Xenopus laevis gelatinase B (Xmmp-9): Development, regeneration, and wound healing

Carinato, Maria E.; Walter, Brian E.; Henry, Jonathan J.

doi:10.1002/(sici)1097-0177(200004)217:4<377::aid-dvdy5>3.0.co;2-u

Cited by 46 publications

(42 citation statements)

References 53 publications

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“…as Xmmp-9 expression (clone B66) cannot be detected in control corneas by means of in situ hybridization analyses (see Carinato et al, 2000). Furthermore, colony lift hybridization revealed that this gene is represented in approximately 1:20,000 clones in the original transdifferentiating cornea cDNA library, whereas this clone is represented in 1:150 clones in the subtracted cDNA library (data not shown).…”

Section: Analysis Of Differential Expressionmentioning

confidence: 91%

“…One of these clones, B66 (corresponding to Xenopus matrix metalloproteinase, MMP-9), is not expressed in the embryonic eye (see Fig. 3A, see also Carinato et al, 2000); however, the other five clones (B87, B99, B105, D43, and E7) were found to be expressed in the developing eye and lens, as well as in other tissues (see Fig. 3B-L).…”

Section: Expression Analyses Of Clones Obtained From the Subtracted Cmentioning

confidence: 99%

“…MMPs play major physiological roles in degrading and remodeling the ECM. The presence of a clone encoding gelatinase-B (B66) is significant, because MMP-9 has been shown to be expressed in wounded corneal epithelium and is implicated in corneal ulceration and graft rejection (Berman, 1989;Fini et al, 1995Fini et al, , 1996Fini et al, , 1998Barro et al, 1998;Ye and Azar, 1998;Carinato et al, 2000). MMPs have also been implicated in regeneration (Yang and Bryant, 1994;Yang et al, 1997).…”

Section: A Profile Of Gene Expression In Transdifferentiating Cornea mentioning

confidence: 99%

“…That several of the genes examined do not appear to be expressed during embryonic development (Table 3) indicates that some gene expression may be specific to the process of cornea-lens transdifferentiation. Some of these genes may represent genes involved in wound healing, such as Xmmp-9 (Carinato et al, 2000); others may represent corneal genes that inadvertently passed through the subtraction process, which have nothing to do with lens formation. A key difference between embryonic development and transdifferentiation, or regeneration, involves the initial generation of progenitor cells by means of the localized de-differentiation of cell fates (Eguchi and Kodama, 1993;Del Rio-Tsonis et al, 1995b;Kodama and Eguchi, 1995;Stocum, 1995;Kosaka et al, 1998).…”

Section: Relationships Between the Process Of Embryonic Lens Developmmentioning

confidence: 99%

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Characterizing gene expression during lens formation in Xenopus laevis: Evaluating the model for embryonic lens induction

Henry

Carinato

Schaefer

et al. 2002

Developmental Dynamics

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Few directed searches have been undertaken to identify the genes involved in vertebrate lens formation. In the frog Xenopus, the larval cornea can undergo a process of transdifferentiation to form a new lens once the original lens is removed. Based on preliminary evidence, we have shown that this process shares many elements of a common molecular/genetic pathway to that involved in embryonic lens development. A subtracted cDNA library, enriched for genes expressed during cornea-lens transdifferentiation, was prepared. The similarities/identities of specific clones isolated from the subtracted cDNA library define an expression profile of cells undergoing cornea-lens transdifferentiation ("lens regeneration") and corneal wound healing (the latter representing a consequence of the surgery required to trigger transdifferentiation). Screens were undertaken to search for genes expressed during both transdifferentiation and embryonic lens development. Significantly, new genes were recovered that are also expressed during embryonic lens development. The expression of these genes, as well as others known to be expressed during embryonic development in Xenopus, can be correlated with different periods of embryonic lens induction and development, in an attempt to define these events in a molecular context. This information is considered in light of our current working model of embryonic lens induction, in which specific tissue properties and phases of induction have been previously defined in an experimental context. Expression data reveal the existence of further levels of complexity in this process and suggests that individual phases of lens induction and specific tissue properties are not strictly characterized or defined by expression of individual genes.

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Section: Analysis Of Differential Expressionmentioning

confidence: 91%

Section: Expression Analyses Of Clones Obtained From the Subtracted Cmentioning

confidence: 99%

Section: A Profile Of Gene Expression In Transdifferentiating Cornea mentioning

confidence: 99%

Section: Relationships Between the Process Of Embryonic Lens Developmmentioning

confidence: 99%

See 2 more Smart Citations

Characterizing gene expression during lens formation in Xenopus laevis: Evaluating the model for embryonic lens induction

Henry

Carinato

Schaefer

et al. 2002

Developmental Dynamics

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“…The predicted molecular mass of MMP-9 identified from humans (Murphy and Cockett, 1995), chickens (HahnDantona et al, 2000) and Xenopus (Carinato et al, 2000) was 92 kDa, 75 kDa and 75 kDa, respectively, and has been shown to consist of signal peptide domain, propeptide domain, catalytic domain, fibronectin type-II -like domain, hinge and hemopexinlike domain in its molecule. Judging from the molecular size, the 38 kDa metalloproteinase seemed to consist of catalytic domain only, and might be produced from latent pro-form and activated by a similar machan is m as a p ro p o sit io n fo r m any MMP s. T he hemopexin-like domain of MMPs is known to play an important role in the recognition of substrate in tissue.…”

mentioning

confidence: 99%

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

et al. 2006

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-During the characterization of hemorrhagic factor in venom of Rhabdophis tigrinus tigrinus, so-called Yamakagashi in Japan, one of the Colubridae family, a novel metalloproteinase with molecular weight of 38 kDa in the Duvernoy's gland of Yamakagashi was identified by gelatin zymography and by monitoring its proteolytic activity using a fluorescence peptide substrate, MOCAc-PLGLA 2 pr(Dnp)AR-NH 2 , which was developed for measuring the well-known matrix metalloproteinase (MMP) activity.After purification by gel filtration HPLC and/or column switch HPLC system consisting of an affinity column, which was immobilized with a synthetic BS-10 peptide (MQKPRCGVPD) originating from propeptide domain of MMP-7 and a reversed-phase column, the N-terminal amino acid sequence of the 38 kDa metalloproteinase was identified as FNTFPGDLK which shared a high homology to Xenopus MMP-9.The 38 kDa metalloproteinase required Zn 2+ and Ca 2+ ions for its proteolytic activity. In addition, the proteolytic activity was almost completely inhibited by BS-10, a MMP inhibitor, but not by the serine proteinase inhibitors, cysteine proteinase inhibitors and aspartic proteinase inhibitors.Together these results demonstrated that the 38 kDa proteinase is a novel snake verom metalloproteinase (SVMP) containing HExGHxxGxxH motif which possesses high affinity to the BS-10 peptide, into its molecule, and the enzymatic properties are closed to that of MMPs.Based on the results obtained in the present study, we concluded that the 38 kDa metalloproteinase is a novel metalloproteinase whose activity may be regulated by the cysteine switch mechanism, and could be classified as one of the matrix metalloproteinases rather than snake venom metalloproteinases.

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Matrix metalloproteinases and collective cell migration in 24 h primary zebrafish explant cultures: MMP13 plays an inhibitory role and MMP14 may respond to stretch during reepithelialisation

et al. 2013

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Zebrafish keratocytes collectively migrate rapidly when established in explant cultures but little is known about the signals that initiate motility or the signal transduction pathways that result in an epithelial to mesenchymal transition. Matrix metalloproteinases (MMPs) are strong candidates for playing a role in this regulation and have previously not been analysed in this wound healing model system. Results presented here document a rapid and dramatic rise in MMP14a, MMP2, MMP9 and MMP13a mRNA levels over time. In a motility assay, a broad-spectrum MMP inhibitor and an inhibitor specific for MMP2 and MMP9 significantly decrease cell migration in a dose dependent manner but treatment with an MMP13 specific inhibitor significantly increases cell sheet area. Immunofluorescence staining with an antibody specific for the catalytic domain of MMP14 indicates that activated MMP14 protein is highly expressed on cells at the leading edge of a sheet compared with follower cells in the centre of the sheet, and is augmented further in leader cells that are stretched, thus likely in the process of detaching from the cell sheet. These data are consistent with a model in which active MMP14 at the leading edge of cell sheets in explant cultures triggers activation of MMP2 and/or MMP9, thus creating promigratory signal(s) that outweigh the inhibitory role of targets cleaved by MMP13. Taken together, these data suggest that MMPs play an important but complex role in regulating the collective cell migration of zebrafish keratocytes and provide support for the relevance of using zebrafish as a model for human disease.

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Xenopus laevis gelatinase B (Xmmp-9): Development, regeneration, and wound healing

Cited by 46 publications

References 53 publications

Characterizing gene expression during lens formation in Xenopus laevis: Evaluating the model for embryonic lens induction

Characterizing gene expression during lens formation in Xenopus laevis: Evaluating the model for embryonic lens induction

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

Matrix metalloproteinases and collective cell migration in 24 h primary zebrafish explant cultures: MMP13 plays an inhibitory role and MMP14 may respond to stretch during reepithelialisation

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