Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Truncated active matrix metalloproteinase-8 gene expression in HepG2 cellsis active against native type I collagen
Autore:
Siller-Lopez, F; Garcia-Banuelos, J; Hasty, KA; Segura, J; Ramos-Marquez, M; Qoronfleh, MW; Aguilar-Cordova, E; Armendariz-Borunda, J;
Indirizzi:
UG, CUCS, Inst Biol Mol Med, Guadalajara, Jalisco, Mexico UG Guadalajara Jalisco Mexico Biol Mol Med, Guadalajara, Jalisco, Mexico Univ Tennessee, Dept Neurobiol & Anat, Memphis, TN USA Univ Tennessee Memphis TN USA ee, Dept Neurobiol & Anat, Memphis, TN USA Antex Biol, Gaithersburg, MD USA Antex Biol Gaithersburg MD USAAntex Biol, Gaithersburg, MD USA Baylor Coll Med, Texas Childrens Hosp, Dept Pediat, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 , Dept Pediat, Houston, TX 77030 USA
Titolo Testata:
JOURNAL OF HEPATOLOGY
fascicolo: 5, volume: 33, anno: 2000,
pagine: 758 - 763
SICI:
0168-8278(200011)33:5<758:TAMMGE>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN NEUTROPHIL COLLAGENASE; SUBSTRATE-SPECIFICITY; HEPATIC FIBROGENESIS; LIVER FIBROSIS; TRANSCRIPTION; PERSPECTIVES; THERAPY; DNA;
Keywords:
active MMP-8; collagen; collagenase; gene transfer;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Armendariz-Borunda, J UG, CUCS, Inst Biol Mol Med, Apdo Postal 2-123, Guadalajara, Jalisco, Mexico UG Apdo Postal 2-123 Guadalajara Jalisco Mexico ico
Citazione:
F. Siller-Lopez et al., "Truncated active matrix metalloproteinase-8 gene expression in HepG2 cellsis active against native type I collagen", J HEPATOL, 33(5), 2000, pp. 758-763

Abstract

Background/Aims: Excess type I collagen accumulation is a major feature offibrotic diseases such as liver cirrhosis, Reversion of this disease has not been fully accomplished, Physiologically, collagen is degraded by interstitial collagenases, neutrophil collagenase (MMP-8) being the most active against type I collagen, Introduction of MMP-8 gene into liver cells could be an advantageous tool to potentiate fibrosis degradation. Methods: We cloned latent and active MMP-8 genes in prokaryotic and eukaryotic expression vectors and an adenoviral vector, Transfection of MMP-8 in HepG2 was effectuated by CaPO4, polylysine-lactose (P-L) and adenoviral transduction, and cells and culture supernatant were harvested 72 h after transfection for analysis of MMP-8 expression by reverse transcription-polymerase chain reaction and collagenolytic activity. Results and Conclusions: We show that a truncated neutrophil collagenase (tMMP-8) lacking a portion of the carboxy terminus and with an intact amino-terminus (latent; l-tMMP-8) or a truncated amino terminus (active; a-tMMP-8) has enzymatic activity against native type I collagen, and the activity was inhibited by EDTA, 1,10-phenanthroline and TIMP-1, Both MMP-8 mRNA (latent and active) were detected by polymerase chain reaction in cells transfected with CaPO4, P-L and adenoviral transduction; however, relative expression of MMP-8 was enhanced when the plasmid was delivered as a P-L complex and increased by adenoviral infection, Finally, a-tMMP-8 cDNA was cloned in avector under transcriptional control of a regulated promoter (PEPCK-a-tMMP-8), HepG2 cells transfect ed with the PEPCK-a-tMMP-8 plasmid DNA up-regulated expression of a-tMMP-8 after incubation of the cells with butyryl-cAMP and glucagon, while stimulation with insulin slightly down-regulated its expression, Recombinant MMP-8 expressed by HepG2-transduced cells can efficiently degrade soluble type I collagen, which is potentially useful for gene transfer therapies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 10:59:54