{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T06:43:43Z","timestamp":1791009823666,"version":"4.1.0"},"reference-count":81,"publisher":"Georg Thieme Verlag KG","issue":"09","funder":[{"name":"grant of Deutsche Forschungsgemeinschaft","award":["Me2037\/3-1"],"award-info":[{"award-number":["Me2037\/3-1"]}]},{"name":"research rotation position for UMH as part of the collaborative research centre","award":["SFB877"],"award-info":[{"award-number":["SFB877"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Thromb Haemost"],"published-print":{"date-parts":[[2013]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Kallikrein-related peptidases (KLKs) constitute a family of 15 highly conserved serine proteases, which show a tissue-specific expression profile. This made them valuable tumour expression markers. It became evident that KLKs are involved in many physiological processes like semen liquefaction and skin desquamation. More recently, we have learnt that they are involved in many pathophysiological conditions and diseases making them promising target of therapeutic intervention. Therefore, regulation of KLKs raised the interest of numerous reports. Herein, we summarise the current knowledge on KLKs regulation with an emphasis on skin-relevant KLKs regulation processes. Regulation of KLKs takes place on the level of transcription, on protease activation and on protease inactivation. A variety of protease inhibitors has been described to interact with KLKs including the irreversible serine protease inhibitors (SERPINs) and the reversible serine protease inhibitors of Kazal-type (SPINKs). In an attempt to integrate current knowledge, we propose that KLK regulation has credentials as targets for therapeutic intervention.<\/jats:p>","DOI":"10.1160\/th12-11-0836","type":"journal-article","created":{"date-parts":[[2013,2,28]],"date-time":"2013-02-28T16:35:53Z","timestamp":1362069353000},"page":"442-449","source":"Crossref","is-referenced-by-count":44,"title":["Regulation of kallikrein-related peptidases in the skin \u2013 from physiology to diseases to therapeutic options"],"prefix":"10.1160","volume":"110","author":[{"given":"Jan","family":"Fischer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulf","family":"Meyer-Hoffert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"194","published-online":{"date-parts":[[2017,11,22]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"e13781.","DOI":"10.1371\/journal.pone.0013781","article-title":"Evolutionary history of tissue kallikreins","volume":"05","author":"A Pavlopoulou","year":"2010","journal-title":"PLoS ONE"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1515\/bc.2010.056","article-title":"Kallikrein-related peptidase genes as promising biomarkers for prognosis and monitoring of human malignancies","volume":"391","author":"M Avgeris","year":"2010","journal-title":"Biol Chem"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1677\/erc.1.00958","article-title":"Kallikrein 4 (hK4) and prostate-specific antigen (PSA) are associated with the loss of E-cadherin and an epithelial-mesenchymal transition (EMT)-like effect in prostate cancer cells","volume":"12","author":"TL Veveris-Lowe","year":"2005","journal-title":"Endocr Relat Cancer"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1515\/bc.2010.038","article-title":"Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier","volume":"391","author":"K Oikonomopoulou","year":"2010","journal-title":"Biol Chem"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1158\/0008-5472.CAN-09-3415","article-title":"Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma","volume":"70","author":"Y Dong","year":"2010","journal-title":"Cancer Res"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1046\/j.1523-1747.2000.00820.x","article-title":"Stratum corneum tryptic enzyme in normal epidermis: a missing link in the desquamation process?","volume":"114","author":"IE Ekholm","year":"2000","journal-title":"J Invest Dermatol"},{"key":"ref7","first-page":"471","article-title":"Stratum corneum chymotryptic enzyme: a proteinase which may be generally present in the stratum corneum and with a possible involvement in desquamation","volume":"71","author":"A Lundstrom","year":"1991","journal-title":"Acta DermVenereol"},{"key":"ref8","first-page":"44","article-title":"Desquamation in the stratums corneum","volume":"208","author":"T Egelrud","year":"2000","journal-title":"Acta DermVenereol"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1515\/BC.2006.095","article-title":"Kallikrein-related peptidase 14 may be a major contributor to trypsin-like proteolytic activity in human stratum corneum","volume":"387","author":"K Stefansson","year":"2006","journal-title":"Biol Chem"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1074\/jbc.M110.125310","article-title":"Kallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade","volume":"286","author":"A Eissa","year":"2011","journal-title":"J Biol Chem"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"2019","DOI":"10.1007\/s00018-008-8024-3","article-title":"Kallikrein-related peptidases","volume":"65","author":"A Lundwall","year":"2008","journal-title":"Cell Mol Life Sci"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1373\/clinchem.2007.088104","article-title":"Distribution of 15 human kallikreins in tissues and biological fluids","volume":"53","author":"JL Shaw","year":"2007","journal-title":"Clin Chem"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1046\/j.1523-1747.2003.12363.x","article-title":"Expression and localisation of tissue kallikrein mRNAs in human epidermis and appendages","volume":"121","author":"N Komatsu","year":"2003","journal-title":"J Invest Dermatol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1111\/j.1365-2133.2005.06754.x","article-title":"Multiple tissue kallikrein mRNA and protein expression in normal skin and skin diseases","volume":"153","author":"N Komatsu","year":"2005","journal-title":"Br J Dermatol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1699","DOI":"10.4049\/jimmunol.157.4.1699","article-title":"IL-1 beta activation in human epidermis","volume":"157","author":"E Nylander-Lundqvist","year":"1996","journal-title":"J Immunol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"7968","DOI":"10.1074\/jbc.M507705200","article-title":"Tissue kallikrein mK13 is a candidate processing enzyme for the precursor of interleukin-1beta in the submandibular gland of mice","volume":"281","author":"C Yao","year":"2006","journal-title":"J Biol Chem"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"2068","DOI":"10.1096\/fj.06-6075com","article-title":"Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin","volume":"20","author":"K Yamasaki","year":"2006","journal-title":"FASEB J"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1038\/nm1616","article-title":"Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea","volume":"13","author":"K Yamasaki","year":"2007","journal-title":"Nat Med"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1038\/jidsymp.2011.2","article-title":"Epidermal proteases in the pathogenesis of rosacea","volume":"15","author":"U Meyer-Hoffert","year":"2011","journal-title":"J Investig Dermatol Symp Proc"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1515\/BC.2008.158","article-title":"Regulation of human tissue kallikrein-related peptidase expression by steroid hormones in 32 cell lines","volume":"389","author":"JL Shaw","year":"2008","journal-title":"Biol Chem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"2229","DOI":"10.4049\/jimmunol.178.4.2229","article-title":"The effects of IL-20 subfamily cytokines on reconstituted human epidermis suggest potential roles in cutaneous innate defense and pathogenic adaptive immunity in psoriasis","volume":"178","author":"SM Sa","year":"2007","journal-title":"J Immunol"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1111\/j.1365-2133.2006.07743.x","article-title":"Aberrant human tissue kallikrein levels in the stratum corneum and serum of patients with psoriasis: dependence on phenotype, severity and therapy","volume":"156","author":"N Komatsu","year":"2007","journal-title":"Br J Dermatol"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1111\/j.1365-2133.2009.09142.x","article-title":"Increased stratum corneum serine protease activity in acute eczematous atopic skin","volume":"161","author":"R Voegeli","year":"2009","journal-title":"Br J Dermatol"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1111\/j.1468-2494.2011.00671.x","article-title":"Increased mass levels of certain serine proteases in the stratum corneum in acute eczematous atopic skin","volume":"33","author":"R Voegeli","year":"2011","journal-title":"Int J Cosmet Sci"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1038\/jid.2009.435","article-title":"Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D(3), and retinoic acid","volume":"130","author":"S Morizane","year":"2010","journal-title":"J Invest Dermatol"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0014-4835(03)00087-3","article-title":"Up-regulated gene expression in the conjunctival epithelium of patients with Sjogren's syndrome","volume":"77","author":"S Kawasaki","year":"2003","journal-title":"Exp Eye Res"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1515\/BC.2009.026","article-title":"A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15","volume":"390","author":"H Yoon","year":"2009","journal-title":"Biol Chem"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"31852","DOI":"10.1074\/jbc.M705190200","article-title":"Activation profiles and regulatory cascades of the human kallikrein-related peptidases","volume":"282","author":"H Yoon","year":"2007","journal-title":"J Biol Chem"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1515\/bc.2010.055","article-title":"Interdependence of kallikrein-related peptidases in proteolytic networks","volume":"391","author":"N Beaufort","year":"2010","journal-title":"Biol Chem"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1515\/hsz-2012-0249","article-title":"Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases","volume":"394","author":"H Yoon","year":"2013","journal-title":"Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1515\/bc.2010.023","article-title":"Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation","volume":"391","author":"A Ohler","year":"2010","journal-title":"Biol Chem"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/ng.629","article-title":"Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome","volume":"42","author":"KU Sales","year":"2010","journal-title":"Nat Genet"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1515\/bc.2010.024","article-title":"Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis","volume":"391","author":"M Blaber","year":"2010","journal-title":"Biol Chem"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1038\/jid.2012.14","article-title":"Doxycycline Indirectly Inhibits Proteolytic Activation of Tryptic Kallikrein-Related Peptidases and Activation of Cathelicidin","volume":"132","author":"KN Kanada","year":"2012","journal-title":"J Invest Dermatol"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.phrs.2010.10.007","article-title":"Clinical applications of non-antimicrobial tetracyclines in dermatology","volume":"63","author":"E Monk","year":"2011","journal-title":"Pharmacol Res"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1515\/BC.2007.049","article-title":"Enzymatic properties of human kallikrein-related peptidase 12 (KLK12)","volume":"388","author":"N Memari","year":"2007","journal-title":"Biol Chem"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"2405","DOI":"10.1074\/jbc.M608348200","article-title":"Expression and functional characterisation of the cancer-related serine protease, human tissue kallikrein 14","volume":"282","author":"CA Borgono","year":"2007","journal-title":"J Biol Chem"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1515\/BC.2004.061","article-title":"Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation\/inactivation","volume":"385","author":"A Bayes","year":"2004","journal-title":"Biol Chem"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"2074","DOI":"10.1038\/sj.jid.5700351","article-title":"Serine protease signaling of epidermal permeability barrier homeostasis","volume":"126","author":"JP Hachem","year":"2006","journal-title":"J Invest Dermatol"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1016\/j.biochi.2010.06.022","article-title":"Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs)","volume":"92","author":"P Goettig","year":"2010","journal-title":"Biochimie"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S1462399406000184","article-title":"Mechanisms of serpin dysfunction in disease","volume":"08","author":"D Kaiserman","year":"2006","journal-title":"Expert Rev Mol Med"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1016\/j.ajpath.2011.05.012","article-title":"Serpin peptidase inhibitor clade A member 1 (SerpinA1) is a novel biomarker for progression of cutaneous squamous cell carcinoma","volume":"179","author":"M Farshchian","year":"2011","journal-title":"Am J Pathol"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"28889","DOI":"10.1074\/jbc.M111.249979","article-title":"Pivotal role for alpha1-antichymotrypsin in skin repair","volume":"286","author":"DC Hoffmann","year":"2011","journal-title":"J Biol Chem"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1046\/j.1523-1747.1999.00644.x","article-title":"Protein C inhibitor is expressed in keratinocytes of human skin","volume":"113","author":"M Krebs","year":"1999","journal-title":"J Invest Dermatol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/j.acthis.2007.04.007","article-title":"Immunolocalisation of protein C inhibitor in differentiation of human epidermal keratinocytes","volume":"109","author":"C Zhang","year":"2007","journal-title":"Acta Histochem"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1002\/jcp.20016","article-title":"PAI-1 expression is required for epithelial cell migration in two distinct phases of in vitro wound repair","volume":"200","author":"KM Providence","year":"2004","journal-title":"J Cell Physiol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/75977","article-title":"Mutations in SPINK5, encoding a serine protease inhibitor, cause Netherton syndrome","volume":"25","author":"S Chavanas","year":"2000","journal-title":"Nat Genet"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1159\/000257290","article-title":"Ichthyosis linearis circumflexa","volume":"98","author":"M Comel","year":"1949","journal-title":"Dermatologica"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1001\/archderm.1958.01560100059009","article-title":"A unique case of trichorrhexis nodosa; bamboo hairs","volume":"78","author":"EW Netherton","year":"1958","journal-title":"AMA Arch Derm"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"2417","DOI":"10.1093\/hmg\/ddg247","article-title":"LEKTI proteolytic processing in human primary keratinocytes, tissue distribution and defective expression in Netherton syndrome","volume":"12","author":"E Bitoun","year":"2003","journal-title":"Hum Mol Genet"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1111\/j.1365-2133.2005.06834.x","article-title":"hK5 and hK7, two serine proteinases abundant in human skin, are inhibited by LEKTI domain 6","volume":"153","author":"T Egelrud","year":"2005","journal-title":"Br J Dermatol"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1038\/ng1493","article-title":"Spink5-deficient mice mimic Netherton syndrome through degradation of desmoglein 1 by epidermal protease hyperactivity","volume":"37","author":"P Descargues","year":"2005","journal-title":"Nat Genet"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1038\/sj.jid.5700288","article-title":"Serine protease activity and residual LEKTI expression determine phenotype in Netherton syndrome","volume":"126","author":"JP Hachem","year":"2006","journal-title":"J Invest Dermatol"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1084\/jem.20082242","article-title":"Kallikrein 5 induces atopic dermatitis-like lesions through PAR2-mediated thymic stromal lymphopoietin expression in Netherton syndrome","volume":"206","author":"A Briot","year":"2009","journal-title":"J Exp Med"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"2736","DOI":"10.1038\/jid.2010.233","article-title":"Par2 inactivation inhibits early production of TSLP, but not cutaneous inflammation, in Netherton syndrome adult mouse model","volume":"130","author":"A Briot","year":"2010","journal-title":"J Invest Dermatol"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.1038\/jid.2011.295","article-title":"When activity requires breaking up: LEKTI proteolytic activation cascade for specific proteinase inhibition","volume":"131","author":"L Furio","year":"2011","journal-title":"J Invest Dermatol"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"3874","DOI":"10.1021\/bi027029v","article-title":"Inhibition of serine proteinases plasmin, trypsin, subtilisin A, cathepsin G, and elastase by LEKTI: a kinetic analysis","volume":"42","author":"K Mitsudo","year":"2003","journal-title":"Biochemistry"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.pep.2003.12.004","article-title":"Expression of LEKTI domains 6-9' in the baculovirus expression system: recombinant LEKTI domains 6-9' inhibit trypsin and subtilisin A","volume":"35","author":"A Jayakumar","year":"2004","journal-title":"Protein Expr Purif"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1515\/BC.2005.134","article-title":"Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI)","volume":"386","author":"NM Schechter","year":"2005","journal-title":"Biol Chem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.jchromb.2003.07.016","article-title":"Recombinant production, purification and biochemical characterisation of domain 6 of LEKTI: a temporary Kazal-type-related serine proteinase inhibitor","volume":"803","author":"P Kreutzmann","year":"2004","journal-title":"J Chromatogr B Analyt Technol Biomed Life Sci"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"3607","DOI":"10.1091\/mbc.e07-02-0124","article-title":"LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction","volume":"18","author":"C Deraison","year":"2007","journal-title":"Mol Biol Cell"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"3640","DOI":"10.1074\/jbc.M607567200","article-title":"A potential role for multiple tissue kallikrein serine proteases in epidermal desquamation","volume":"282","author":"CA Borgono","year":"2007","journal-title":"J Biol Chem"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1038\/jid.2011.174","article-title":"Proteolytic activation cascade of the Netherton syndrome-defective protein, LEKTI, in the epidermis: implications for skin homeostasis","volume":"131","author":"P Fortugno","year":"2011","journal-title":"J Invest Dermatol"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"4187","DOI":"10.1093\/hmg\/dds243","article-title":"The 420K LEKTI variant alters LEKTI proteolytic activation and results in protease deregulation: implications for atopic dermatitis","volume":"21","author":"P Fortugno","year":"2012","journal-title":"Hum Mol Genet"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"e4372.","DOI":"10.1371\/journal.pone.0004372","article-title":"Identification of lympho-epithelial Kazal-type inhibitor 2 in human skin as a kallikrein-related peptidase 5-specific protease inhibitor","volume":"04","author":"U Meyer-Hoffert","year":"2009","journal-title":"PLoS ONE"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1038\/jid.2008.448","article-title":"SPINK9: A Selective, Skin-Specific Kazal-Type Serine Protease Inhibitor","volume":"129","author":"M Brattsand","year":"2009","journal-title":"J Invest Dermatol"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1515\/hsz-2011-0238","article-title":"Characterisation of SPINK9, a KLK5-specific inhibitor expressed in palmo-plantar epidermis","volume":"393","author":"K Brannstrom","year":"2012","journal-title":"Biol Chem"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1111\/j.1600-0625.2011.01355.x","article-title":"Expression and regulation of murine SPINK12, a potential orthologue of human LEKTI2","volume":"20","author":"K Reiss","year":"2011","journal-title":"Exp Dermatol"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"32174","DOI":"10.1074\/jbc.M109.091850","article-title":"Isolation of SPINK6 in human skin: selective inhibitor of kallikrein-related peptidases","volume":"285","author":"U Meyer-Hoffert","year":"2010","journal-title":"J Biol Chem"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1016\/j.peptides.2011.03.009","article-title":"Inhibition of Kallikrein-related Peptidases by the Serine Protease Inhibitor of Kazal-type 6","volume":"32","author":"T Kantyka","year":"2011","journal-title":"Peptides"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.pep.2011.12.004","article-title":"Expression, purification and characterisation of recombinant human serine proteinase inhibitor Kazal-type 6 (SPINK6) in Pichia pastoris","volume":"82","author":"H Lu","year":"2012","journal-title":"Protein Expr Purif"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"4289","DOI":"10.1021\/pr1003467","article-title":"New role for LEKTI in skin barrier formation: label-free quantitative proteomic identification of caspase 14 as a novel target for the protease inhibitor LEKTI","volume":"09","author":"K Bennett","year":"2010","journal-title":"J Proteome Res"},{"key":"ref73","doi-asserted-by":"crossref","DOI":"10.1038\/jid.2012.482","volume-title":"Cross-Linking of SPINK6 by Transglutaminases Protects from Epidermal Proteases","author":"J Fischer","year":"2013"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1136\/gut.50.5.687","article-title":"Mutations in serine protease inhibitor Kazal type 1 are strongly associated with chronic pancreatitis","volume":"50","author":"JP Drenth","year":"2002","journal-title":"Gut"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1042\/bj3400569","article-title":"The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core","volume":"340","author":"J Schalkwijk","year":"1999","journal-title":"Biochem J"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1172\/JCI41440","article-title":"Elastase 2 is expressed in human and mouse epidermis and impairs skin barrier function in Netherton syndrome through filaggrin and lipid misprocessing","volume":"120","author":"C Bonnart","year":"2010","journal-title":"J Clin Invest"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"21886","DOI":"10.1074\/jbc.271.36.21886","article-title":"Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation","volume":"271","author":"CW Franzke","year":"1996","journal-title":"J Biol Chem"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"12209","DOI":"10.1074\/jbc.272.18.12209","article-title":"Characterisation of placental bikunin, a novel human serine protease inhibitor","volume":"272","author":"KA Delaria","year":"1997","journal-title":"J Biol Chem"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"5060","DOI":"10.2741\/2448","article-title":"Matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis","volume":"12","author":"TH Bugge","year":"2007","journal-title":"Front Biosci"},{"key":"ref80","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1111\/j.1742-4658.2008.06265.x","article-title":"Activation of hepatocyte growth factor activator zymogen (pro-HGFA) by human kallikrein 1-related peptidases","volume":"275","author":"S Mukai","year":"2008","journal-title":"Febs J"},{"key":"ref81","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1515\/bc.2010.037","article-title":"Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia","volume":"391","author":"JE Swedberg","year":"2010","journal-title":"Biol Chem"}],"container-title":["Thrombosis and Haemostasis"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.thieme-connect.de\/products\/ejournals\/pdf\/10.1160\/TH12-11-0836.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,31]],"date-time":"2023-05-31T11:55:52Z","timestamp":1685534152000},"score":1,"resource":{"primary":{"URL":"http:\/\/www.thieme-connect.de\/DOI\/DOI?10.1160\/TH12-11-0836"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013]]},"references-count":81,"journal-issue":{"issue":"09","published-online":{"date-parts":[[2017,11,29]]},"published-print":{"date-parts":[[2013]]}},"URL":"https:\/\/doi.org\/10.1160\/th12-11-0836","archive":["Portico","CLOCKSS"],"relation":{},"ISSN":["0340-6245","2567-689X"],"issn-type":[{"value":"0340-6245","type":"print"},{"value":"2567-689X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013]]}}}