{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nST14, which encodes the type II transmembrane serine protease matriptase, plays a pivotal role in malignant transformation and tumor progression. In epithelial cancers, overexpression or dysregulated activation of matriptase—in the absence of sufficient endogenous inhibition by HAI-1 or HAI-2—drives oncogenic signaling by proteolytically activating key substrates such as pro–hepatocyte growth factor (pro‐HGF), PDGF‐D, pro–urokinase plasminogen activator (pro‐uPA), and MSP‐1. These proteolytic events trigger downstream pathways including PI3K–Akt and c‐Met signaling, promote extracellular matrix degradation, and facilitate cancer cell invasion and metastasis across breast, prostate, ovarian, and skin tumors. In addition, modifications such as beta1-6 GlcNAc branching and microRNA regulation (e.g., by miR-27b) further fine tune matriptase levels and activity, underscoring its potential as a prognostic biomarker and therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its tumor-promoting roles, matriptase is essential for normal epithelial development, homeostasis, and barrier function. In the skin and intestine, it orchestrates proteolytic cascades that process structural and signaling proteins—such as profilaggrin, corneodesmosomes, and the GPI-anchored protease prostasin—to ensure proper desquamation, hair follicle formation, and tight junction assembly. Mutations in ST14, including the recurrent G827R missense mutation, abrogate matriptase’s catalytic activity and are causative of congenital ichthyosis with hypotrichosis. Moreover, the precise regulation of matriptase activity by its inhibitors HAI-1 and HAI-2 is critical for maintaining epithelial integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMatriptase activation is finely tuned by a range of extrinsic and intrinsic stimuli that ensure its spatiotemporal activity. Its zymogen autoactivation is promoted through a transactivation mechanism that depends on intact noncatalytic domains, proper glycosylation, and the preservation of lipid bilayer microenvironments. External factors such as acidic pH, bioactive sphingolipids (notably sphingosine 1-phosphate), and cytoskeletal rearrangements induce rapid matriptase activation and localization at cell–cell contacts, thereby regulating its participation in both proteolytic cascades and cell signaling pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Shinji Ihara, Eiji Miyoshi, Jeong Heon Ko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M200673200"}], "href": "https://doi.org/10.1074/jbc.M200673200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11864986"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11864986"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Christelle M Benaud, Michael Oberst, Robert B Dickson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deregulated activation of matriptase in breast cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Exp Metastasis (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1023/a:1020985632550"}], "href": "https://doi.org/10.1023/a:1020985632550"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12498394"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12498394"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Michael D Oberst, Cicely A Williams, Robert B Dickson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M304282200"}], "href": "https://doi.org/10.1074/jbc.M304282200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12738778"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12738778"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Mika Suzuki, Hiroshi Kobayashi, Naohiro Kanayama, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M313130200"}], "href": "https://doi.org/10.1074/jbc.M313130200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14747469"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14747469"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Karin List, Roman Szabo, Alfredo Molinolo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes Dev (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1101/gad.1300705"}], "href": "https://doi.org/10.1101/gad.1300705"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16103220"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16103220"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Jong-Shiaw Jin, Dar-Shih Hsieh, Shih-Hurng Loh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mod Pathol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/modpathol.3800495"}], "href": "https://doi.org/10.1038/modpathol.3800495"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16439987"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16439987"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Lynette M Kilpatrick, Roger L Harris, Kate A Owen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2006-02-001073"}], "href": "https://doi.org/10.1182/blood-2006-02-001073"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16794252"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16794252"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "K Uhland "}, {"type": "b", "children": [{"type": "t", "text": "Matriptase and its putative role in cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Mol Life Sci (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00018-006-6298-x"}], "href": "https://doi.org/10.1007/s00018-006-6298-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17131055"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17131055"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Ami S Bhatt, Alana Welm, Christopher J Farady, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0606514104"}], "href": "https://doi.org/10.1073/pnas.0606514104"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17389401"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17389401"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Alana L Welm, Julie B Sneddon, Carmen Taylor, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The macrophage-stimulating protein pathway promotes metastasis in a mouse model for breast cancer and predicts poor prognosis in humans."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0702095104"}], "href": "https://doi.org/10.1073/pnas.0702095104"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17456594"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17456594"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Molly R Darragh, Ami S Bhatt, Charles S Craik "}, {"type": "b", "children": [{"type": "t", "text": "MT-SP1 proteolysis and regulation of cell-microenvironment interactions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Front Biosci (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2741/2698"}], "href": "https://doi.org/10.2741/2698"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17981566"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17981566"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "I-Chu Tseng, Feng-Pai Chou, Sheng-Feng Su, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Cell Physiol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpcell.00164.2008"}], "href": "https://doi.org/10.1152/ajpcell.00164.2008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18550704"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18550704"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Yanfang Wang, Rajamani Rathinam, Amelia Walch, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ST14 (suppression of tumorigenicity 14) gene is a target for miR-27b, and the inhibitory effect of ST14 on cell growth is independent of miR-27b regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.012617"}], "href": "https://doi.org/10.1074/jbc.M109.012617"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19546220"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19546220"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Kate A Owen, Deyi Qiu, Juliano Alves, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20091448"}], "href": "https://doi.org/10.1042/BJ20091448"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20015050"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20015050"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Carolyn V Ustach, Wei Huang, M Katie Conley-LaComb, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A novel signaling axis of matriptase/PDGF-D/ß-PDGFR in human prostate cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-10-0511"}], "href": "https://doi.org/10.1158/0008-5472.CAN-10-0511"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21098708"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21098708"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "R Szabo, A L Rasmussen, A B Moyer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2010.586"}], "href": "https://doi.org/10.1038/onc.2010.586"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21217780"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21217780"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Tai-Shan Cheng, Wen-Chi Chen, Ya-Yun Lin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Curcumin-targeting pericellular serine protease matriptase role in suppression of prostate cancer cell invasion, tumor growth, and metastasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Prev Res (Phila) (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1940-6207.CAPR-12-0293-T"}], "href": "https://doi.org/10.1158/1940-6207.CAPR-12-0293-T"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23466486"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23466486"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Jelani C Zarif, Laura E Lamb, Veronique V Schulz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Androgen receptor non-nuclear regulation of prostate cancer cell invasion mediated by Src and matriptase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.3119"}], "href": "https://doi.org/10.18632/oncotarget.3119"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25730905"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25730905"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Lina Basel-Vanagaite, Revital Attia, Akemi Ishida-Yamamoto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1086/512487"}], "href": "https://doi.org/10.1086/512487"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17273967"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17273967"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Karin List, Brooke Currie, Tiffany C Scharschmidt, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M705521200"}], "href": "https://doi.org/10.1074/jbc.M705521200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17940283"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17940283"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Thomas Alef, Serena Torres, Ingrid Hausser, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ichthyosis, follicular atrophoderma, and hypotrichosis caused by mutations in ST14 is associated with impaired profilaggrin processing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Invest Dermatol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/jid.2008.311"}], "href": "https://doi.org/10.1038/jid.2008.311"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18843291"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18843291"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Marguerite S Buzza, Sarah Netzel-Arnett, Terez Shea-Donohue, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Membrane-anchored serine protease matriptase regulates epithelial barrier formation and permeability in the intestine."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0903923107"}], "href": "https://doi.org/10.1073/pnas.0903923107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20142489"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20142489"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Cheng-Jueng Chen, Bai-Yao Wu, Pai-In Tsao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Increased matriptase zymogen activation in inflammatory skin disorders."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Cell Physiol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpcell.00403.2010"}], "href": "https://doi.org/10.1152/ajpcell.00403.2010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21123732"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21123732"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Stine Friis, Sine Godiksen, Jette Bornholdt, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.186874"}], "href": "https://doi.org/10.1074/jbc.M110.186874"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21148558"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21148558"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Stine Friis, Katiuchia Uzzun Sales, Sine Godiksen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M113.469932"}], "href": "https://doi.org/10.1074/jbc.M113.469932"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23673661"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23673661"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Christelle Benaud, Michael Oberst, John P Hobson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109064200"}], "href": "https://doi.org/10.1074/jbc.M109064200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11792696"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11792696"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Ruei-Jiun Hung, Ia-Wen J Hsu, Jennifer L Dreiling, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Cell Physiol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpcell.00400.2003"}], "href": "https://doi.org/10.1152/ajpcell.00400.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15075215"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15075215"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Ming-Shyue Lee, I-Chu Tseng, Youhong Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Autoactivation of matriptase in vitro: requirement for biomembrane and LDL receptor domain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Cell Physiol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpcell.00611.2006"}], "href": "https://doi.org/10.1152/ajpcell.00611.2006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17344310"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17344310"}]}]}]}