The Interaction of Fibulin-1 with Fibrinogen

Tran, Hoanh; Tanaka, Asashi; Litvinovich, Sergei V.; Medved, Leonid; Haudenschild, C C; Argraves, W. Scott

doi:10.1074/jbc.270.33.19458

Cited by 85 publications

(33 citation statements)

References 34 publications

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“…In fact, inflammatory vascular pathologies such as atherosclerosis showed high levels of ADAMTS-1 and fibulin-1 (45,46). Thus, fibulin-1 could play an important role in the degradation of proteoglycans by ADAMTS-1 during pathological conditions induced by inflammatory processes.…”

Section: Discussionmentioning

confidence: 99%

Fibulin-1 Acts as a Cofactor for the Matrix Metalloprotease ADAMTS-1

Lee

Rodrı́guez-Manzaneque

Thai

et al. 2005

Journal of Biological Chemistry

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ADAMTS-1 is a metalloprotease that has been implicated in the inhibition of angiogenesis and is a mediator of proteolytic cleavage of the hyaluronan binding proteoglycans, aggrecan and versican. In an attempt to further understand the biological function of ADAMTS-1, a yeast two-hybrid screen was performed using the carboxyl-terminal region of ADAMTS-1 as bait. As a result, the extracellular matrix protein fibulin-1 was identified as a potential interacting molecule. Through a series of analyses that included ligand affinity chromatography, co-immunoprecipitation, pulldown assays, and enzyme-linked immunosorbent assay, the ability of these two proteins to interact was substantiated. Additional studies showed that ADAMTS-1 and fibulin-1 colocalized in vivo. Furthermore, fibulin-1 was found to enhance the capacity of ADAMTS-1 to cleave aggrecan, a proteoglycan known to bind to fibulin-1. We confirmed that fibulin-1 was not a proteolytic substrate for ADAMTS-1. Together, these findings indicate that fibulin-1 is a new regulator of ADAMTS-1-mediated proteoglycan proteolysis and thus may play an important role in proteoglycan turnover in tissues where there is overlapping expression.Proteolytic events within the extracellular matrix (ECM) 3 are essential for developmental morphogenesis, homeostasis of adult tissues, and pathological conditions such as wound healing and tumor angiogenesis (1-3). ADAMTS-1 (a disintegrin-like and metalloprotease with thrombospondin type 1 motifs) belongs to a family of metalloproteases involved in the processing of ECM proteins such as procollagen types I and II (4, 5), von Willebrand factor (6 -8), and proteoglycans, including aggrecan, versican, and brevican (9 -12).A large percentage of mice that lack ADAMTS-1 die perinatally (45%), and those that survive display urinary track obstructions and kidney pathologies (13,14). In addition, most ADAMTS-1 null females are infertile because of abnormalities in the ovaries and endometrium (13). Evaluation of secondary follicles in the ovaries of ADAMTS-1 null mice revealed poor cumulus expansion and defective ovulation. These anomalies were attributed to incomplete versican proteolysis (15).Thus, a concrete understanding of the array of ADAMTS-1 biological functions will likely rely on insights from its substrates and regulation of catalytic function.The fibulins are a family of secreted glycoproteins that are components of elastic matrix fibers and basement membranes. Currently, there are six members of the fibulin family (16). The prototypic member, fibulin-1, contains the signature structural features of all fibulin family members, a series of epidermal growth factor-like repeats followed by a fibulin-type module at its carboxyl terminus (16).Functionally, fibulin-1 binds to many ECM proteins, including laminin, fibrinogen, fibronectin, nidogen-1, and endostatin, and to the proteoglycans, aggrecan and versican (17-22). Mice lacking fibulin-1 die perinatally and display vascular anomalies in the kidney in addition to extensive hemorrhage i...

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Section: Discussionmentioning

confidence: 99%

Fibulin-1 Acts as a Cofactor for the Matrix Metalloprotease ADAMTS-1

Lee

Rodrı́guez-Manzaneque

Thai

et al. 2005

Journal of Biological Chemistry

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“…The ability of fibulin-1 to associate with matrix structures such as elastic fibers or basement membranes, perhaps through its ability to interact with extracellular matrix proteins such as fibronectin (19), laminin, and nidogen (23), may act to modulate the formation, stabilization, and function of such structures and consequently to facilitate locoregional invasion by cancer cells. In addition, fibulin-1 may also promote tumor cell extravasation at the distance of the metastatic embolus, since it has recently been shown to increase platelet adhesion by interacting with fibrinogen (24).…”

Section: Discussionmentioning

confidence: 99%

Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells.

Clinton

Rougeot

Derancourt

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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Ovarian cancers have a high ability to invade the peritoneal cavity and some are stimulated by estrogens. In an attempt to understand the mode of action of estrogens on these cancer cells and to develop new markers, we have characterized estrogen-regulated proteins. This study was aimed at identifying a protein secreted by ovarian cancer cells whose level was increased by estradiol [Galtier-Dereure,

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“…In testing this hypothesis, we measured changes in luciferase expression driven by a synthetic AP-1 promoter ((TGAC-TAA) 7 ). Although FBLN-5 expression failed to affect basal AP-1 activity in Mv1Lu cells, its expression in combination with TGF-␤ treatment did synergistically stimulate AP-1 activity as compared with control cells stimulated solely with TGF-␤ (Fig.…”

Section: Fbln-5 Stimulates Mv1lumentioning

confidence: 99%

Context-specific Effects of Fibulin-5 (DANCE/EVEC) on Cell Proliferation, Motility, and Invasion

Schiemann¹,

Blobe²,

Kalume³

et al. 2002

Journal of Biological Chemistry

144

100

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The Fibulin gene family comprises five distinct genes that encode more than eight protein products via alternative splicing. Fibulins are widely expressed secretory proteins found in the blood and in the basement membranes and stroma of most tissues, where they self-associate (e.g. Fibulins 1 and 2) (1, 2) and/or interact with a variety of extracellular matrix components, including fibronectin, laminin, nidogen, aggrecan, versican, endostatin, and elastin (3-5). Thus, Fibulins likely participate in the assembly and stabilization of extracellular matrix structures; they also have been implicated in regulating organogenesis, vasculogenesis, fibrogenesis, and tumorigenesis (6 -8). Although the molecular mechanisms underlying the various biological activities of Fibulins remain to be elucidated, recent work suggests that Fibulins may interact directly with cell surface receptors, raising the possibility that these secretory proteins also function in mediating cell-cell and cell-matrix communication.The newest member of the Fibulin family is Fibulin-5 (FBLN-5; also known as EVEC (9) or DANCE (10)), 1 a 448-amino acid glycoprotein with interesting structural features; it contains an integrin-binding RGD motif, six calcium-binding epidermal growth factor-like repeats, a Pro-rich insert in the first calcium-binding epidermal growth factor-like repeat, and a globular C-terminal domain (9, 10). Functionally, FBLN-5 binds ␣ v ␤ 3 , ␣ v ␤ 5 , and ␣ 9 ␤ 1 integrins (4) and mediates endothelial cell adhesion via its RGD motif (10). In response to mechanical injury, FBLN-5 expression is induced dramatically in vascular endothelial and smooth muscle cells (9, 10), suggesting that FBLN-5 regulates vasculogenesis and endothelial cell function. Inactivation of the FBLN-5 gene in mice produces profound elastinopathy in the skin, lung, and vasculature (4, 5), demonstrating its importance in scaffolding cells to elastic fibers.Despite these recent advances, many questions regarding the role of FBLN-5 in mammalian biology remain to be answered, particularly (i) what are the signaling systems/molecules that regulate (ii) what are the effects of FBLN-5 on cell proliferation, migration, and invasion, and (iii) what are the signaling systems/molecules stimulated by FBLN-5. Through the use of expression proteomics, we show here that FBLN-5 is a novel TGF-␤-inducible protein that

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The Interaction of Fibulin-1 with Fibrinogen

Cited by 85 publications

References 34 publications

Fibulin-1 Acts as a Cofactor for the Matrix Metalloprotease ADAMTS-1

Fibulin-1 Acts as a Cofactor for the Matrix Metalloprotease ADAMTS-1

Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells.

Context-specific Effects of Fibulin-5 (DANCE/EVEC) on Cell Proliferation, Motility, and Invasion

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