Truncated active matrix metalloproteinase-8 gene expression in HepG2 cells is active against native type I collagen

Siller-López, Fernando; García-Bañuelos, Jesús; Hasty, Karen A.; Segura, J; Ramos-Márquez, Martha E.; Qoronfleh, M. Walid; Aguilar-Córdova, Estuardo; Armendáriz‐Borunda, Juan

doi:10.1016/s0168-8278(00)80307-4

Cited by 12 publications

(13 citation statements)

References 21 publications

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“…To determine whether this system could be useful in improving liver cirrhosis in an experimental model, we selected neutrophil collagenase (Matrix Metalloproteinase 8; MMP8) as a potential therapeutic reagent, 21 due to the fact that this enzyme preferentially hydrolyzes collagens faster than hepatic fibroblast collagenase. In human cirrhosis, collagen I is the most prominent extracellular protein and its abundant synthesis and deposition is responsible for alterations in hepatic architecture and consequent hemodynamic dysfunctions.…”

Section: Figure 3 Histologic Analysis Of Transduction and Fibrosis Inmentioning

confidence: 99%

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Cirrhotic rat livers with extensive fibrosis can be safely transduced with clinical-grade adenoviral vectors. Evidence of cirrhosis reversion

et al. 2002

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Section: Figure 3 Histologic Analysis Of Transduction and Fibrosis Inmentioning

confidence: 99%

“…For the experiments to check for fibrosis revertion, AdMMP8 was generated as described before by our group. 21 Briefly, pAdHM2-MMP8 was transfected into 293 cells. pAdHM2-MMP8 was constructed by an in vitro ligation method of the MMP-8 cDNA in a replication-defective dE1, dE3 adenoviral plasmid.…”

Section: Adenoviral Vectorsmentioning

confidence: 99%

Cirrhotic rat livers with extensive fibrosis can be safely transduced with clinical-grade adenoviral vectors. Evidence of cirrhosis reversion

et al. 2002

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“…MMP-8, also known as neutrophil collagenase, is not only expressed in neutrophils, but it is also expressed in wide variety of cells, including chondrocytes, endothelial cells, synovial fibroblast and various cancer cells (Siller-Lopez et al, 2000;Stadlemann et al, 2003;Lint and Libert, 2006). MMP-8 cleaves all three ␣-chains of type I, II and III collagen and also a wide range of non-collagenous substrates, and plays important roles in inflammation and in cancer progression (Lint and Libert, 2006).…”

Section: Introductionmentioning

confidence: 99%

The C-terminus of ephrin-B1 regulates metalloproteinase secretion and invasion of cancer cells

Tanaka¹,

Sasaki

Kamata³

et al. 2007

Journal of Cell Science

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Interaction of the Eph family of receptor protein tyrosine kinases and their ligands, ephrin family members, induces bi-directional signaling via cell-cell contacts. High expression of B-type ephrin is associated with high invasion potential of tumors, however, the mechanism by which ephrin-B promotes cancer cell invasion is poorly understood. We show that interaction of ephrin-B1 with the Eph receptor B2 (EphB2) significantly enhances processing of the extracellular domain of ephrin-B1, which is regulated by the C-terminus. Matrix metalloproteinase-8 (MMP-8) is the key protease that cleaves ephrin-B1, and the C-terminus of ephrin-B1 regulates activation of the extracellular release of MMP-8 without requirement of de novo protein synthesis. One possible mechanism by which ephrin-B1 regulates the exocytosis of MMP-8 is the activation of Arf1 GTPase, a critical regulator of membrane trafficking. In support of this hypothesis, activation of ephrin-B1 increased GTP-bound Arf1, and the secretion of MMP-8 was reduced by expression of a dominant-negative mutant of Arf1. Expression of ephrin-B1 promoted the invasion of cancer cells in vivo, which required the C-terminus of ephrin-B1. Our results suggest a novel function of the C-terminus of ephrin-B1 in activating MMP-8 secretion, which promotes the invasion of cancer cells.

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“…4). Although it has been reported that HepG2 cells respond to glucagon treatment (71), most studies suggest that glucagon receptors are markedly downregulated in hepatoma cells (20,54). Not surprisingly, therefore, glucagon failed to induce G-6-Pase catalytic subunit-luciferase fusion gene expression in HepG2 cells (Fig.…”

mentioning

confidence: 90%

Selective stimulation of G-6-Pase catalytic subunit but not G-6-Ptransporter gene expression by glucagon in vivo and cAMP in situ

Hornbuckle¹,

Everett²,

Martin³

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

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We recently compared the regulation of glucose-6-phosphatase (G-6-Pase) catalytic subunit and glucose 6-phosphate (G-6- P) transporter gene expression by insulin in conscious dogs in vivo (Hornbuckle LA, Edgerton DS, Ayala JE, Svitek CA, Neal DW, Cardin S, Cherrington AD, and O'Brien RM. Am J Physiol Endocrinol Metab 281: E713–E725, 2001). In pancreatic-clamped, euglycemic conscious dogs, a 5-h period of hypoinsulinemia led to a marked increase in hepatic G-6-Pase catalytic subunit mRNA; however, G-6- P transporter mRNA was unchanged. Here, we demonstrate, again using pancreatic-clamped, conscious dogs, that glucagon is a candidate for the factor responsible for this selective induction. Thus glucagon stimulated G-6-Pase catalytic subunit but not G-6- P transporter gene expression in vivo. Furthermore, cAMP stimulated endogenous G-6-Pase catalytic subunit gene expression in HepG2 cells but had no effect on G-6- P transporter gene expression. The cAMP response element (CRE) that mediates this induction was identified through transient transfection of HepG2 cells with G-6-Pase catalytic subunit-chloramphenicol acetyltransferase fusion genes. Gel retardation assays demonstrate that this CRE binds several transcription factors including CRE-binding protein and CCAAT enhancer-binding protein.

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Truncated active matrix metalloproteinase-8 gene expression in HepG2 cells is active against native type I collagen

Cited by 12 publications

References 21 publications

Cirrhotic rat livers with extensive fibrosis can be safely transduced with clinical-grade adenoviral vectors. Evidence of cirrhosis reversion

Cirrhotic rat livers with extensive fibrosis can be safely transduced with clinical-grade adenoviral vectors. Evidence of cirrhosis reversion

The C-terminus of ephrin-B1 regulates metalloproteinase secretion and invasion of cancer cells

Selective stimulation of G-6-Pase catalytic subunit but not G-6-Ptransporter gene expression by glucagon in vivo and cAMP in situ

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