JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on April 12, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/16/13650    most recent
M111361200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Santas, A. J.
Right arrow Articles by Peters, D. M. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Santas, A. J.
Right arrow Articles by Peters, D. M. P.
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?

Papers In Press, published online ahead of print February 6, 2002
J. Biol. Chem, 10.1074/jbc.M111361200
Submitted on November 28, 2001
Revised on January 23, 2002
Accepted on February 6, 2002

Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading

Amy J. Santas, Jennifer A. Peterson, Jennifer L. Halbleib, Sue E. Craig, Martin J. Humphries, and Donna M. Pesciotta Peters

Department of Pathology, University of Wisconsin, Madison, WI 53706

Corresponding Author: dmpeter2{at}facstaff.wisc.edu

The Heparin (Hep) II binding domain of fibronectin regulates the formation of focal adhesions and actin stress fibers and hence plays an important role in cell spreading, migration and fibronectin fibrillogenesis. Using human skin fibroblast cultures, we demonstrate that alternative splicing of the neighboring IIICS domain may regulate the activities of the Hep II domain in cell spreading and fibronectin fibrillogenesis. Recombinant Hep II domains, adjacent to either the IIICS domain or the H89 splice variant that contains the amino terminal sequence of the IIICS domain, blocked fibronectin fibrillogenesis and required sulfated proteoglycans to mediate cell spreading. If the Hep II domain was adjacent to either the HO or H95 splice variants, which both lack the amino terminus of the IIICS domain, fibrillogenesis was not inhibited and cell spreading was independent of a sulfated proteoglycan-mediated mechanism. The effect of the splice variants on the Hep II domain could be mimicked using a Hep II domain that contained only 6 amino acids from the III15 repeat or 10 amino acids from the IIICS domain suggesting that sequences proximal to the III14 repeat determined the role of the Hep II domain in these processes. We propose that alternative splicing of the IIICS domain modulates interactions between heparan sulfate proteoglycans and the Hep II domain and that this serves as a mechanism to control the biological activities of fibronectin.


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
 IOVSHome page
K. E. Keller, J. M. Bradley, M. J. Kelley, and T. S. Acott
Effects of Modifiers of Glycosaminoglycan Biosynthesis on Outflow Facility in Perfusion Culture
Invest. Ophthalmol. Vis. Sci., June 1, 2008; 49(6): 2495 - 2505.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
F. Castelletti, R. Donadelli, F. Banterla, F. Hildebrandt, P. F. Zipfel, E. Bresin, E. Otto, C. Skerka, A. Renieri, M. Todeschini, et al.
Mutations in FN1 cause glomerulopathy with fibronectin deposits
PNAS, February 19, 2008; 105(7): 2538 - 2543.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
M. S. Filla, A. Woods, P. L. Kaufman, and D. M. Peters
{beta}1 and {beta}3 Integrins Cooperate to Induce Syndecan-4-Containing Cross-linked Actin Networks in Human Trabecular Meshwork Cells
Invest. Ophthalmol. Vis. Sci., May 1, 2006; 47(5): 1956 - 1967.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
V. Vittal, A. Rose, K. E. Gregory, M. J. Kelley, and T. S. Acott
Changes in Gene Expression by Trabecular Meshwork Cells in Response to Mechanical Stretching
Invest. Ophthalmol. Vis. Sci., August 1, 2005; 46(8): 2857 - 2868.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. A. Peterson, N. Sheibani, G. David, A. Garcia-Pardo, and D. M. Peters
Heparin II Domain of Fibronectin Uses {alpha}4{beta}1 Integrin to Control Focal Adhesion and Stress Fiber Formation, Independent of Syndecan-4
J. Biol. Chem., February 25, 2005; 280(8): 6915 - 6922.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
A. J. Santas, C. Bahler, J. A. Peterson, M. S. Filla, P. L. Kaufman, E. R. Tamm, D. H. Johnson, and D. M. P. Peters
Effect of Heparin II Domain of Fibronectin on Aqueous Outflow in Cultured Anterior Segments of Human Eyes
Invest. Ophthalmol. Vis. Sci., November 1, 2003; 44(11): 4796 - 4804.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Gendelman, N. I. Burton-Wurster, J. N. MacLeod, and G. Lust
The Cartilage-specific Fibronectin Isoform Has a High Affinity Binding Site for the Small Proteoglycan Decorin
J. Biol. Chem., March 21, 2003; 278(13): 11175 - 11181.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.