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Differential modulation of interleukin-1α (IL-1α) and interleukin-1β(IL-1β in human epidermal keratinocytes by UVB (1994)

Kondo, Seiji ; Sauder, Daniel N. ; Kono, Takeshi ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Experimental dermatology 3 (1994), S. 0

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ISSN: 1600-0625

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Abstract Conflicting reports exist concerning ultraviolet-B (UVB) effects on keralinocyte (KC) interleukin-l (IL-1) expression. To clarify the modulatery effects of UVB on IL-1, the following study was undertaken. Normal human epidermal KCs cultured in a standard low Ca2+ and serum-free medium were irradiated in quiescent phase with UVB. In this study, we used semiquantitative reverse transcriptase-polymerase chain reaction (RT-PCR) to determine the mRNA level of interleukin-1α (IL-1α) and interleukin-1β (IL-β). After exposure to 100 or 300 J/m2 UVB, a transient increase in mRNA levels was observed within I hour for IL-1α and 3 to 6 h for IL-β Following this transient induction, mRNA levels for both IL-1α and IL-1β returned to steady-state levels after 100 J/m2. After 300 J/m2 irradiation, IL-1α and IL-1β levels were downregulated compared to unirradiated cultures at 24-h post-irradiation. The half-life for IL-1α and IL-1β was estimated using actinomycin D treatment. Both IL-1α and IL-1β mRNAs half-lives (t1/2) decreased faster in irradiated cells (t1/2 = 30 minutes for IL-1α and 2 h for IL-1β) compared to unirradiated cells (t1/2= 1 h and 4 h, respectively). These results suggest that IL-1α and IL-1β mRNA expression are differentially regulated by UVB. In contrast to down-regulation of mRNA levels, a significant increase in IL-1α protein levels, measured by ELISA. was observed in culture supernatant from 6 h to 24 h after 300 J/m2 UVB irradiation. Cycloheximide treatment did not abrogate this increase in IL-1α protein level. Since this dose of UVB irradiation decreased the stability of IL-1α and IL-1β mRNA, this suggests that the release of IL-1α after UVB irradiation was due to leakage from UVB-damaged cells and not from de novo protein synthesis.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1600-0625.1994.tb00263.x

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Coupling of ATP Hydrolysis with Channel Gating by Purified, Reconstituted CFTR (1997)

Bear, Christine E. ; Li, Canhui ; Galley, Kevin ; [et al.]

Springer

Journal of bioenergetics and biomembranes 29 (1997), S. 465-473

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ISSN: 1573-6881

Keywords: Cystic fibrosis ; transmembrane conductance regulator (CFTR) ; chloride channel activity ; ATPase activity ; purified protein

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Physics

Notes: Abstract The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel situated on the apical membrane of epithelial cells. Our recent studies of purified, reconstituted CFTR revealed that it also functions as an ATPase and that there may be coupling between ATP hydrolysis and channel gating. Both the ATP turnover rate and channel gating are slow, in the range of 0.2 to 1 s−1, and both activities are suppressed in a disease-causing mutation situated in a putative nucleotide binding motif. Our future studies using purified protein will be directed toward understanding the structural basis and mechanism for coupling between hydrolysis and channel function.