The spatiotemporal control of human matriptase action on its physiological substrates: a case against a direct role for matriptase proteolytic activity in profilaggrin processing and desquamation-Reference-Cited by-同舟云学术

The spatiotemporal control of human matriptase action on its physiological substrates: a case against a direct role for matriptase proteolytic activity in profilaggrin processing and desquamation

Published:2020-04-18 Issue:3 Volume:33 Page:459-469
ISSN:1749-0774
Container-title:Human Cell
language:en
Short-container-title:Human Cell

Author:

Lin Chen-Yong^ORCID,Wang Jehng-Kang,Johnson Michael D.

Funder

National Cancer Institute

Ministry of National Defense Medical Affair Bureau, Taiwan

Chi Mei Medical Center

Publisher

Springer Science and Business Media LLC

Subject

Cancer Research,Cell Biology

Link

https://link.springer.com/content/pdf/10.1007/s13577-020-00361-7.pdf

Reference57 articles.

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2. List K, Szabo R, Molinolo A, Sriuranpong V, Redeye V, Murdock T, Burke B, Nielsen BS, Gutkind JS, Bugge TH. Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation. Genes Dev. 2005;19:1934–50.

3. Kim MG, Chen C, Lyu MS, Cho EG, Park D, Kozak C, Schwartz RH. Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains. Immunogenetics. 1999;49:420–8.

4. Lin CY, Anders J, Johnson M, Sang QA, Dickson RB. Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. J Biol Chem. 1999;274:18231–6.

5. Takeuchi T, Shuman MA, Craik CS. Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. Proc Natl Acad Sci USA. 1999;96:11054–61.

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