Cloning and Characterization of a Rat Ortholog of MMP-23 (Matrix Metalloproteinase-23), a Unique Type of Membrane-Anchored Matrix Metalloproteinase and Conditioned Switching of Its Expression during the Ovarian Follicular Development

Ohnishi, Junji; Ohnishi, Eriko; Jin, Mulan; Hirano, Wakako; Nakane, Dai; Matsui, Hitoshi; Kimura, Atsushi; Sawa, Hirofumi; Nakayama, Kazuhisa; Shibuya, H.; Nagashima, Kazuo; Takahashi, Takayuki

doi:10.1210/mend.15.5.0638

Cited by 37 publications

(22 citation statements)

References 34 publications

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“…MMP23A (matrix metallopeptidase 23A), whose transcription is down-regulated, is a membrane-anchored matrix metalloproteinase. Interestingly, in serum-free primary culture of rat granulosa cells, a drastic diminution of MMP23 expression is observed in response to folliclestimulating hormone (25). The same signaling activates aromatase, which is stimulated by FOXL2.…”

Section: Resultsmentioning

confidence: 99%

Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics

Batista

Vaiman

Dausset

et al. 2007

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

110

102

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FOXL2 is a gene encoding a forkhead transcription factor, whose mutations are responsible for the blepharophimosis-ptosisepicanthus inversus syndrome that often involves premature ovarian failure. FOXL2 is one of the earliest ovarian markers and it offers, along with its targets, an excellent model to study ovarian development and function in normal and pathological conditions. We have recently shown that the aromatase gene is a target of FOXL2, and only three other targets have been reported so far. To detect potential transcriptional targets of FOXL2, we used DNA chips and quantitative PCR to compare the transcriptomes of granulosa-like cells overexpressing, or not, FOXL2. This analysis showed that mediators of inflammation, apoptotic and transcriptional regulators, genes involved in cholesterol metabolism, and genes encoding enzymes and transcription factors involved in reactive oxygen species detoxification were up-regulated. On the other hand, FOXL2 down-regulated the transcription of several genes involved in proteolysis and signal transduction and in transcription regulation. A bioinformatic analysis was conducted to discriminate between potential target promoters activated and repressed by FOXL2. In addition, the promoters of strongly activated genes were enriched in forkhead recognition sites, suggesting that these genes might be direct FOXL2 targets. Altogether, these results provide insight into the activity of FOXL2 and may help in understanding the mechanisms of pathogenesis of FOXL2 mutations if the targets prove to be the same in the ovary.forkhead ͉ infertility ͉ premature ovarian failure ͉ ovary

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Section: Resultsmentioning

confidence: 99%

Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics

Batista

Vaiman

Dausset

et al. 2007

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

110

102

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“…Full-length MMP23 has been reported previously to be expressed mainly in ER/Golgi membranes (21,22 (20,23,(63)(64)(65)(66)) (see the BioGPS Web site) that overlap with the tissue expression of MMP23-sensitive K ϩ channels. Therefore, there is a reasonable likelihood that MMP23 will modulate K ϩ channels in vivo.…”

Section: Discussionmentioning

confidence: 99%

Potassium Channel Modulation by a Toxin Domain in Matrix Metalloprotease 23

Rangaraju

Khoo

Feng

et al. 2010

Journal of Biological Chemistry

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Mechanisms that fine tune the activity of potassium channels are crucial to a cell's ability to integrate and respond to a plethora of internal and external signals. Peptide toxins from venomous creatures have served as vital tools to define the molecular mechanisms underlying K ϩ channel function (1, 2). It has been suggested that toxins evolved from endogenous genes that function in normal cellular pathways (3, 4). Indeed, venomous creatures possess toxins with homology to several proteins, including acetylcholinesterases (5), phospholipases (6, 7), nerve growth factor (8), endothelins (9), Lynx-1 (10, 11), Kunitz-type serine protease inhibitors (12), and the ion channel regulatory (ICR) 5 domains of cysteinerich secretory proteins (CRISPs) (3,13,14). Mammalian proteins containing toxin-like domains (TxDs) that block K ϩ channels have not been characterized previously.BgK, a 37-residue peptide toxin from the sea anemone Bunodosoma granulifera (15,16), and ShK, a 35-residue peptide toxin from the sea anemone Stichodactyla helianthus (17,18) are potent inhibitors of K ϩ channels. The Simple Modular Architecture Research Tool (SMART) (available on the World Wide Web) predicts the existence of a large superfamily of proteins that contain domains (referred to as ShKT domains in the SMART data base) resembling these two toxins (Fig. 1A). Many of these proteins (ϳ70 proteins) are metallopeptidases, whereas others are prolyl-4-hydroxylases, tyrosinases, peroxidases, oxidoreductases, or proteins containing epidermal growth factor-like domains, thrombospondin-type repeats, or trypsin-like serine protease domains (Fig. 1B). The only human protein containing a ShKT domain in the SMART data base is MMP23 (matrix metalloprotease 23). Matrix metalloproteases belong to the metzincin superfamily and play important roles in tissue remodeling, development, and the immune response (19).MMP23 is expressed in many tissues and exists either as a type II transmembrane protein in ER/nuclear membranes or as a secreted form following cleavage of the RRRRY motif just N-terminal to the Zn 2ϩ -dependent metalloprotease domain (20 -23). The ShKT domain of MMP23 (MMP23 TxD ) lies between the metalloprotease domain and an immunoglobulinlike cell adhesion molecule (IgCAM) domain ( Fig. 2A). MMP23 has been implicated in prostate, brain, and breast cancer (24 -26). In humans, two related sequences, MMP23A (a pseudogene) and MMP23B, are co-located on chromosome 1p36 (20). We have investigated MMP23 to gain insight into the structure and physiological functions of ShKT toxin domains and describe the solution structure of the MMP23 TxD domain, its * This work was supported, in whole or in part, by National Institutes of Health

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“…RNA hybridized with the radiolabeled probe was detected with a BAS-5000 imaging system (Fuji Film). In situ hybridization was performed as described previously (20). Briefly, mouse testis and human brain were embedded in Tissue-Tec OCT compound and frozen in liquid nitrogen.…”

Section: Methodsmentioning

confidence: 99%

A Novel Dynamin-associating Molecule, Formin-binding Protein 17, Induces Tubular Membrane Invaginations and Participates in Endocytosis

Kamioka

Fukuhara

Sawa

et al. 2004

Journal of Biological Chemistry

Self Cite

108

112

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Dynamin associates with a variety of SH3 domaincontaining molecules via a C-terminal proline-rich motif and takes part, with them, in endocytic processes. Here, we have investigated a new dynamin-associating molecule, formin-binding protein 17 (FBP17), involved in deforming the plasma membrane and in endocytosis. FBP17 formed tubular invaginations originating from the plasma membrane. Its N-terminal Fer/CIP4 homology domain, a coiled-coil domain, and a proline-rich motif were required for tubular invagination and self-assembly, by which tubular invagination might be induced. Using anti-FBP17 antibody, we detected positive immunoreactions in the testis that were restricted to the germ cells. We also detected FBP17 in the brain by immunoblotting and in situ hybridization. When COS cells expressing enhanced green fluorescent proteintagged FBP17 were incubated with fluorescently labeled transferrin, epidermal growth factor, and cholera toxin, these molecules co-localized with FBP17-induced tubular invaginations, suggesting that FBP17 is involved in dynamin-mediated endocytosis in both a clathrin-dependent and -independent manner. These observations therefore indicate that FBP17 interacts with dynamin and regulates endocytosis by forming vesicotubular structures.The plasma membrane changes its structure dynamically in response to a wide variety of extracellular stimuli that alter cell shape. Membrane extension, including the formation of filopodia and lamellipodia, is controlled by the Rho family GTPases Cdc42 and Rac, respectively (1). Rac and Cdc42 are involved in forming membrane protrusions essential for phagocytosis and macropinocytosis (2), whereas another GTPase, dynamin, has been implicated in producing membrane invaginations and vesicles from the plasma membrane (3).Dynamin is a multidomain GTPase; it consists of a GTPase domain followed by a central domain lacking homology to any other proteins, a pleckstrin homology domain, an effector domain, and a C-terminal proline-rich motif (4). Dynamin-1 (neuron-specific), dynamin-2 (ubiquitously expressed), and dynamin-3 (expressed only in the testis, brain, and lung), constitute the dynamin family (5-7). These proteins are essential for clathrin-dependent and also caveolae-mediated endocytosis (reviewed in Refs. 8 and 9). In addition, association of dynamin with Src homology 3 (SH3) 1 domain-containing molecules has been shown to modulate endocytosis since the Cterminal proline-rich motif provides an SH3 domain-binding site (10). The dynamin-binding molecules amphiphysin, endophilin, intersectin, and PACSIN/syndapin have been reported to be involved in modulating dynamin-dependent endocytosis (4, 11).Formin-binding protein 17 (FBP17) consists of an N-terminal Fer/Cdc42-interacting protein 4 (CIP4) homology (FCH) domain followed by the first coiled-coil domain, a proline-rich motif, the second coiled-coil domain, a Rho family proteinbinding domain (RBD), and a C-terminal SH3 domain. FBP17 was originally isolated as a molecule that binds to the prolinerich region of ...

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Cloning and Characterization of a Rat Ortholog of MMP-23 (Matrix Metalloproteinase-23), a Unique Type of Membrane-Anchored Matrix Metalloproteinase and Conditioned Switching of Its Expression during the Ovarian Follicular Development

Cited by 37 publications

References 34 publications

Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics

Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics

Potassium Channel Modulation by a Toxin Domain in Matrix Metalloprotease 23

A Novel Dynamin-associating Molecule, Formin-binding Protein 17, Induces Tubular Membrane Invaginations and Participates in Endocytosis

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