HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 8, 6160-6167, February 21, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/8/6160    most recent M208322200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Spessotto, P. Articles by Colombatti, A. Search for Related Content PubMed PubMed Citation Articles by Spessotto, P. Articles by Colombatti, A. Social Bookmarking                      What's this?

₁ Integrin-dependent Cell Adhesion to EMILIN-1 Is Mediated by the gC1q Domain^*

Paola Spessotto, Marta Cervi^§, Maria Teresa Mucignat, Gabriella Mungiguerra, Ida Sartoretto, Roberto Doliana, and Alfonso Colombatti^¶**

From the  Divisione di Oncologia Sperimentale 2, Centro di Riferimento Oncologico, Aviano, the ^¶ Dipartimento di Scienze e Tecnologie Biomediche and the  Microgravity, Ageing, Training, and Immobility Center of Excellence, Università di Udine, Udine 35100, Italy

EMILIN-1 (Elastin Microfibril Interface Located ProteIN), the prototype of the EMILIN family, consists of a cysteine-rich domain (EMI domain) at the N terminus, an extended region with a high potential coiled-coil structure, a short collagenous stalk, and a self-interacting globular gC1q-l domain. EMILIN-1 is an adhesive extracellular matrix constituent associated with elastic fibers, detected also in the proximity of cell surfaces. To localize the cell attachment site(s), monoclonal antibodies (mAbs) against EMILIN-1 or the gC1q-1 domain were used to inhibit cell attachment to EMILIN-1. Thus, one mAb mapping to the gC1q-1 domain caused complete inhibition of cell attachment. EMILIN-1 and gC1q-1 displayed a comparable dose-dependent ability to promote cell adhesion. Adhesion kinetics was similar to that of fibronectin (FN), reaching the maximum level of attachment at 20 min, but in the absence of cations adhesion was negligible. The relative adhesion strength to detach 50% of the cells was similar for EMILIN-1 and gC1q-1 (250-270 × g) but lower than that for FN (500). Cell adhesion to EMILIN-1 or gC1q-1 was completely blocked by a function-blocking ₁ integrin subunit mAb. In contrast, adhesion to the complement C1q component was totally unaffected. Among the various function-blocking mAbs against the  integrin subunits only the anti-₄ fully abrogated cell adhesion to gC1q-1 and up to 70% to EMILIN-1. Furthermore, only K562 cells transfected with the ₄ integrin chain, but not wild type K562, were able to adhere to EMILIN-1 and were specifically inhibited by anti-₄ function-blocking mAb. Finally, cells attached to EMILIN-1 or gC1q-1, compared with cells plated on FN or vitronectin, which appeared well spread out on the substrate with prominent stress fibers and focal contacts, were much smaller with wide ruffles and a different organization status of the actin cytoskeleton along the cell periphery. This pattern was in accord with the ability of EMILIN-1 to promote cell movement.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				K. Fujarewicz, M. Jarzab, M. Eszlinger, K. Krohn, R. Paschke, M. Oczko-Wojciechowska, M. Wiench, A. Kukulska, B. Jarzab, and A. Swierniak A multi-gene approach to differentiate papillary thyroid carcinoma from benign lesions: gene selection using support vector machines with bootstrapping Endocr. Relat. Cancer, September 1, 2007; 14(3): 809 - 826. [Abstract] [Full Text] [PDF]

				P. Spessotto, R. Bulla, C. Danussi, O. Radillo, M. Cervi, G. Monami, F. Bossi, F. Tedesco, R. Doliana, and A. Colombatti EMILIN1 represents a major stromal element determining human trophoblast invasion of the uterine wall J. Cell Sci., November 1, 2006; 119(21): 4574 - 4584. [Abstract] [Full Text] [PDF]

				X. Shi-wen, L. A. Stanton, L. Kennedy, D. Pala, Y. Chen, S. L. Howat, E. A. Renzoni, D. E. Carter, G. Bou-Gharios, R. J. Stratton, et al. CCN2 Is Necessary for Adhesive Responses to Transforming Growth Factor-beta1 in Embryonic Fibroblasts J. Biol. Chem., April 21, 2006; 281(16): 10715 - 10726. [Abstract] [Full Text] [PDF]