30 research outputs found
Prognostic model to predict postoperative acute kidney injury in patients undergoing major gastrointestinal surgery based on a national prospective observational cohort study.
Background: Acute illness, existing co-morbidities and surgical stress response can all contribute to postoperative acute kidney injury (AKI) in patients undergoing major gastrointestinal surgery. The aim of this study was prospectively to develop a pragmatic prognostic model to stratify patients according to risk of developing AKI after major gastrointestinal surgery. Methods: This prospective multicentre cohort study included consecutive adults undergoing elective or emergency gastrointestinal resection, liver resection or stoma reversal in 2-week blocks over a continuous 3-month period. The primary outcome was the rate of AKI within 7 days of surgery. Bootstrap stability was used to select clinically plausible risk factors into the model. Internal model validation was carried out by bootstrap validation. Results: A total of 4544 patients were included across 173 centres in the UK and Ireland. The overall rate of AKI was 14路2 per cent (646 of 4544) and the 30-day mortality rate was 1路8 per cent (84 of 4544). Stage 1 AKI was significantly associated with 30-day mortality (unadjusted odds ratio 7路61, 95 per cent c.i. 4路49 to 12路90; P < 0路001), with increasing odds of death with each AKI stage. Six variables were selected for inclusion in the prognostic model: age, sex, ASA grade, preoperative estimated glomerular filtration rate, planned open surgery and preoperative use of either an angiotensin-converting enzyme inhibitor or an angiotensin receptor blocker. Internal validation demonstrated good model discrimination (c-statistic 0路65). Discussion: Following major gastrointestinal surgery, AKI occurred in one in seven patients. This preoperative prognostic model identified patients at high risk of postoperative AKI. Validation in an independent data set is required to ensure generalizability
Isolation, purification and characterization of an N-acetyl-D-lactosamine binding mitogenic and anti-proliferative lectin from tubers of a cobra lily Arisaema utile Schott
Lectins are the carbohydrate-binding proteins of
non-immune origin which have been the subject of
intense investigation over the last few decades owing
to the variety of interesting biological properties.
Most of the lectins which have been purified and
characterized from plants have been obtained from
dicotyledons. In the present study a lectin was purified
from tubers of a monocot plant Arisaema utile
(AUL) Schott by affinity chromatography on asialofetuin-
linked amino activated silica beads. AUL
gave a single band in SDS-PAGE at pH 8.3 corresponding
to subunit Mr 13.5 kDa. The native molecular
mass of AUL was 54 kDa suggesting a homotetrameric
structure. AUL gave multiple bands in
isoelectric focusing and in native PAGE at pH 8.3.
AUL was inhibited by N-acetyl-D-lactosamine (Lac
NAc), a disaccharide and asialofetuin, a complex desialylated
serum glycoprotein. When treated with
denaturing agents, the lectin was stable in the presence
of urea (3 M), thiourea (4 M) and guanidine HCl
(4 M). AUL was a glycoprotein with a carbohydrate
content of 1.2%. Complete loss of activity was observed
upon modification of tryptophan residues of
the lectin. The activity was reduced to 25% after
modification of tyrosine. Chemical modification of
arginine, histidine, serine and cysteine residues of
AUL did not affect its activity. Using Far UV CD
spectra the estimated secondary structure was 37%
伪-helix, 25% 尾-sheet and 38% random contributions.
The lectin showed potent mitogenic response towards
human lymphocytes. In vitro anti-proliferative assay
using 11 human cancer cell lines resulted in 50% inhibition
of six cell lines viz. SW-620, HCT-15,
SK-N-SH, IMR-32, Colo-205 and HT-29 at 38, 42, 43,
49, 50 and 89 渭g/ml, respectively
Herbaceous homicide:The Panax ginseng metabolite compound K accelerates caspase-3/7 activation and enhances macrophage cell death in a P2X7-dependent manner
Isolation of a Novel N-acetyl-d-lactosamine Specific Lectin from Alocasia cucullata (Schott.)
An N-acetyl-D-lactosamine (LacNAc) specific lectin from tubers of Alocasia cucullata was purified by affinity chromatography on asialofetuin-linked amino activated silica. The pure lectin showed a single band in SDS-PAGE at pH 8.8 and was a homotetramer with a subunit molecular mass of 13.5 kDa and native molecular mass of 53 kDa. It was heat stable up to 55 锟紺 for 15 min and showed optimum hemagglutination activity from pH 2 to 11. The lectin was affected by denaturing agents such as urea (2 M), thiourea
(2 M) and guanidine锟紿Cl (0.5 M) and did not require Ca2+ and Mn2+ for its activity. It was a potent mitogen at 10 lg/ml towards human peripheral blood mononuclear cells with 50% growth inhibitory potential towards SiHa (human cervix ) cancer cell line at 100 lg/ml