La maladie de Parkinson au Canada (serveur d'exploration)

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Functional Roles of Human Kallikrein-related Peptidases*

Identifieur interne : 000548 ( Pmc/Curation ); précédent : 000547; suivant : 000549

Functional Roles of Human Kallikrein-related Peptidases*

Auteurs : Georgia Sotiropoulou ; Georgios Pampalakis ; Eleftherios P. Diamandis

Source :

RBID : PMC:2785139

Abstract

Kallikrein-related peptidases constitute a single family of 15 (chymo)trypsin-like proteases (KLK1–15) with pleiotropic physiological roles. Aberrant regulation of KLKs has been associated with diverse diseases such as hypertension, renal dysfunction, skin disorders, inflammation, neurodegeneration, and cancer. Recent studies suggested that coordinated activation and regulation of KLK activity are achieved via a complex network of interactions referred to as the “KLK activome.” However, it remains to be validated whether these hypothetical KLK activation cascade pathways are operative in vivo. In addition, KLKs have emerged as versatile signaling molecules. In summary, KLKs represent attractive biomarkers for clinical applications and potential therapeutic targets for common human pathologies.


Url:
DOI: 10.1074/jbc.R109.027946
PubMed: 19819870
PubMed Central: 2785139

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PMC:2785139

Le document en format XML

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<p>Kallikrein-related peptidases constitute a single family of 15 (chymo)trypsin-like proteases (KLK1–15) with pleiotropic physiological roles. Aberrant regulation of KLKs has been associated with diverse diseases such as hypertension, renal dysfunction, skin disorders, inflammation, neurodegeneration, and cancer. Recent studies suggested that coordinated activation and regulation of KLK activity are achieved via a complex network of interactions referred to as the “KLK activome.” However, it remains to be validated whether these hypothetical KLK activation cascade pathways are operative
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<aff id="aff1">From the
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Department of Pharmacy, University of Patras, Rion, 26500 Rion-Patras, Greece,</aff>
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Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada,</aff>
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Department of Clinical Biochemistry, University Health Network, Toronto, Ontario M5G 2C4, Canada and</aff>
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Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 1A1, Canada</aff>
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To whom correspondence should be addressed. E-mail:
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<p>Kallikrein-related peptidases constitute a single family of 15 (chymo)trypsin-like proteases (KLK1–15) with pleiotropic physiological roles. Aberrant regulation of KLKs has been associated with diverse diseases such as hypertension, renal dysfunction, skin disorders, inflammation, neurodegeneration, and cancer. Recent studies suggested that coordinated activation and regulation of KLK activity are achieved via a complex network of interactions referred to as the “KLK activome.” However, it remains to be validated whether these hypothetical KLK activation cascade pathways are operative
<italic>in vivo</italic>
. In addition, KLKs have emerged as versatile signaling molecules. In summary, KLKs represent attractive biomarkers for clinical applications and potential therapeutic targets for common human pathologies.</p>
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