The serine proteinase hepsin is an activator of pro-matrix metalloproteinases: molecular mechanisms and implications for extracellular matrix turnover
نویسندگان
چکیده
منابع مشابه
The Extracellular Matrix, Matrix Metalloproteinases and their roles in Disease
Biomedical research is often thought to primarily focus upon the trillions of cells that make up the body. However just as study of the immune system cannot ignore the lymph in favor of blood, the extracellular matrix (ECM) cannot be ignored in favor of the cells. The ECM is a dynamic structure that acts as scaffolding substrate for cell adhesion, as well as a reservoir of various proteins, gro...
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Hepsin, a type II transmembrane serine protease, is strongly up-regulated in prostate cancer. Hepsin overexpression in a mouse prostate cancer model resulted in tumor progression and metastasis, associated with basement membrane disorganization. We investigated whether hepsin enzymatic activity was linked to the basement membrane defects by examining its ability to initiate the plasminogen/plas...
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متن کاملdeterminant of the hankel matrix with binomial entries
abstract in this thesis at first we comput the determinant of hankel matrix with enteries a_k (x)=?_(m=0)^k??((2k+2-m)¦(k-m)) x^m ? by using a new operator, ? and by writing and solving differential equation of order two at points x=2 and x=-2 . also we show that this determinant under k-binomial transformation is invariant.
15 صفحه اولComplete primary structure of calcium-dependent serine proteinase capable of degrading extracellular matrix proteins.
A novel calcium-dependent serine proteinase (CASP) secreted from malignant hamster embryo fibroblast Ni 12C2 degrades extracellular matrix proteins. A complementary DNA encoding CASP has been isolated with the use of oligonucleotide probes synthesized based on partial amino acid sequences of CASP. The complete amino acid sequences of CASP revealed that it has a active site at the C-terminal sid...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2017
ISSN: 2045-2322
DOI: 10.1038/s41598-017-17028-3