Cloning and regional localization of the mouse faciogenital dysplasia (Fgd1) gene

Pasteris, N. German; Gouyon, Béatrice; Cadle, A. B.; Campbell, Kathy; Herman, Gail E.; Gorski, Jerome L.

doi:10.1007/bf00352375

Cited by 15 publications

(12 citation statements)

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“…As shown in Figure 5A, the anti‐ Fgd1 antibody detected a protein migrating at 107 kDa in isolated primary mouse calvarial cells (PMC cells), a standard preparation for osteoblast cells (Majeska, 1996). The 107 kDa size of the detected protein coincided with the predicted size of the Fgd1 protein (Pasteris et al, 1995). Anti‐ Fgd1 antibody detected an identically sized 107 kDa protein in MC3T3‐E1 cells, a permanent non‐transformed osteoblast‐like cell line derived from normal mouse bone that retains the ability to form well‐developed bone matrix in culture (Sudo et al, 1983).…”

Section: Resultssupporting

confidence: 72%

“…Northern blot and non‐quantitative RT‐PCR studies were previously used to examine the pattern of FGD1 expression in a limited number of adult and embryonic human tissues (Pasteris et al, 1994, 1995); however, skeletal tissues were not included in these studies. Preliminary northern blot analyses showed that Fgd1 transcripts were predominantly expressed in mouse skeletal tissue (Pasteris et al, 1995; data not shown). Thus, to further elucidate the role of FGD1 in skeletal formation, additional studies were performed to determine a more precise spatiotemporal pattern of Fgd1 expression during mouse embryogenesis.…”

Section: Resultsmentioning

confidence: 99%

“…To gain further understanding of the function of FGD1 in skeletal formation, we studied the expression of Fgd1 , the FGD1 mouse ortholog (Pasteris et al, 1995), in the developing mouse embryo. Here we demonstrate that Fgd1 has a unique pattern of expression; transcripts are most abundant in the ossifying skeletal components of craniofacial bones, vertebrae, ribs, long bones and phalanges, skeletal components derived from neural crest, periaxial mesoderm, and lateral mesoderm.…”

Section: Introductionmentioning

confidence: 99%

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FTIR microspectroscopy study of composition fluctuations in extruded amylopectin–gelatin blends

et al. 2001

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The spatial variation in the composition of nonexpanded biopolymer blends prepared by extrusion of mixtures of gelatin with either native or pregelatinized waxy maize starch was studied using a 30-microm aperture FTIR microspectroscopy technique. The ratio of the areas of the "saccharide" bands (953-1180 cm(-1)) and the amide I and II bands (1483-1750 cm(-1)) was used to monitor the relative distributions of the two components of the blend. Two calibration methods were used to obtain amylopectin concentration values from the ratios of the IR bands. The results suggested a high degree of heterogeneity in these blends, despite the thorough mixing expected by twin-screw extrusion processing. The concentration fluctuations were greater for the blends produced by extruding gelatin and native waxy maize starch mixtures. This was in agreement with the reduced degree of conversion of the starch granules when extruded in the presence of gelatin. The FTIR 2-dimensional maps obtained suggested that in the blends produced from either native or pregelatinized starch at all concentrations studied (25/75, 50/50, and 75/25 amylopectin/gelatin) the gelatin constituted the continuous phase. The effect of the spatial resolution on the FTIR microspectroscopy results was considered and the proposed interpretation was verified by the use of polarized light microscopy and FTIR microspectroscopy acquired at higher spatial resolution (10 microm).

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Section: Resultssupporting

confidence: 72%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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FTIR microspectroscopy study of composition fluctuations in extruded amylopectin–gelatin blends

et al. 2001

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“…Fgd1 is an important actor in skeletal formation because mutations in this gene result in the disease faciogenital dysplasia or Aarskog-Scott syndrome (AAS), an X-linked developmental disorder that adversely affects the formation of multiple skeletal structures (27). Consequently, most studies have thus far focused on osteoblasts and osteoblast-like cell lines.…”

Section: Discussionmentioning

confidence: 99%

The Aarskog-Scott Syndrome Protein Fgd1 Regulates Podosome Formation and Extracellular Matrix Remodeling in Transforming Growth Factor β-Stimulated Aortic Endothelial Cells

Daubon

Buccione

Génot

2011

Molecular and Cellular Biology

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Podosomes are dynamic actin-rich adhesion plasma membrane microdomains endowed with extracellular matrix-degrading activities. In aortic endothelial cells, podosomes are induced by transforming growth factor ␤ (TGF-␤), but how this occurs is largely unknown. It is thought that, in endothelial cells, podosomes play a role in vessel remodeling and/or in breaching anatomical barriers. We demonstrate here that, in bovine aortic endothelial cells, that the Cdc42-specific guanine exchange factor (GEF) Fgd1 is expressed and regulated by TGF-␤ to induce Cdc42-dependent podosome assembly. Within 15 min of TGF-␤ stimulation, Fgd1, but none of the other tested Cdc42 GEFs, undergoes tyrosine phosphorylation, associates with Cdc42, and translocates to the subcortical cytoskeleton via a cortactin-dependent mechanism. Small interfering RNA-mediated Fgd1 knockdown inhibits TGF-␤-induced Cdc42 activation. Fgd1 depletion also reduces podosome formation and associated matrix degradation and these defects are rescued by reexpression of Fgd1. Although overexpression of Fgd1 does not promote podosome formation per se, it enhances TGF-␤-induced matrix degradation. Our results identify Fgd1 as a TGF-␤-regulated GEF and, as such, the first GEF to be involved in the process of cytokine-induced podosome formation. Our findings reveal the involvement of Fgd1 in endothelial cell biology and open up new avenues to study its role in vascular pathophysiology.The cytokine transforming growth factor ␤ (TGF-␤) induces pleiotropic effects. It is a pivotal regulator of vascular homeostasis, in particular in the arterial tree, during adult life (15), but how it fulfils this particular role remains unclear. We recently uncovered a novel role for TGF-␤ in endothelial cell physiology. In the cultured bovine aortic endothelial (BAE) cell model, TGF-␤ was found to remodel the actin cytoskeleton giving rise to the formation of podosomes. These typically occur in large, ring-shaped clusters of about 8 m in diameter (podosome superstructures also termed rosettes) (32). Podosomes are specialized plasma membrane actin-based microdo-

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“…FGD1, the gene responsible for FGDY, was isolated by using an FGDY-specific familial translocation with an Xp11.21 breakpoint to perform positional cloning (Pasteris et al, 1994). The FGD1 mouse ortholog, Fgd1, was also cloned and mapped to a syntenic region of the mouse X chromosome (Pasteris et al, 1995). Biochemical analyses showed that FGD1 encoded a guanine nucleotide exchange factor (GEF) for the p21 GTPase Cdc42, a member of the Rho (Ras homology) family of GTPase proteins (Olson et al, 1996;Zheng et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Isolation, Characterization, and Mapping of the Mouse and Human Fgd2 Genes, Faciogenital Dysplasia (FGD1; Aarskog Syndrome) Gene Homologues

1999

Genomics

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Cloning and regional localization of the mouse faciogenital dysplasia (Fgd1) gene

Cited by 15 publications

References 15 publications

FTIR microspectroscopy study of composition fluctuations in extruded amylopectin–gelatin blends

FTIR microspectroscopy study of composition fluctuations in extruded amylopectin–gelatin blends

The Aarskog-Scott Syndrome Protein Fgd1 Regulates Podosome Formation and Extracellular Matrix Remodeling in Transforming Growth Factor β-Stimulated Aortic Endothelial Cells

Isolation, Characterization, and Mapping of the Mouse and Human Fgd2 Genes, Faciogenital Dysplasia (FGD1; Aarskog Syndrome) Gene Homologues

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