Fibulins: Multiple roles in matrix structures and tissue functions

被引：221

作者：

de Vega, S. ^{[1
]}

Iwamoto, T. ^{[1
,2
]}

Yamada, Y. ^{[1
]}

机构：

[1] Natl Inst Dent & Craniofacial Res, Lab Cell & Dev Biol, NIH, DHHS, Bethesda, MD 20892 USA

[2] Kyushu Univ, Sch Dent, Dept Pediat Dent, Fukuoka 8128582, Japan

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2009年 / 66卷 / 11-12期

基金：

美国国家卫生研究院;

关键词：

Fibulins; protein interactions; extracellular matrix network; embryonic development; elastogenesis; angiogenesis; genetic disorders; GROWTH-FACTOR-BETA; CONTROLS CELL-MIGRATION; ELASTIC FIBER FORMATION; RECESSIVE CUTIS LAXA; EXTRACELLULAR-MATRIX; MACULAR DEGENERATION; BREAST-CANCER; C-ELEGANS; IN-VIVO; CAENORHABDITIS-ELEGANS;

D O I：

10.1007/s00018-009-8632-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The fibulins are a family of secreted glycoproteins associated with basement membranes, elastic fibers, and other matrices. They are expressed in a variety of tissues. Association with these matrix structures is mediated by their ability to interact with many extracellular matrix constituents. The seven members of the family are defined by the presence of two structural modules, a tandem repeat of epidermal growth factor-like modules and a unique C-terminal fibulin-type module. They act not only as intermolecular bridges within the extracellular matrix to form supramolecular structures, but also as mediators for cellular processes and tissue remodeling. These important functions of fibulins in a wide range of biological processes have been shown in in vitro systems, gene knockout mice, and human genetic disorders. In this review, we describe the structure and function of these proteins and discuss the implication of fibulins in development and diseases.

引用

页码：1890 / 1902

页数：13

共 105 条

[1] Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules [J].

Adam, S ;

Gohring, W ;

Wiedemann, H ;

Chu, ML ;

Timpl, R ;

Kostka, G .

JOURNAL OF MOLECULAR BIOLOGY, 1997, 272 (02) :226-236

[2] Fibulin-5 antagonizes vascular endothelial growth factor (VEGF) signaling and angiogenic sprouting by endothelial cells [J].

Albig, AR ;

Schiemann, WP .

DNA AND CELL BIOLOGY, 2004, 23 (06) :367-379

[3] Fibulins: physiological and disease perspectives [J].

Argraves, WS ;

Greene, LM ;

Cooley, MA ;

Gallagher, WM .

EMBO REPORTS, 2003, 4 (12) :1127-1131

[4] FIBULIN IS AN EXTRACELLULAR-MATRIX AND PLASMA GLYCOPROTEIN WITH REPEATED DOMAIN-STRUCTURE [J].

ARGRAVES, WS ;

TRAN, H ;

BURGESS, WH ;

DICKERSON, K .

JOURNAL OF CELL BIOLOGY, 1990, 111 (06) :3155-3164

[5] FIBULIN, A NOVEL PROTEIN THAT INTERACTS WITH THE FIBRONECTIN RECEPTOR-BETA SUBUNIT CYTOPLASMIC DOMAIN [J].

ARGRAVES, WS ;

DICKERSON, K ;

BURGESS, WH ;

RUOSLAHTI, E .

CELL, 1989, 58 (04) :623-629

[6] Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican [J].

Aspberg, A ;

Adam, S ;

Kostka, G ;

Timpl, R ;

Heinegård, D .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (29) :20444-20449

[7]

BALBONA K, 1992, J BIOL CHEM, V267, P20120

[8] Identification of chicken and C-elegans fibulin-1 homologs and characterization of the C-elegans fibulin-1 gene [J].

Barth, JL ;

Argraves, KM ;

Roark, EF ;

Little, CD ;

Argraves, WS .

MATRIX BIOLOGY, 1998, 17 (8-9) :635-646

[9] Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans [J].

Blelloch, R ;

Kimble, J .

NATURE, 1999, 399 (6736) :586-590

[10] Latent transforming growth factor β-binding protein-3 and fibulin-1C interact with the extracellular domain of the heparin-binding EGF-like growth factor precursor -: art. no. 2 [J].

Brooke, JS ;

Cha, JH ;

Eidels, L .

BMC CELL BIOLOGY, 2002, 3 (1)

← 1 2 3 4 5 6 7 8 9 10 →