,
Demuth HansUlrich,
Kindermann Andrea,
Magdolen Viktor,
Forssmann WolfGeorg,
Seliger Barbara,
Mägert HansJürgen
Publication year - 2018
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.201747452
Subject(s) - chemokine receptor , kallikrein , biology , chemokine , ccr1 , inflammation , cancer research , immunology , biochemistry , enzyme
Chemokine CCL14 is inactive in its proform. Here, we show that inflammation‐ and cancer‐associated kallikrein‐related peptidases KLK5 and KLK8 remove the N‐terminal eight amino acids from the proform thereby converting CCL14 to its active state. Activity of the chemokine is demonstrated by migration of myeloid cells expressing relevant receptors.

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