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Titolo:
RENAL EPIDERMAL GROWTH-FACTOR PRECURSOR - PROTEOLYTIC PROCESSING IN AN IN-VITRO CELL-FREE SYSTEM
Autore:
JOURNE F; WATTIEZ R; PIRON A; CARION M; LAURENT G; HEUSONSTIENNON JA; FALMAGNE P;
Indirizzi:
UNIV MONS,DEPT BIOL CHEM,SCH SCI,AVE MAISTRIAU 21 B-7000 MONS BELGIUM UNIV MONS,DEPT BIOL CHEM,SCH SCI B-7000 MONS BELGIUM UNIV MONS,SCH MED,DEPT HISTOL B-7000 MONS BELGIUM
Titolo Testata:
Biochimica et biophysica acta. Molecular cell research
fascicolo: 1, volume: 1357, anno: 1997,
pagine: 18 - 30
SICI:
0167-4889(1997)1357:1<18:REGP-P>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACUTE TUBULAR-NECROSIS; RAT-KIDNEY; URINARY-EXCRETION; FACTOR RECEPTOR; FACTOR BINDING; MESSENGER-RNA; EGF RECEPTOR; KALLIKREIN; EXPRESSION; FAILURE;
Keywords:
EPIDERMAL GROWTH FACTOR; GROWTH FACTOR PRECURSOR; KALLIKREIN; KIDNEY MEMBRANE; RENAL TUBULAR REGENERATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
F. Journe et al., "RENAL EPIDERMAL GROWTH-FACTOR PRECURSOR - PROTEOLYTIC PROCESSING IN AN IN-VITRO CELL-FREE SYSTEM", Biochimica et biophysica acta. Molecular cell research, 1357(1), 1997, pp. 18-30

Abstract

The enzymatic processing of the membrane-bound renal epidermal growthfactor precursor (proEGF) could be an important step in the control of nephrogenic repair consecutive to kidney insult. The enzyme machinery responsible for that processing was examined in a cell-free system consisting of renal membranes isolated from kidney homogenates by differential centrifugation, and incubated in vitro. After a 24-h incubation at 37 degrees C, 6-14% of membrane-bound proEGF was processed and soluble products with EGF immunoreactivity were released. As revealed byHPLC and Western blotting analysis, the products of proEGF proteolysis consisted of 6 kDa EGF (the molecular weight of mature EGF) and two polypeptides with molecular weights around 45 kDa. Interestingly the 45 kDa EGF forms, like the 6 kDa EGF, exhibited mitogenic activity toward growth-arrested NRK-52E renal cell line. The kinetic study of proEGF degradation gave data consistent with the 45 kDa product(s) being processing intermediate(s) between proEGF and 6 kDa EGF. The enzymatic activity responsible for proEGF nicking was inhibited by divalent heavymetal ions (Cu2+ Or Zn2+) and several protease inhibitors (aprotinin,PMSF, leupeptin, soybean trypsin inhibitor), suggesting that proEGF is processed by kallikrein-like serine proteases present in the membrane preparations. Along with previous studies, the current observations suggest that renal kallikreins might play a role in renal tubular regeneration by promoting the release of soluble EGF in renal tissue.

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Documento generato il 01/12/20 alle ore 07:38:42