A new tumor biomarker: Serum protein peak at 3144 m/z in patients with node-positive breast cancer.

e22050 Background: To explore the association of the 3144 m/z and the clinicopathological features and its clinical value in the diagnosis and prognosis of breast cancer. Methods: Using SELDI-TOF-MS, we analyzed serum 3144 m/z in 298 patients patients with node-positive breast cancer after mastectomy. The association between 3144 m/z and clinicopathological features was evaluated. We also evaluated their prognosis value in survival using univariable and multivariable statistical analyses. Results: The positive rate was higher in 3144 m/z than CA153 (36.6% versus 11.5%, p <0.001). The 3144 m/z positive rate was no difference in patients with CA153 negative or positive (35.3% versus 29.6%, P =0.563). 3144 m/z was higher elder cases (> 50 years old) than young group(<or=50 years old). There were no correlation was found between 3144 m/z and other clinicopathological features, except for the age (42.8% in > 50-year-old and 31.2% in young,χ2=4.227, P=0.040). The patients with 3144m/z negative (n=189) had higher 3-year OS rate than positive (n=109), 89.5% versus 81.7% (P=0.034). Also in young (P=0.024), postmenopasual (P=0.025), small tumor (P<0.001), node(-) or less (P<0.001), early stage (P<0.001), good molecular type (P=0.019), normal CA153 (P<0.001), neoadjuvant chemotherapy (P=0.001). Using Cox proportional hazards model,analysis showed that basal-like type (worse, P=0.038), CA153 positive (worse, P=0.015), adjuvant chemotherapy (better, P=0.028) and adjuvant radiotherapy (better, P=0.032) were independent prognostic factors in patients with node-positive breast cancer. but the 3144m/z was not. Conclusions: Serum protein peak at 3144 m/z provides a new, practical biomarker for diagnosis and prognosis of breast cancer.

Effect of Ion-Exchange Adsorption on the Protein Profiles of White Wines

The protein profiles of two different wines of Austrian and Portuguese origin, characterized by HPLC fractionation, were compared before and after ion-exchange adsorption of the wine proteins. Conventionally used sodium bentonite and three alternative nonswelling commercial resins were used. Profile similarity was assessed in terms of the Euclidean distance of all protein peak areas for two samples, and of the average of the differences between each protein peak percentile area between two samples. In general, the differences between profiles for the same material increased with the amount of wine adsorbed, showing that some protein fractions were more easily adsorbed than others. Differences between the adsorption with bentonite or with the alternative adsorbents were not statistically significant, with the exception of one adsorbent in one of the wines, where protein removal was more extensive.

Peroxidase-Polyphenol Oxidase Association in Dioscorea esculenta

A crude enzyme extract from Dioscorea esculenta var. fasiculata tissue subjected to ion exchange chromatography on DEAE-Sephadex A-50 column. This proced ure resolved the extract into two main protein peaks one of which eluted through the column relatively unbound while the other protein peak which remained bound to the column was eluted with 1.0 ᴍ NaCl. Both protein peaks contained polyphenol oxidase (PPO) and peroxidase (POD) activities. The non-binding protein peak was resolved by gel filtration on Sephadex G-200 into distinct PPO and POD activities and by virtue of their apparent molecular weights of 95.5 Kd and 38.0 Kd for PPO and POD respectively were determined to be the typical enzymes. The PPO activity was completely inhibited invitro by 5 mᴍ polyvinyl pyrrolidone (PVP). The binding protein peak was not resolved by gel filtration. It contained PPO activity which was not inhibited by PVP and a POD activity which was completely inhibited by dithiothreitol (DTT) This ionic protein peak contained 60% of total POD in the tissue, has an apparent molecular weight of 56 Kd and is suggested to be a strongly anionic peroxidase which also exhibits polyphenol oxidase activity.

ANG II stimulates endothelial nitric oxide synthase expression in bovine pulmonary artery endothelium

Although angiotensin II (ANG II) is a known pulmonary vasoconstrictor, the purpose of this study was to examine the effect of ANG II on pulmonary artery endothelial cell nitric oxide synthase (ecNOS) mRNA and protein expression. Cultured bovine pulmonary artery endothelial (BPAE; passages 5-8) cells were incubated for 0-12 h with 10(-6) M ANG II. Total RNA was extracted, and ecNOS expression was assessed by Northern blot analysis. In BPAE cells, ecNOS mRNA was significantly increased 2.4 +/- 0.3-fold (P < 0.05 vs. basal; n = 5) 6 h after the addition of ANG II over basal levels. In & similar time course, it was found that ecNOS protein concentrations are increased 247 +/- 62% (P < 0.05 vs. basal; n = 8) over basal levels 4 h after ANG II addition. There is a second protein peak 8 h after ANG II addition in which ecNOS was increased 333 +/- 145% over basal (P < 0.05, n = 3). These data suggest that ANG II stimulates ecNOS mRNA expression and are followed by increased levels of ecNOS protein in cultured BPAE cells, consistent with an observed increase in nitrite production. Both the increase in ecNOS protein and mRNA expression could be inhibited with the ANG II receptor antagonist saralasin. Additionally, actinomycin D, an inhibitor of transcription, prevented the rise in mRNA at 6 h while cycloheximide inhibited the initial protein peak. The effects of ANG II on ecNOS were specific for the pulmonary artery endothelium. Addition of ANG II did not increase ecNOS protein or mRNA expression in parallel studies in bovine coronary artery endothelium. The stimulation of ecNOS by ANG II may act to protect the lung and maintain low pulmonary artery pressures in the renin-angiotensin model of systemic hypertension.