Real-time visualization of MMP-13 promoter activity in transgenic mice

Wu, Nanjun; Opalenik, Susan R.; Liu, Jinhua; Jansen, E.; Giro, M.G.; Davidson, Jeffrey M.

doi:10.1016/s0945-053x(01)00192-5

Cited by 34 publications

(46 citation statements)

References 41 publications

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“…Based on our identification of nucleolin as an ANKRD1 interacting factor and evidence that it acts as a transcriptional regulator of MMP13 (28), we examined the effect of ANKRD1 on regulation of MMP13 promoter activity. We previously reported that murine MMP13 core promoter activity resides within the proximal 660 bp, a region that includes two PEA3 (Ϫ75 and Ϫ122) and one AP1 (Ϫ46) consensus sequences (18) (Fig. 2A).…”

Section: Resultsmentioning

confidence: 97%

“…2A). Therefore, we used a reporter construct containing the MMP13 core promoter cloned upstream of the luciferase gene (p660-MMP13 Luc) as previously described (18) to study the role of ANKRD1 in MMP13 regulation. To confirm the importance of an intact AP-1 site in the MMP13 promoter, we developed four different mutant constructs that had mutations of the AP-1 site within the MMP-13 proximal promoter region of the p660-MMP13 Luc construct ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Collagenases degrade native fibrillar collagens in the extracellular space (16). MMP-13 is one of three mammalian collagenases capable of initiating the degradation of interstitial collagens during wound healing (17,18). It has been reported that angiogenesis and granulation tissue development was delayed in MMP-13 knockout mice (19,20).…”

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confidence: 99%

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ANKRD1 Acts as a Transcriptional Repressor of MMP13 via the AP-1 Site

et al. 2014

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

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ANKRD1 Acts as a Transcriptional Repressor of MMP13 via the AP-1 Site

et al. 2014

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“…To date, studies that examine expression of promoter-luciferase gene expression in transgenic mice using whole-animal measurement of bioluminescence are few (Sadikot et al 2001(Sadikot et al ,2002Carlsen et al 2002;Wu N et al 2002). Here we have examined bioluminescence in LPS-treated mice that express firefly luciferase driven by the NF-B-dependent regulatory portion of the HIV-1 LTR.…”

Section: Discussionmentioning

confidence: 99%

Bioluminescent Detection of Endotoxin Effects on HIV-1 LTR-driven Transcription in Vivo

Yull

Han

Jansen

et al. 2003

J Histochem Cytochem.

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S U M M A R YWe investigated the effects of Gram-negative bacterial lipopolysaccharide (LPS) on luciferase expression in transgenic reporter mice in which luciferase expression is driven by the nuclear factor B (NF-B)-dependent portion of the human immunodeficiency virus-1 (HIV-1) long terminal repeat (HIV-1 LTR). Using these mice, we dissected the sources of luciferase activity at the organ level by (a) assessing luciferase activity in organ homogenates, (b) bioluminescence imaging in vivo, and (c) bioluminescence imaging of individual organs ex vivo. Luciferin dosage was a critical determinant of the magnitude of photon emission from these reporter mice. Photon emission increased at doses from 0.5-6 mg of luciferin given by intraperitoneal (IP) injection. The differential between basal and LPS-induced bioluminescence was maximal at 3-6 mg of luciferin. Luciferase expression was highly inducible in lungs, liver, spleen, and kidneys after a single IP injection of LPS, as assessed by luciferase activity measurements in organ homogenates. Luciferase activity was also induced in the forebrain by treatment with IP LPS. In contrast, aerosolized LPS produced a response localized to the lungs as assessed by both bioluminescence and ex vivo luciferase assay measurements. These studies demonstrate the utility of luciferase reporter mice for determining organ-specific gene expression in response to local and systemic stimuli.

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“…In addition, it plays an important role in cutaneous wound healing (31) and bone formation (14). While different cell types are involved in these processes, the steps parallel those of skeletal muscle repair, where cells must proliferate and migrate to sites of damage and then coordinate the restoration of functional intact tissues.…”

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confidence: 99%

Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration

Lei

Leong

Smith

et al. 2013

American Journal of Physiology-Cell Physiology

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Lei H, Leong D, Smith LR, Barton ER. Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration. Am J Physiol Cell Physiol 305: C529-C538, 2013. First published June 12, 2013 doi:10.1152/ajpcell.00051.2013.-Efficient skeletal muscle repair and regeneration require coordinated remodeling of the extracellular matrix (ECM). Previous reports have indicated that matrix metalloproteinases (MMPs) play the pivotal role in ECM remodeling during muscle regeneration. The goal of the current study was to determine if the interstitial collagenase MMP-13 was involved in the muscle repair process. Using intramuscular cardiotoxin injections to induce acute muscle injury, we found that MMP-13 expression and activity transiently increased during the regeneration process. In addition, in muscles from mdx mice, which exhibit chronic injury, MMP-13 expression and protein levels were elevated. In differentiating C2C12 cells, a murine myoblast cell line, Mmp13 expression was most pronounced after myoblast fusion and during myotube formation. Using pharmacological inhibition of MMP-13 to test whether MMP-13 activity is necessary for the proliferation, differentiation, migration, and fusion of C2C12 cells, we found a dramatic blockade of myoblast migration, as well as a delay in differentiation. In contrast, C2C12 cells with stable overexpression of MMP-13 showed enhanced migration, without affecting myoblast maturation. Taken together, these results support a primary role for MMP-13 in myoblast migration that leads to secondary effects on differentiation.collagenase; matrix metalloproteinase; muscle repair; myoblast maturation

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Real-time visualization of MMP-13 promoter activity in transgenic mice

Cited by 34 publications

References 41 publications

ANKRD1 Acts as a Transcriptional Repressor of MMP13 via the AP-1 Site

ANKRD1 Acts as a Transcriptional Repressor of MMP13 via the AP-1 Site

Bioluminescent Detection of Endotoxin Effects on HIV-1 LTR-driven Transcription in Vivo

Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration

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