Regulatory Role of Extracellular Matrix Components in Expression of Matrix Metalloproteinases in Cultured Hepatic Stellate Cells.

Li, Yilei; Sato, Mitsuru; Kojima, Naosuke; Miura, Mitsutaka; Senoo, Haruki

doi:10.1247/csf.24.255

Cited by 25 publications

(30 citation statements)

References 26 publications

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“…MMP-2 mRNA was up-regulated in HSCs cultured on type I collagen gel, as compared with its level in the cells cultured on the polystyrene surface, type I collagen-coated surface, or Matrigel. However, even when HSCs were cultured in serum-supplemented DMEM, the active form of MMP-2 specifically appeared in HSCs cultured on type I collagen gel but not on a polystyrene surface, type I collagen-coated surface, and Matrigel (Li et al, 1999). Since the serum (FBS) used for cell culture contains a significant amount of pro-MMP-2 but no active form of MMP-2 (Li et al, 1999), as was shown in Fig.…”

Section: Discussionmentioning

confidence: 89%

“…However, even when HSCs were cultured in serum-supplemented DMEM, the active form of MMP-2 specifically appeared in HSCs cultured on type I collagen gel but not on a polystyrene surface, type I collagen-coated surface, and Matrigel (Li et al, 1999). Since the serum (FBS) used for cell culture contains a significant amount of pro-MMP-2 but no active form of MMP-2 (Li et al, 1999), as was shown in Fig. 1, the pro-MMP-2 activation events are specific to the HSC culture on type I collagen gel, probably through up-regulation of MT1-MMP and TIMP-2.…”

Section: Discussionmentioning

confidence: 96%

“…Aliquots (100 ml) of each conditioned medium (CM) were treated with 4 volumes of cold acetone, and the precipitates were dissolved in Laemmli's sample buffer without 2-mercaptoethanol, and then used for gelatin zymography as previously described (Gilles et al, 1997;Li et al, 1999). In brief, acetoneprecipitates from the CMs were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using 10% polyacrylamide gel containing 1 mg/ml gelatin.…”

Section: Gelatin Zymographymentioning

confidence: 99%

“…In addition to MMPs, TIMP-1 and -2, which can inhibit MMP activities, are expressed only in HSCs (Iredale et al, 1992;Herbst et al, 1997;Knittel et al, 1999;Friedman and Arthur, 2002). Cultured HSCs have been found to respond to extracellular type I or type III collagen fibrils used as a substratum by displaying altered morphology and function including proliferation, ECM production, or MMP expression (Senoo et al, 1996;Li et al, 1999;Sato et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

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Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Wang

Sato

et al. 2003

Cell Struct. Funct.

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ABSTRACT. Cultured hepatic stellate cells (HSCs) are known to change their morphology and function with respect to the production of extracellular matrices (ECMs) and matrix metalloproteinases (MMPs) in response to ECM components. We examined the regulatory role of the native form of type I collagen fibrils in pro-MMP-2 production and activation in cultured HSCs. Gelatin zymography of the conditioned media revealed that pro-and active form of MMP-2 was increased in the HSCs cultured on type I collagen gel but not on type I collagen-coated surface, gelatin-coated surface, type IV collagen-coated surface, or Matrigel, suggesting the importance of the native form of type I collagen fibrils in pro-MMP-2 production and activation. The induction of active MMP-2 by extracellular type I collagen was suppressed by the blocking antibody against integrin b1 subunits, indicating the involvement of integrin signaling in pro-MMP-2 activation. RT-PCR analysis indicated that MMP-2, membrane type-1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) mRNA levels were elevated in HSCs cultured on type I collagen gel. The increased MT1-MMP proteins were localized on the cell surface of HSCs cultured on type I collagen gel. In contrast to the expression of MMP-2, HSCs showed a great decline in MMP-13 expression in HSCs cultured on type I collagen gel. These results indicate that the native fibrillar (polymerized) but not monomeric form of type I collagen induced pro-MMP-2 production and activation through MT1-MMP and TIMP-2 in cultured HSCs, suggesting an important role of HSCs in ECM remodeling in the hepatic perisinusoidal spaces.

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 96%

Section: Gelatin Zymographymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Wang

Sato

et al. 2003

Cell Struct. Funct.

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“…114 Active forms of MMP-1 and MMP-2 can be detected around human HSC cultured on collagen gel by in situ zymography and in the culture medium, respectively. 115 The expression of MMP-13 increases in rat liver MFB when the cells are embedded in attached collagen gel. However, the observed collagen degradation is a result of a joint action of a few proteinases.…”

mentioning

confidence: 96%

Collagen matrix as a tool in studying fibroblastic cell behavior

Kanta

2015

Cell Adhesion & Migration

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Distribution of vitamin A‐storing lipid droplets in hepatic stellate cells in liver lobules—A comparative study

Higashi

Senoo

2003

Anat. Rec.

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To investigate the storage mechanisms of vitamin A, we examined the liver of adult polar bears and arctic foxes, which physiologically store a large amount of vitamin A, by high-performance liquid chromatography (HPLC), transmission electron microscopy (TEM) morphometry, gold chloride staining, fluorescence microscopy for the detection of autofluorescence of vitamin A, staining with hematoxylin-eosin (H&E), Masson's trichrome, and Ishii and Ishii's silver impregnation. HPLC revealed that the polar bears and arctic foxes contained 1.8 -1.9 ϫ 10 4 nmol total retinol (retinol plus retinyl esters) per gram liver. In the arctic foxes, the composition of the retinyl esters was found to be 51.1% palmitate, 26.6% oleate, 15.4% stearate, and 7% linoleate. The hepatic stellate cells of the arctic animals were demonstrated by TEM to contain the bulk of the vitamin A-lipid droplets in their cytoplasm. The liver lobules of the arctic animals showed a zonal gradient in the storage of vitamin A. The gradient was expressed as a symmetric crescendo-decrescendo profile starting at the periportal zone, peaking at the middle zone, and sloping down toward the central zone in the liver lobule. The density (i.e., cell number per area) of hepatic stellate cells was essentially the same among the zones. The gradient and the composition of the retinyl esters in storing vitamin A were not changed by differences in the vitamin A amount in the livers. These results indicate that the heterogeneity of vitamin A-storage capacity in hepatic stellate cells of arctic foxes and polar bears is genetically determined. Anat Rec Part A 271A: 240 -248, 2003.

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Regulatory Role of Extracellular Matrix Components in Expression of Matrix Metalloproteinases in Cultured Hepatic Stellate Cells.

Cited by 25 publications

References 26 publications

Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Collagen matrix as a tool in studying fibroblastic cell behavior

Distribution of vitamin A‐storing lipid droplets in hepatic stellate cells in liver lobules—A comparative study

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