Selective Substrates and Inhibitors for Kallikrein-Related Peptidase 7 (KLK7) Shed Light on KLK Proteolytic Activity in the Stratum Corneum.
Identifieur interne : 000377 ( PubMed/Checkpoint ); précédent : 000376; suivant : 000378Selective Substrates and Inhibitors for Kallikrein-Related Peptidase 7 (KLK7) Shed Light on KLK Proteolytic Activity in the Stratum Corneum.
Auteurs : Simon J. De Veer [France] ; Laetitia Furio [France] ; Joakim E. Swedberg [Australie] ; Christopher A. Munro [Australie] ; Maria Brattsand [Suède] ; Judith A. Clements [Australie] ; Alain Hovnanian [France] ; Jonathan M. Harris [Australie]Source :
- The Journal of investigative dermatology [ 1523-1747 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- antagonistes et inhibiteurs : Kallicréines.
- métabolisme : Kallicréines, Épiderme.
- Banque de peptides, Humains.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Kallikreins.
- metabolism : Epidermis, Kallikreins.
- Humans, Peptide Library.
Abstract
Proteases have pivotal roles in the skin's outermost layer, the epidermis. In the stratum corneum, serine proteases from the kallikrein-related peptidase (KLK) family have been implicated in several key homeostatic processes, including desquamation. However, the precise contribution of specific KLKs to each process remains unclear. To address this, we used a chemical biology approach and designed selective substrates and inhibitors for KLK7, the most abundant KLK protease in the stratum corneum. The resulting KLK7 inhibitor is the most potent inhibitor of this protease reported to date (Ki = 140 pM), and displays at least 1,000-fold selectivity over several proteases that are related by function (KLK5 and KLK14) or specificity (chymotrypsin). We then used substrates and inhibitors for KLK5, KLK7, and KLK14 to explore the activity of each protease in the stratum corneum using casein zymography and an ex vivo desquamation assay. These experiments provide the most detailed assessment of each KLK's contribution to corneocyte shedding in the plantar stratum corneum, revealing that inhibition of KLK7 alone is sufficient to block shedding, whereas KLK5 is also a major contributor. Collectively, these findings unveil chemical tools for studying KLK activity and demonstrate their potential for characterizing KLK biological functions in epidermal homeostasis.
DOI: 10.1016/j.jid.2016.09.017
PubMed: 27697464
Affiliations:
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Harris</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia. 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De Veer</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia; Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia; Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Furio, Laetitia" sort="Furio, Laetitia" uniqKey="Furio L" first="Laetitia" last="Furio">Laetitia Furio</name><affiliation wicri:level="3"><nlm:affiliation>Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Swedberg, Joakim E" sort="Swedberg, Joakim E" uniqKey="Swedberg J" first="Joakim E" last="Swedberg">Joakim E. Swedberg</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Munro, Christopher A" sort="Munro, Christopher A" uniqKey="Munro C" first="Christopher A" last="Munro">Christopher A. Munro</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Brattsand, Maria" sort="Brattsand, Maria" uniqKey="Brattsand M" first="Maria" last="Brattsand">Maria Brattsand</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Biosciences, Pathology, Umeå University, Umeå, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biosciences, Pathology, Umeå University, Umeå</wicri:regionArea><wicri:noRegion>Umeå</wicri:noRegion></affiliation></author><author><name sortKey="Clements, Judith A" sort="Clements, Judith A" uniqKey="Clements J" first="Judith A" last="Clements">Judith A. Clements</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia; Australian Prostate Cancer Research Centre, Translational Research Institute, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia; Australian Prostate Cancer Research Centre, Translational Research Institute, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Hovnanian, Alain" sort="Hovnanian, Alain" uniqKey="Hovnanian A" first="Alain" last="Hovnanian">Alain Hovnanian</name><affiliation wicri:level="3"><nlm:affiliation>Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France; Department of Genetics, Necker Hospital for Sick Children, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France; Department of Genetics, Necker Hospital for Sick Children, Paris</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Harris, Jonathan M" sort="Harris, Jonathan M" uniqKey="Harris J" first="Jonathan M" last="Harris">Jonathan M. Harris</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia. Electronic address: j2.harris@qut.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of investigative dermatology</title><idno type="eISSN">1523-1747</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Epidermis (metabolism)</term><term>Humans</term><term>Kallikreins (antagonists & inhibitors)</term><term>Kallikreins (metabolism)</term><term>Peptide Library</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Banque de peptides</term><term>Humains</term><term>Kallicréines (antagonistes et inhibiteurs)</term><term>Kallicréines (métabolisme)</term><term>Épiderme (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Kallikreins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Kallicréines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epidermis</term><term>Kallikreins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Kallicréines</term><term>Épiderme</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Peptide Library</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Banque de peptides</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Proteases have pivotal roles in the skin's outermost layer, the epidermis. In the stratum corneum, serine proteases from the kallikrein-related peptidase (KLK) family have been implicated in several key homeostatic processes, including desquamation. However, the precise contribution of specific KLKs to each process remains unclear. To address this, we used a chemical biology approach and designed selective substrates and inhibitors for KLK7, the most abundant KLK protease in the stratum corneum. The resulting KLK7 inhibitor is the most potent inhibitor of this protease reported to date (Ki = 140 pM), and displays at least 1,000-fold selectivity over several proteases that are related by function (KLK5 and KLK14) or specificity (chymotrypsin). We then used substrates and inhibitors for KLK5, KLK7, and KLK14 to explore the activity of each protease in the stratum corneum using casein zymography and an ex vivo desquamation assay. These experiments provide the most detailed assessment of each KLK's contribution to corneocyte shedding in the plantar stratum corneum, revealing that inhibition of KLK7 alone is sufficient to block shedding, whereas KLK5 is also a major contributor. Collectively, these findings unveil chemical tools for studying KLK activity and demonstrate their potential for characterizing KLK biological functions in epidermal homeostasis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27697464</PMID><DateCreated><Year>2016</Year><Month>10</Month><Day>04</Day></DateCreated><DateCompleted><Year>2017</Year><Month>07</Month><Day>20</Day></DateCompleted><DateRevised><Year>2017</Year><Month>07</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1523-1747</ISSN><JournalIssue CitedMedium="Internet"><Volume>137</Volume><Issue>2</Issue><PubDate><Year>2017</Year><Month>Feb</Month></PubDate></JournalIssue><Title>The Journal of investigative dermatology</Title><ISOAbbreviation>J. Invest. Dermatol.</ISOAbbreviation></Journal><ArticleTitle>Selective Substrates and Inhibitors for Kallikrein-Related Peptidase 7 (KLK7) Shed Light on KLK Proteolytic Activity in the Stratum Corneum.</ArticleTitle><Pagination><MedlinePgn>430-439</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0022-202X(16)32463-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jid.2016.09.017</ELocationID><Abstract><AbstractText>Proteases have pivotal roles in the skin's outermost layer, the epidermis. In the stratum corneum, serine proteases from the kallikrein-related peptidase (KLK) family have been implicated in several key homeostatic processes, including desquamation. However, the precise contribution of specific KLKs to each process remains unclear. To address this, we used a chemical biology approach and designed selective substrates and inhibitors for KLK7, the most abundant KLK protease in the stratum corneum. The resulting KLK7 inhibitor is the most potent inhibitor of this protease reported to date (Ki = 140 pM), and displays at least 1,000-fold selectivity over several proteases that are related by function (KLK5 and KLK14) or specificity (chymotrypsin). We then used substrates and inhibitors for KLK5, KLK7, and KLK14 to explore the activity of each protease in the stratum corneum using casein zymography and an ex vivo desquamation assay. These experiments provide the most detailed assessment of each KLK's contribution to corneocyte shedding in the plantar stratum corneum, revealing that inhibition of KLK7 alone is sufficient to block shedding, whereas KLK5 is also a major contributor. Collectively, these findings unveil chemical tools for studying KLK activity and demonstrate their potential for characterizing KLK biological functions in epidermal homeostasis.</AbstractText><CopyrightInformation>Copyright © 2016 The Authors. Published by Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>de Veer</LastName><ForeName>Simon J</ForeName><Initials>SJ</Initials><AffiliationInfo><Affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia; Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Furio</LastName><ForeName>Laetitia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Swedberg</LastName><ForeName>Joakim E</ForeName><Initials>JE</Initials><AffiliationInfo><Affiliation>Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Munro</LastName><ForeName>Christopher A</ForeName><Initials>CA</Initials><AffiliationInfo><Affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brattsand</LastName><ForeName>Maria</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Medical Biosciences, Pathology, Umeå University, Umeå, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Clements</LastName><ForeName>Judith A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia; Australian Prostate Cancer Research Centre, Translational Research Institute, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hovnanian</LastName><ForeName>Alain</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratory of Genetic Skin Diseases, INSERM UMR 1163 and Imagine Institute of Genetic Diseases, Paris, France; Université Paris V Descartes-Sorbonne Paris Cité, Paris, France; Department of Genetics, Necker Hospital for Sick Children, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harris</LastName><ForeName>Jonathan M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland, Australia. Electronic address: j2.harris@qut.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>09</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Invest Dermatol</MedlineTA><NlmUniqueID>0426720</NlmUniqueID><ISSNLinking>0022-202X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019151">Peptide Library</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="C425336">KLK14 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="C400147">KLK5 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="C082472">KLK7 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D007610">Kallikreins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004817" MajorTopicYN="N">Epidermis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007610" MajorTopicYN="N">Kallikreins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019151" MajorTopicYN="N">Peptide Library</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>08</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>09</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>10</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>7</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>10</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27697464</ArticleId><ArticleId IdType="pii">S0022-202X(16)32463-0</ArticleId><ArticleId IdType="doi">10.1016/j.jid.2016.09.017</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>France</li><li>Suède</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><country name="France"><region name="Île-de-France"><name sortKey="De Veer, Simon J" sort="De Veer, Simon J" uniqKey="De Veer S" first="Simon J" last="De Veer">Simon J. De Veer</name></region><name sortKey="Furio, Laetitia" sort="Furio, Laetitia" uniqKey="Furio L" first="Laetitia" last="Furio">Laetitia Furio</name><name sortKey="Hovnanian, Alain" sort="Hovnanian, Alain" uniqKey="Hovnanian A" first="Alain" last="Hovnanian">Alain Hovnanian</name></country><country name="Australie"><noRegion><name sortKey="Swedberg, Joakim E" sort="Swedberg, Joakim E" uniqKey="Swedberg J" first="Joakim E" last="Swedberg">Joakim E. Swedberg</name></noRegion><name sortKey="Clements, Judith A" sort="Clements, Judith A" uniqKey="Clements J" first="Judith A" last="Clements">Judith A. Clements</name><name sortKey="Harris, Jonathan M" sort="Harris, Jonathan M" uniqKey="Harris J" first="Jonathan M" last="Harris">Jonathan M. Harris</name><name sortKey="Munro, Christopher A" sort="Munro, Christopher A" uniqKey="Munro C" first="Christopher A" last="Munro">Christopher A. Munro</name></country><country name="Suède"><noRegion><name sortKey="Brattsand, Maria" sort="Brattsand, Maria" uniqKey="Brattsand M" first="Maria" last="Brattsand">Maria Brattsand</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \
| NlmPubMed2Wicri -a AustralieFrV1
| This area was generated with Dilib version V0.6.33. |  |