A Proteolytic Cascade of Kallikreins in the Stratum Corneum

A Proteolytic Cascade of Kallikreins in the Stratum Corneum

Serine proteases belonging to the kallikrein group may play a central role in desquamation. We have identified human kallikreins 5, 7, and 14 (hK5, hK7, hK14) in catalytically active form in stratum corneum. All three enzymes are produced as inactive precursors. In this work, we prepared recombinant...

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Bibliographic Details
Published in:Journal of investigative dermatology Vol. 124; no. 1; pp. 198 - 203
Main Authors: Brattsand, Maria, Stefansson, Kristina, Lundh, Christine, Haasum, Ylva, Egelrud, Torbjörn
Format: Journal Article
Language:English
Published: Danvers, MA Elsevier Inc 01-01-2005
Nature Publishing
Elsevier Limited
Subjects:
Animals
Biological and medical sciences
Cells, Cultured
Dermatology
Epidermis - cytology
Epidermis - enzymology
Humans
Hydrogen-Ion Concentration
Insecta
Kallikreins - metabolism
KLK
Medical sciences
Peptides - metabolism
protease
SCCE
SCTE
Serine Endopeptidases - metabolism
Substrate Specificity
protease
KLK
SCCE
SCTE
substrate specificity
Peptidases
Stratum corneum
Vasodilator agent
Enzyme
Dermatology
Substrate specificity
KLK/protease/SCCE/SCTE/substrate specificity
Hydrolases
Skin
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Summary:Serine proteases belonging to the kallikrein group may play a central role in desquamation. We have identified human kallikreins 5, 7, and 14 (hK5, hK7, hK14) in catalytically active form in stratum corneum. All three enzymes are produced as inactive precursors. In this work, we prepared recombinant enzymes and enzyme precursors and characterized the catalytic properties of hK5 and hK14. With peptide substrates hK5 and hK14 both showed trypsin-like specificity and alkaline pH-optima. For the substrates tested, hK14 was superior to hK5 as regards maximum catalytic rate as well as catalytic efficiency. hK5, but not hK14, could activate pro-hK7 in a reaction which was optimal at pH 5–7. hK5 could activate its own precursor as well as pro-hK14. This was in contrast to hK14, which could activate pro-hK5 but not its own precursor. The activation of pro-hK5 either by auto-activation or by hK14 occurred at maximum rate at neutral or weakly alkaline pH, whereas activation of pro-hK14 by hK5 was optimal at pH 6–7. We conclude that the enzymes studied may be part of a protease cascade in the stratum corneum, and that the observed pH effects may have physiological relevance.
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content type line 23
ISSN:0022-202X
1523-1747
1523-1747
DOI:10.1111/j.0022-202X.2004.23547.x