Sequence of extracellular mouse protein BM‐90/fibulin and its calcium‐dependent binding to other basement‐membrane ligands

Pan, Te‐Cheng; Kluge, Matthias; Zhang, Ruizhu; Mayer, Ulríke; Timpl, Rupert; Chu, Mon‐Li

doi:10.1111/j.1432-1033.1993.tb18086.x

Cited by 102 publications

(115 citation statements)

References 41 publications

(45 reference statements)

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“…Fibulin-1 interacts with several adhesive and migration-promoting extracellular matrix proteins such as ®bronectin, laminin and nidogen (Pan et al, 1993;Balbona et al, 1992;Adam et al, 1997;Sasaki et al, 1995). The C-terminal region of ®bulin-1C has been shown to interact with NOVH, a cell di erentiation regulator in connective tissues (Perbal et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…We have recently shown that ®bulin-1 protein expression is increased in human ovarian epithelial cancers as compared to normal and benign tumors and that epithelial ovarian cells expressed ®bulin-1 mRNA in vivo . The ability of ®bulin-1 to bind extracellular matrix proteins such as ®bronectin and laminin and its localization at sites of epithelial mesenchymal transition suggest a role in cell attachment and motility (Hayashido et al, 1998;Pan et al, 1993;Balbona et al, 1992;Aspberg et al, 1999;Roark et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

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Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells

Katsaros²,

et al. 2002

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Fibulin-1 is an extracellular matrix protein induced by estradiol in estrogen receptor (ER) positive ovarian cancer cell lines. Alternative splicing of ®bulin-1 mRNA results in four di erent variants named A, B, C and D that may have distinct biological functions. We studied the relative expression of ®bulin-1 mRNA variants and their estrogen regulation in human ovarian cancer cells. In ovarian tissues and cancer cell lines, ®bulin-1C and -1D are the predominant forms, whereas ®bulin-1A and -1B are weakly expressed. We developed a competitive PCR assay based on coampli®cation of ®bulin-1C and -1D to study the relative expression of these ®bulin-1 variants in human ovarian samples. In ovarian cancer cell lines and ovarian cancer samples, there was a marked increase in the ®bulin-1C:1D and ®bulin-1C:HPRT mRNA ratios as compared to normal ovaries. In the BG1 estrogen receptor positive ovarian cancer cell line, ®bulin-1C mRNA was induced by estradiol in a dose-and time-dependent manner. Since others and we have previously shown an increased expression of ERa as compared to ERb in ovarian cancer cells, we investigated whether ERa or ERb is involved in this induction. For this aim, MDA-MB-231 breast cancer cell line, which expresses both low basal levels of ERs and ®bulin-1, was infected with recombinant ERa or ERb encoding adenovirus and treated with estradiol. Fibulin-1C was induced by estradiol in ERa-but not ERb-infected cells, suggesting that ®bulin-1C induction is mediated through ERa. In ovarian tumors, a trend towards a correlation between ®bulin-1C and ERa expression levels was noted. In conclusion, this study showed an increased ®bulin-1C: -1D mRNA ratio in ovarian cancer cells as compared to normal ovaries. This ®nding suggests that the C variant may be involved in ovarian carcinogenesis. Fibulin-1C overexpression may thus be a clue for the understanding of a putative role of estrogens in ERa promoted ovarian tumor progression.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells

Katsaros²,

et al. 2002

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“…Mammalian fibulin-1 binds to nidogen-1, laminin-1, and some proteoglycans (15,17,33). Mouse fibulin-1 also interacts weakly with type IV collagen (34). Therefore, LET-2 and FBL-1 may bind directly or indirectly through other ECM molecules to form a supramolecular network in the BM to support proper gonad morphogenesis.…”

Section: Nid-1-dependent and -Independent Pathways Downstream Of Mig-17mentioning

confidence: 99%

MIG-17/ADAMTS controls cell migration by recruiting nidogen to the basement membrane in C. elegans

Kubota¹,

Ohkura

Tamai

et al. 2008

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

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Mutations in the a disintegrin and metalloprotease with thrombospondin motifs (ADAMTS) family of secreted proteases cause diseases linked to ECM abnormalities. However, the mechanisms by which these enzymes modulate the ECM during development are mostly unexplored. The Caenorhabditis elegans MIG-17/AD-AMTS protein is secreted from body wall muscle cells and localizes to the basement membrane (BM) of the developing gonad where it controls directional migration of gonadal leader cells. Here we show that specific amino acid changes in the ECM proteins fibulin-1C (FBL-1C) and type IV collagen (LET-2) result in bypass of the requirement for MIG-17 activity in gonadal leader cell migration in a nidogen (NID-1)-dependent and -independent manner, respectively. The MIG-17, FBL-1C and LET-2 activities are required for proper accumulation of NID-1 at the gonadal BM. However, mutant FBL-1C or LET-2 in the absence of MIG-17 promotes NID-1 localization. Furthermore, overexpression of NID-1 in mig-17 mutants substantially rescues leader cell migration defects. These results suggest that functional interactions among BM molecules are important for MIG-17 control of gonadal leader cell migration. We propose that FBL-1C and LET-2 act downstream of MIG-17-dependent proteolysis to recruit NID-1 and that LET-2 also activates a NID-1-independent pathway, thereby inducing the remodeling of the BM required for directional control of leader cell migration.ECM ͉ fibulin-1 ͉ organogenesis ͉ type IV collagen T he interaction between basement membranes (BMs) and migrating cells or the epithelial layer is a complicated but carefully controlled process that involves remodeling of the ECM. For example, the migration of border cells required for oogenesis and patterning of the early embryo in Drosophila melanogaster is accompanied by precise regulation of the synthesis and degradation of type IV collagen, laminin, and perlecan (1, 2). Fibronectin expression is required for branching morphogenesis of the submandibular salivary gland, lung, and kidney in mouse (3). However, the mechanisms of cell-ECM interactions and the roles of BMs in cell migration remain largely unknown.Gonadogenesis in the nematode Caenorhabditis elegans serves as a simple model system for elucidating the function of BMs in organ morphogenesis. The development of hermaphrodite gonads is regulated by the migration of gonadal distal tip cells (DTCs), which promote directional elongation of the gonad arms during the larval stages to form the U-shaped gonads found in adult animals (4, 5). Two secreted a disintegrin and metalloprotease with thrombospondin motifs (ADAMTS) family metalloproteases, MIG-17 and GON-1, are involved in this process. GON-1 is required for DTC motility, whereas MIG-17 controls the direction of DTC movement but does not control DTC motility per se (6, 7). MIG-17 is expressed in the body wall muscles and is localized to the BM of the gonad surface, where it is required for DTC migration (7,8). It has been proposed that MIG-17 and GON-1 remodel BMs via prote...

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“…The fragments II8 -9ϩIII, II7-9ϩIII, and II6 -9ϩIII, were produced by amplifying the corresponding regions of the cDNA, nucleotides 1324, 1450, and 1570 to 2241, respectively, in the mouse fibulin-1 sequence (17). Primers were used in the polymerase chain reaction that introduced a NheI site immediately upstream, and an XbaI site immediately downstream of the fibulin-1 fragment.…”

Section: Construction Of Recombinant Lectin Domain Expression Plasmids-mentioning

confidence: 99%

Fibulin-1 Is a Ligand for the C-type Lectin Domains of Aggrecan and Versican

Aspberg

Adam

Kostka

et al. 1999

Journal of Biological Chemistry

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The aggregating proteoglycans (aggrecan, versican, neurocan, and brevican) are important components of many extracellular matrices. Their N-terminal globular domain binds to hyaluronan, but the function of their C-terminal region containing a C-type lectin domain is less clear. We now report that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican. Amino acid sequencing of tryptic peptides from this protein identified it as fibulin-1. This extracellular matrix glycoprotein is strongly expressed in tissues where versican is expressed (blood vessels, skin, and developing heart), and also expressed in developing cartilage and bone. It is thus likely to interact with these proteoglycans in vivo. Surface plasmon resonance measurements confirmed that aggrecan and versican lectin domains bind fibulin-1, whereas brevican and neurocan do not. As expected for a C-type lectin, the interactions with fibulin-1 are Ca 2؉ -dependent, with K D values in the low nanomolar range. Using various deletion mutants, the binding site for aggrecan and versican lectin domains was mapped to the epidermal growth factor-like repeats in domain II of fibulin-1. No difference in affinity was found for deglycosylated fibulin-1, indicating that the proteoglycan C-type lectin domains bind to the protein part of fibulin-1.The lectican family of large aggregating proteoglycans consists of versican, aggrecan, neurocan, and brevican (1). Their core proteins are organized with a central, extended, glycosaminoglycan-carrying part of variable length, flanked by globular domains (2-6). It has long been known that these proteoglycans are anchored to the hyaluronan meshwork through their N-terminal globular domains, in link protein-stabilized complexes (7-10). We have recently shown that the C-terminal globular domain also functions as a binding domain, in that it binds the brain-specific extracellular matrix protein tenascin-R (11, 12). Indeed, all these proteoglycans are expressed in the brain (1, 13). Although neurocan and brevican expression is restricted to the central nervous system, aggrecan is prominent in cartilage only (14), while versican is widely expressed in the extracellular matrix of many tissues, notably blood vessels and skin (15). Until now, no extra-neuronal ligand for the C-terminal globular domains of aggrecan and versican has been identified.We now report that the fibrillar extracellular matrix protein fibulin-1 is such a ligand. Fibulin-1 was previously shown to be an elongated protein which consists of three domains (I-III) with different molecular structures. The C-terminal domain III can be varied by splicing (variants A-D) and this was shown to affect its binding properties to nidogen-1 (16 -18). Here we show that fibulin-1 binds to the C-type lectin domains of versican and aggrecan with high affinity, but shows no binding to the brain-specific proteoglycans brevican and neurocan. We also map the binding site on the fibulin-1 molecule to th...

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Sequence of extracellular mouse protein BM‐90/fibulin and its calcium‐dependent binding to other basement‐membrane ligands

Cited by 102 publications

References 41 publications

Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells

Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells

MIG-17/ADAMTS controls cell migration by recruiting nidogen to the basement membrane in C. elegans

Fibulin-1 Is a Ligand for the C-type Lectin Domains of Aggrecan and Versican

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