Advertisement
JBC

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


     


Originally published In Press as doi:10.1074/jbc.M200988200 on June 28, 2002

J. Biol. Chem., Vol. 277, Issue 37, 33683-33689, September 13, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/37/33683    most recent
M200988200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Martin, J.
Right arrow Articles by Steadman, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martin, J.
Right arrow Articles by Steadman, R.
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?

The Role of ADAM 15 in Glomerular Mesangial Cell Migration*

John MartinDagger , Lisa V. Eynstone, Malcolm Davies, John D. Williams, and Robert Steadman

From the Institute of Nephrology, University of Wales College of Medicine, Heath Park, Cardiff, CF14 4XN, Wales, United Kingdom

Mesangial cells (MC) occupy the core of the renal glomerulus and are surrounded by a mesangial matrix. In certain diseases, MC migrate through this matrix into the pericapillary space. The mechanisms involved, however, are poorly understood. Members of the ADAM (A Disintegrin And Metalloproteinase) family of membrane proteins have the potential to be key modulators of cell-matrix interactions through the activities of their constituent domains. We have studied the possible role of ADAM 15 in human (H) MC migration in vitro. HMC ADAM 15 was expressed at low levels in serum-free medium but was increased during migration. Antibodies to the individual domains of ADAM 15 and the incorporation of antisense ADAM 15, (but not control oligonucleotide) inhibited this migration. Furthermore, inhibition of migration by the broad spectrum metalloproteinase inhibitor BB3103, demonstrated that metalloproteinase activity was essential for migration. ADAM 15, extracted from HMC membranes, was an active metalloproteinase, which degraded both type IV collagen and gelatin prepared from fibrillar collagen. Activity was inhibited by EDTA but not by phenylmethylsulfonyl fluoride. This is the first report of the potential of ADAM 15 for involvement in the restructuring of the mesangial matrix and in the migration of MC in disease.


* This work was supported by the National Kidney Research Fund and the Kidney Research Unit for Wales Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 44-029-2074-8446; Fax: 44-029-2074-8470; Email: martinj1@cf.ac.uk.


Copyright © 2002 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
J. Biol. Chem.Home page
T. Tousseyn, A. Thathiah, E. Jorissen, T. Raemaekers, U. Konietzko, K. Reiss, E. Maes, A. Snellinx, L. Serneels, O. Nyabi, et al.
ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the {gamma}-Secretase
J. Biol. Chem., April 24, 2009; 284(17): 11738 - 11747.
[Abstract] [Full Text] [PDF]


Home page
LupusHome page
A. Tveita, Y Ninomiya, Y Sado, O. Rekvig, and S. Zykova
Development of lupus nephritis is associated with qualitative changes in the glomerular collagen IV matrix composition
Lupus, April 1, 2009; 18(4): 355 - 360.
[Abstract] [PDF]


Home page
J. Biol. Chem.Home page
A. J. Najy, K. C. Day, and M. L. Day
The Ectodomain Shedding of E-cadherin by ADAM15 Supports ErbB Receptor Activation
J. Biol. Chem., June 27, 2008; 283(26): 18393 - 18401.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
D. D. Mruk, B. Silvestrini, and C. Y. Cheng
Anchoring Junctions As Drug Targets: Role in Contraceptive Development
Pharmacol. Rev., June 1, 2008; 60(2): 146 - 180.
[Abstract] [Full Text] [PDF]


Home page
FASEB J.Home page
L. Charrier-Hisamuddin, C. L. Laboisse, and D. Merlin
ADAM-15: a metalloprotease that mediates inflammation
FASEB J, March 1, 2008; 22(3): 641 - 653.
[Abstract] [Full Text] [PDF]


Home page
Mol Cancer ResHome page
J. L. Zhong, Z. Poghosyan, C. J. Pennington, X. Scott, M. M. Handsley, A. Warn, J. Gavrilovic, K. Honert, A. Kruger, P. N. Span, et al.
Distinct Functions of Natural ADAM-15 Cytoplasmic Domain Variants in Human Mammary Carcinoma
Mol. Cancer Res., March 1, 2008; 6(3): 383 - 394.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
A. J. Najy, K. C. Day, and M. L. Day
ADAM15 Supports Prostate Cancer Metastasis by Modulating Tumor Cell-Endothelial Cell Interaction
Cancer Res., February 15, 2008; 68(4): 1092 - 1099.
[Abstract] [Full Text] [PDF]


Home page
Nephrol Dial TransplantHome page
H.-A. Shui, T.-H. Huang, S.-M. Ka, P.-H. Chen, Y.-F. Lin, and A. Chen
Urinary proteome and potential biomarkers associated with serial pathogenesis steps of focal segmental glomerulosclerosis
Nephrol. Dial. Transplant., January 1, 2008; 23(1): 176 - 185.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Pathol.Home page
S. Kastner, G. J. Thomas, R. H. Jenkins, M. Davies, and R. Steadman
Hyaluronan Induces the Selective Accumulation of Matrix- and Cell-Associated Proteoglycans by Mesangial Cells
Am. J. Pathol., December 1, 2007; 171(6): 1811 - 1821.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Respir. Cell Mol. Bio.Home page
D. Lu, S. Xie, M. B. Sukkar, X. Lu, M. F. Scully, and K. F. Chung
Inhibition of Airway Smooth Muscle Adhesion and Migration by the Disintegrin Domain of ADAM-15
Am. J. Respir. Cell Mol. Biol., October 1, 2007; 37(4): 494 - 500.
[Abstract] [Full Text] [PDF]


Home page
Clin. Cancer Res.Home page
P. M. McGowan, B. M. Ryan, A. D.K. Hill, E. McDermott, N. O'Higgins, and M. J. Duffy
ADAM-17 Expression in Breast Cancer Correlates with Variables of Tumor Progression
Clin. Cancer Res., April 15, 2007; 13(8): 2335 - 2343.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Dyczynska, D. Sun, H. Yi, A. Sehara-Fujisawa, C. P. Blobel, and A. Zolkiewska
Proteolytic Processing of Delta-like 1 by ADAM Proteases
J. Biol. Chem., January 5, 2007; 282(1): 436 - 444.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
B. Rossi, M. Espeli, C. Schiff, and L. Gauthier
Clustering of Pre-B Cell Integrins Induces Galectin-1-Dependent Pre-B Cell Receptor Relocalization and Activation
J. Immunol., July 15, 2006; 177(2): 796 - 803.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
J. Huang, L. C. Bridges, and J. M. White
Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members
Mol. Biol. Cell, October 1, 2005; 16(10): 4982 - 4991.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
L. Charrier, Y. Yan, A. Driss, C. L. Laboisse, S. V. Sitaraman, and D. Merlin
ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers
Am J Physiol Gastrointest Liver Physiol, February 1, 2005; 288(2): G346 - G353.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Roy, U. M. Wewer, D. Zurakowski, S. E. Pories, and M. A. Moses
ADAM 12 Cleaves Extracellular Matrix Proteins and Correlates with Cancer Status and Stage
J. Biol. Chem., December 3, 2004; 279(49): 51323 - 51330.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Respir. Cell Mol. Bio.Home page
R. M. Powell, J. Wicks, J. W. Holloway, S. T. Holgate, and D. E. Davies
The Splicing and Fate of ADAM33 Transcripts in Primary Human Airways Fibroblasts
Am. J. Respir. Cell Mol. Biol., July 1, 2004; 31(1): 13 - 21.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
V. Trochon-Joseph, D. Martel-Renoir, L. M. Mir, A. Thomaidis, P. Opolon, E. Connault, H. Li, C. Grenet, F. Fauvel-Lafeve, J. Soria, et al.
Evidence of Antiangiogenic and Antimetastatic Activities of the Recombinant Disintegrin Domain of Metargidin
Cancer Res., March 15, 2004; 64(6): 2062 - 2069.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
K. Horiuchi, G. Weskamp, L. Lum, H.-P. Hammes, H. Cai, T. A. Brodie, T. Ludwig, R. Chiusaroli, R. Baron, K. T. Preissner, et al.
Potential Role for ADAM15 in Pathological Neovascularization in Mice
Mol. Cell. Biol., August 15, 2003; 23(16): 5614 - 5624.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. M. Fourie, F. Coles, V. Moreno, and L. Karlsson
Catalytic Activity of ADAM8, ADAM15, and MDC-L (ADAM28) on Synthetic Peptide Substrates and in Ectodomain Cleavage of CD23
J. Biol. Chem., August 15, 2003; 278(33): 30469 - 30477.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
T. Kuncewicz, E. A. Sheta, I. L. Goldknopf, and B. C. Kone
Proteomic Analysis of S-Nitrosylated Proteins in Mesangial Cells
Mol. Cell. Proteomics, March 1, 2003; 2(3): 156 - 163.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
D. F. Seals and S. A. Courtneidge
The ADAMs family of metalloproteases: multidomain proteins with multiple functions
Genes & Dev., January 1, 2003; 17(1): 7 - 30.
[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 © 2002 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement