JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Steffensen, B.
Right arrow Articles by Overall, C. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Steffensen, B.
Right arrow Articles by Overall, C. M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 273, Issue 32, 20622-20628, August 7, 1998

The Involvement of the Fibronectin Type II-like Modules of Human Gelatinase A in Cell Surface Localization and Activation

Bjorn Steffensen, Heather F. Bigg, and Christopher M. Overall

From the Faculty of Dentistry and Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada

Recombinant collagen-binding domain (rCBD) comprising the three fibronectin type II-like modules of human gelatinase A was found to compete the zymogen form of this matrix metalloproteinase from the cell surface of normal human fibroblasts in culture. Upon concanavalin A treatment of cells, the induced cellular activation of gelatinase A was markedly elevated in the presence of the rCBD. Therefore, the mechanistic aspects of gelatinase A binding to cells by this domain were further studied using cell attachment assays. Fibroblasts attached to rCBD-coated microplate wells in a manner that was inhibited by soluble rCBD, blocking antibodies to the beta 1-integrin subunit but not the alpha 2-integrin subunit, and bacterial collagenase treatment. Addition of soluble collagen rescued the attachment of collagenase-treated cells to the rCBD. As a probe on ligand blots of octyl-beta -D-thioglucopyranoside-solubilized cell membrane extracts, the rCBD bound 140- and 160-kDa protein bands. Their identities were likely procollagen chains being both bacterial collagenase-sensitive and also converted upon pepsin digestion to 112- and 126-kDa bands that co-migrated with collagen alpha 1(I) and alpha 2(I) chains. A rCBD mutant protein (Lys263 right-arrow Ala) with reduced collagen affinity showed less cell attachment, whereas a heparin-binding deficient mutant (Lys357 right-arrow Ala), heparinase treatment, or heparin addition did not alter attachment. Thus, a cell-binding mechanism for gelatinase A is revealed that does not involve the hemopexin COOH domain. Instead, an attachment complex comprising gelatinase A-native type I collagen-beta 1-integrin forms as a result of interactions involving the collagen-binding domain of the enzyme. Moreover, this distinct pool of cell collagen-bound proenzyme appears recalcitrant to cellular activation.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
A. Doucet, G. S. Butler, D. Rodriguez, A. Prudova, and C. M. Overall
Metadegradomics: Toward in Vivo Quantitative Degradomics of Proteolytic Post-translational Modifications of the Cancer Proteome
Mol. Cell. Proteomics, October 1, 2008; 7(10): 1925 - 1951.
[Abstract] [Full Text] [PDF]

Home page
 INT J LOW EXTREM WOUNDSHome page
M. S. Agren and M. Werthen
The Extracellular Matrix in Wound Healing: A Closer Look at Therapeutics for Chronic Wounds
International Journal of Lower Extremity Wounds, June 1, 2007; 6(2): 82 - 97.
[Abstract] [PDF]

Home page
 Clin. Cancer Res.Home page
Y. He, X.-d. Liu, Z.-y. Chen, J. Zhu, Y. Xiong, K. Li, J.-h. Dong, and X. Li
Interaction between Cancer Cells and Stromal Fibroblasts Is Required for Activation of the uPAR-uPA-MMP-2 Cascade in Pancreatic Cancer Metastasis
Clin. Cancer Res., June 1, 2007; 13(11): 3115 - 3124.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. J. Morrison and C. M. Overall
TIMP Independence of Matrix Metalloproteinase (MMP)-2 Activation by Membrane Type 2 (MT2)-MMP Is Determined by Contributions of Both the MT2-MMP Catalytic and Hemopexin C Domains
J. Biol. Chem., September 8, 2006; 281(36): 26528 - 26539.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
M. Stefanidakis and E. Koivunen
Cell-surface association between matrix metalloproteinases and integrins: role of the complexes in leukocyte migration and cancer progression
Blood, September 1, 2006; 108(5): 1441 - 1450.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
R. E. Nisato, G. Hosseini, C. Sirrenberg, G. S. Butler, T. Crabbe, A. J.P. Docherty, M. Wiesner, G. Murphy, C. M. Overall, S. L. Goodman, et al.
Dissecting the Role of Matrix Metalloproteinases (MMP) and Integrin {alpha}v{beta}3 in Angiogenesis In vitro: Absence of Hemopexin C Domain Bioactivity, but Membrane-Type 1-MMP and {alpha}v{beta}3 Are Critical
Cancer Res., October 15, 2005; 65(20): 9377 - 9387.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
X. Xu, Y. Wang, Z. Chen, M. D. Sternlicht, M. Hidalgo, and B. Steffensen
Matrix Metalloproteinase-2 Contributes to Cancer Cell Migration on Collagen
Cancer Res., January 1, 2005; 65(1): 130 - 136.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
E. Mira, R. A. Lacalle, J. M. Buesa, G. G. de Buitrago, S. Jimenez-Baranda, C. Gomez-Mouton, C. Martinez-A, and S. Manes
Secreted MMP9 promotes angiogenesis more efficiently than constitutive active MMP9 bound to the tumor cell surface
J. Cell Sci., May 1, 2004; 117(9): 1847 - 1857.
[Abstract] [Full Text] [PDF]

Home page
 J AndrolHome page
M. J. Wilson, A. Jiang, C. Wiehr, X. Wang, A. A. Sinha, and D. Pei
Limited Processing of Pro-Matrix Metalloprotease-2 (Gelatinase A) Overexpressed by Transfection in PC-3 Human Prostate Tumor Cells: Association With Restricted Cell Surface Localization of Membrane-Type Matrix Metalloproteinase-1
J Androl, March 1, 2004; 25(2): 274 - 285.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. M. Tam, Y. I. Wu, G. S. Butler, M. S. Stack, and C. M. Overall
Collagen Binding Properties of the Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Hemopexin C Domain. THE ECTODOMAIN OF THE 44-kDa AUTOCATALYTIC PRODUCT OF MT1-MMP INHIBITS CELL INVASION BY DISRUPTING NATIVE TYPE I COLLAGEN CLEAVAGE
J. Biol. Chem., October 4, 2002; 277(41): 39005 - 39014.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Hirohata, L. W. Wang, M. Miyagi, L. Yan, M. F. Seldin, D. R. Keene, J. W. Crabb, and S. S. Apte
Punctin, a Novel ADAMTS-like Molecule, ADAMTSL-1, in Extracellular Matrix
J. Biol. Chem., March 29, 2002; 277(14): 12182 - 12189.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
S. Saad, D. J. Gottlieb, K. F. Bradstock, C. M. Overall, and L. J. Bendall
Cancer Cell-associated Fibronectin Induces Release of Matrix Metalloproteinase-2 from Normal Fibroblasts
Cancer Res., January 1, 2002; 62(1): 283 - 289.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
L. L.L. Robinson, N. A. Sznajder, S. C. Riley, and R. A. Anderson
Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human fetal testis and ovary
Mol. Hum. Reprod., July 1, 2001; 7(7): 641 - 648.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
J. M. B. Bradley, M. J. Kelley, X. Zhu, A. M. Anderssohn, J. P. Alexander, and T. S. Acott
Effects of Mechanical Stretching on Trabecular Matrix Metalloproteinases
Invest. Ophthalmol. Vis. Sci., June 1, 2001; 42(7): 1505 - 1513.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
S. Hernandez-Barrantes, M. Toth, M. M. Bernardo, M. Yurkova, D. C. Gervasi, Y. Raz, Q. A. Sang, and R. Fridman
Binding of Active (57 kDa) Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) to Tissue Inhibitor of Metalloproteinase (TIMP)-2 Regulates MT1-MMP Processing and Pro-MMP-2 Activation
J. Biol. Chem., April 14, 2000; 275(16): 12080 - 12089.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. M. Overall, A. E. King, D. K. Sam, A. D. Ong, T. T. Y. Lau, U. M. Wallon, Y. A. DeClerck, and J. Atherstone
Identification of the Tissue Inhibitor of Metalloproteinases-2 (TIMP-2) Binding Site on the Hemopexin Carboxyl Domain of Human Gelatinase A by Site-directed Mutagenesis. THE HIERARCHICAL ROLE IN BINDING TIMP-2 OF THE UNIQUE CATIONIC CLUSTERS OF HEMOPEXIN MODULES III AND IV
J. Biol. Chem., February 12, 1999; 274(7): 4421 - 4429.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Li, L. H. Chow, and J. G. Pickering
Cell Surface-bound Collagenase-1 and Focal Substrate Degradation Stimulate the Rear Release of Motile Vascular Smooth Muscle Cells
J. Biol. Chem., November 3, 2000; 275(45): 35384 - 35392.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. M. Ellerbroek, Y. I. Wu, C. M. Overall, and M. S. Stack
Functional Interplay between Type I Collagen and Cell Surface Matrix Metalloproteinase Activity
J. Biol. Chem., June 29, 2001; 276(27): 24833 - 24842.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. M. Overall, E. Tam, G. A. McQuibban, C. Morrison, U. M. Wallon, H. F. Bigg, A. E. King, and C. R. Roberts
Domain Interactions in the Gelatinase A{middle dot}TIMP-2{middle dot}MT1-MMP Activation Complex. THE ECTODOMAIN OF THE 44-kDa FORM OF MEMBRANE TYPE-1 MATRIX METALLOPROTEINASE DOES NOT MODULATE GELATINASE A ACTIVATION
J. Biol. Chem., December 8, 2000; 275(50): 39497 - 39506.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. A. Hahn-Dantona, R. T. Aimes, and J. P. Quigley
The Isolation, Characterization, and Molecular Cloning of a 75-kDa Gelatinase B-like Enzyme, a Member of the Matrix Metalloproteinase (MMP) Family. AN AVIAN ENZYME THAT IS MMP-9-LIKE IN ITS CELL EXPRESSION PATTERN BUT DIVERGES FROM MAMMALIAN GELATINASE B IN SEQUENCE AND BIOCHEMICAL PROPERTIES
J. Biol. Chem., December 22, 2000; 275(52): 40827 - 40838.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhuge and J. Xu
Rac1 Mediates Type I Collagen-dependent MMP-2 Activation. ROLE IN CELL INVASION ACROSS COLLAGEN BARRIER
J. Biol. Chem., May 4, 2001; 276(19): 16248 - 16256.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Berton, V. Rigot, E. Huet, M. Decarme, Y. Eeckhout, L. Patthy, G. Godeau, W. Hornebeck, G. Bellon, and H. Emonard
Involvement of Fibronectin Type II Repeats in the Efficient Inhibition of Gelatinases A and B by Long-chain Unsaturated Fatty Acids
J. Biol. Chem., June 1, 2001; 276(23): 20458 - 20465.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Miyamori, T. Takino, Y. Kobayashi, H. Tokai, Y. Itoh, M. Seiki, and H. Sato
Claudin Promotes Activation of Pro-matrix Metalloproteinase-2 Mediated by Membrane-type Matrix Metalloproteinases
J. Biol. Chem., July 20, 2001; 276(30): 28204 - 28211.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.