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1.
Korean J Anesthesiol ; 61(4): 302-7, 2011 Oct.
Article in English | MEDLINE | ID: mdl-22110883

ABSTRACT

BACKGROUND: During general anesthesia, core temperature decreases, largely due to heat loss caused by peripheral vasodilation, resulting in heat redistribution to peripheral tissues. Multiple factors contribute to body temperature regulation during general anesthesia. It was reported that baroreceptor unloading by positive end-expiratory pressure (PEEP) attenuates anesthetically-induced hypothermia. So, we evaluated the effects of PEEP on thermoregulatory responses during total intravenous anesthesia (TIVA). METHODS: Forty healthy patients scheduled for tympanoplasty were allocated two groups, Group ZEEP (zero end-expiratory pressure, n = 20) and Group PEEP (PEEP application of 5 cmH(2)O, n = 20). Ambient temperature was maintained at 22-24℃, and anesthesia was induced and maintained with propofol-remifentanil. The core temperature and the temperature difference between forearm and fingertip skin were monitored before and after the induction of general anesthesia having a duration of 180 minutes. RESULTS: The core temperature gradient (Ti-Tf) was higher in patients with ZEEP than with PEEP. The core temperature was maintained at a higher level in patients with PEEP. Additionally, the vasoconstriction threshold was higher in patients with PEEP. CONCLUSIONS: It seems that PEEP attenuates anesthetically-induced hypothermia during TIVA.

2.
Proc Natl Acad Sci U S A ; 104(52): 20793-8, 2007 Dec 26.
Article in English | MEDLINE | ID: mdl-18087039

ABSTRACT

Posttranslational modification by small ubiquitin-like modifier (SUMO) controls diverse cellular functions of transcription factors and coregulators and participates in various cellular processes including signal transduction and transcriptional regulation. Here, we report that pontin, a component of chromatin-remodeling complexes, is SUMO-modified, and that SUMOylation of pontin is an active control mechanism for the transcriptional regulation of pontin on androgen-receptor target genes in prostate cancer cells. Biochemical purification of pontin-containing complexes revealed the presence of the Ubc9 SUMO-conjugating enzyme that underlies its function as an activator. Intriguingly, 5alpha-dihydroxytestosterone treatments significantly increased the SUMOylation of pontin, and SUMOylated pontin showed further activation of a subset of nuclear receptor-dependent transcription and led to an increase in proliferation and growth of prostate cancer cells. These data clearly define a functional model and provide a link between SUMO modification and prostate cancer progression.


Subject(s)
Carrier Proteins/chemistry , Chromatin/chemistry , DNA Helicases/chemistry , Prostatic Neoplasms/metabolism , Small Ubiquitin-Related Modifier Proteins/chemistry , ATPases Associated with Diverse Cellular Activities , Cell Line, Tumor , Cell Proliferation , Cell Transformation, Neoplastic , Humans , Hydroxytestosterones/pharmacology , Lysine/chemistry , Male , Models, Biological , SUMO-1 Protein , Signal Transduction , Transcription, Genetic , Ubiquitin-Conjugating Enzymes/metabolism
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