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Molecular and Cellular Biology, February 2008, p. 1061-1067, Vol. 28, No. 3
0270-7306/08/$08.00+0     doi:10.1128/MCB.01876-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Fibulin-2 Is Dispensable for Mouse Development and Elastic Fiber Formation{triangledown}

Francois-Xavier Sicot ,1,{dagger},# Takeshi Tsuda,1,{ddagger},# Dessislava Markova,1,§ John F. Klement,1 Machiko Arita,1 Rui-Zhu Zhang,1 Te-Cheng Pan,1 Robert P. Mecham,2 David E. Birk,3 and Mon-Li Chu1,4*

Department of Dermatology and Cutaneous Biology,1 Department of Pathology, Anatomy and Cell Biology,3 Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107,4 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri2

Received 15 October 2007/ Returned for modification 29 October 2007/ Accepted 15 November 2007

Fibulin-2 is an extracellular matrix protein belonging to the five-member fibulin family, of which two members have been shown to play essential roles in elastic fiber formation during development. Fibulin-2 interacts with two major constituents of elastic fibers, tropoelastin and fibrillin-1, in vitro and localizes to elastic fibers in many tissues in vivo. The protein is prominently expressed during morphogenesis of the heart and aortic arch vessels and at early stages of cartilage development. To examine its role in vivo, we generated mice that do not express the fibulin-2 gene (Fbln2) through homologous recombination of embryonic stem cells. Unexpectedly, the fibulin-2-null mice were viable and fertile and did not display gross and anatomical abnormalities. Histological and ultrastructural analyses revealed that elastic fibers assembled normally in the absence of fibulin-2. No compensatory up-regulation of mRNAs for other fibulin members was detected in the aorta and skin tissue. However, in the fibulin-2 null aortae, fibulin-1 immunostaining was increased in the inner elastic lamina, where fibulin-2 preferentially localizes. The results demonstrate that fibulin-2 is not required for mouse development and elastic fiber formation and suggest possible functional redundancy between fibulin-1 and fibulin-2.

* Corresponding author. Mailing address: Department of Dermatology and Cutaneous Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107. Phone: (215) 503-4834. Fax: (215) 503-5788. E-mail: mon-li.chu{at}jefferson.edu

{triangledown} Published ahead of print on 10 December 2007.

{dagger} Present address: Takara Bio Europe S.A.S., 78100 Saint-Germain-en-Laye, France.

# F.-X. Sicot and T. Tsuda contributed equally to this work.

{ddagger} Present address: Nemours Biomedical Research and Nemours Cardiac Center, Alfred duPont Hospital for Children, Wilmington, DE 19803.

§ Present address: Department of Rehabilitation Medicine, Thomas Jefferson University, Philadelphia, PA 19107.

Molecular and Cellular Biology, February 2008, p. 1061-1067, Vol. 28, No. 3
0270-7306/08/$08.00+0     doi:10.1128/MCB.01876-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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