Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin

被引:27
作者
Jin, XL
Hirosaki, T
Lin, CY
Dickson, RB
Higashi, S
Kitamura, H
Miyazaki, K
机构
[1] Yokohama City Univ, Kihara Inst Biol Res, Div Cell Biol, Totsuka Ku, Yokohama, Kanagawa 2440813, Japan
[2] Yokohama City Univ, Sch Med, Dept Cellular Pathobiol, Kanazawa Ku, Yokohama, Kanagawa 2360008, Japan
[3] Georgetown Univ, Med Ctr, Lombardi Comprehens Canc Ctr, Washington, DC 20057 USA
关键词
serine proteinase; matriptase; trypsin; HAI-1; cancer;
D O I
10.1002/jcb.20418
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The membrane-bound serine proteinase matriptase, which is often released from the plasma membrane of epithelial and carcinoma cells, has been implicated to play important roles in both physiological and pathological conditions. However, the regulatory mechanism of its activity is poorly understood. In the present study, we examined expression and activation state of soluble matriptase in 24 human cancer cell lines. Soluble matriptase was detected in the conditioned media from all of 5 colon and 4 breast carcinoma cell lines and 8 of 10 stomach carcinoma cell lines tested. Only two of five lung cancer cell lines released the matriptase protein into the culture media. Out of the five matriptase-negative cell lines, two cell lines expressed the matriptase mRNA. Among 24 cancer cell lines tested, 13 cell lines secreted trypsin in an active or latent form and all of them released matriptase. Most of the 24 cell lines released a latent, single-chain matriptase of 75 kDa as a major form, as well as low levels of complex forms of an activated two-chain enzyme with its specific inhibitor HAI-1. Thus, these soluble matriptases appeared to have little proteolytic activity. Treatment of stomach and colon cancer cell lines with epidermal growth factor stimulated the release of matripatase/HAI-1 complexes. In cancercell lines secreting active trypsin, however, matriptase was released mostly as an inhibitor-free, two-chain active form. Trypsin seemed to activate the membrane-bound, latent matriptase on the cell surface. These results suggest that matriptase and trypsin cooperatively function for extracellular proteolysis. J. Cell. Biochem. 95: 632-647, 2005. (c) 2005 Wiley-Liss, Inc.
引用
收藏
页码:632 / 647
页数:16
相关论文
共 43 条
[1]   Endothelial cell serine proteases expressed during vascular morphogenesis and angiogenesis [J].
Aimes, RT ;
Zijlstra, A ;
Hooper, JD ;
Ogbourne, SM ;
Sit, ML ;
Fuchs, S ;
Gotley, DC ;
Quigley, JP ;
Antalis, TM .
THROMBOSIS AND HAEMOSTASIS, 2003, 89 (03) :561-572
[2]   Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase [J].
Benaud, C ;
Oberst, M ;
Hobson, JP ;
Spiegel, S ;
Dickson, RB ;
Lin, CY .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (12) :10539-10546
[3]   Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor [J].
Benaud, C ;
Dickson, RB ;
Lin, CY .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (05) :1439-1447
[4]   Deregulated activation of matriptase in breast cancer cells [J].
Benaud, CM ;
Oberst, M ;
Dickson, RB ;
Lin, CY .
CLINICAL & EXPERIMENTAL METASTASIS, 2002, 19 (07) :639-649
[5]  
BORDIER C, 1981, J BIOL CHEM, V256, P1604
[6]   Processing of integrin αv subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase [J].
Deryugina, EI ;
Ratnikov, BI ;
Postnova, TI ;
Rozanov, DV ;
Strongin, AY .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (12) :9749-9756
[7]   New functions for the matrix metalloproteinases in cancer progression [J].
Egeblad, M ;
Werb, Z .
NATURE REVIEWS CANCER, 2002, 2 (03) :161-174
[8]   Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration [J].
Endo, K ;
Takino, T ;
Miyamori, H ;
Kinsen, H ;
Yoshizaki, T ;
Furukawa, M ;
Sato, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (42) :40764-40770
[9]   Differential expression of trypsin in human ovarian carcinomas and low-malignant-potential tumors [J].
Hirahara, F ;
Miyagi, E ;
Nagashima, Y ;
Miyagi, Y ;
Yasumitsu, H ;
Koshikawa, N ;
Nakatani, Y ;
Nakazawa, T ;
Udagawa, K ;
Kitamura, H ;
Minaguchi, H ;
Miyazaki, K .
GYNECOLOGIC ONCOLOGY, 1998, 68 (02) :162-165
[10]  
Ichikawa Y, 2000, CLIN CANCER RES, V6, P1385