No abstract

The ileal apical sodium-dependent bile acid cotransporter (ASBT) plays an essential role in the absorption of bile acids from intestinal lumina. ASBT cDNA has been cloned from mammalian and fish species, and the primary structure of the protein and expression properties of the mRNA have been characterized. In this study, we identified chicken ASBT mRNA by cDNA cloning. Chicken ASBT cDNA consisted of 91 bp of the 5'-untranslated region, 1,083 bp of the coding region, and 1,896 bp of the 3'-untranslated region. The cDNA encoded a protein of 360 amino acids showing significant sequence identity with mammalian and fish ASBT. The amino acid residues known to participate in the functions of mammalian ASBT were conserved in chicken ASBT. Real-time polymerase chain reaction analysis revealed that chicken ASBT mRNA was expressed at markedly higher levels in the ileum and proximal colon/rectum, relatively lower levels in the kidney, and very low levels in the jejunum and cecum. Expression levels in the ileum markedly increased after hatching, reached the highest levels on day 7 posthatching, and then decreased to adult levels. A similar expression pattern was observed in the proximal colon/rectum except for the significant decrease from day 7 posthatching to day 21 posthatching. These results suggest that chicken ASBT functions as a bile acid transporter in the ileum and proximal colon/rectum, particularly during the early posthatching period.

This study aims to investigate the vasorelaxation effects of a Rosa centifolia petal extract (ROSE CRYSTA®-70: ROSE-70) on the isolated aorta and the protective effect of ROSE-70 on human umbilical vein endothelial cells (HUVECs) dysfunction. ROSE-70 inhibited phenylephrine (PE) -induced contraction in an endotheliumdependent and endothelium-independent manner; however, this relaxation was lower in the endothelium-denuded aorta. ROSE-70-induced relaxation was attenuated by L-N G -nitroarginine methyl ester (L-NAME), a nitric oxide synthase inhibitor in the endothelium-intact aorta. Moreover, the relaxation in the endothelium-denuded aorta in response to increases in cAMP was inhibited by SQ22536, an adenylate cyclase inhibitor, and this relaxation was also attenuated by 4-aminopyridine, a voltageactivated K + channel inhibitor. ROSE-70 contains high concentrations of quercetin, rutin, and other compounds. Pure quercetin and rutin also inhibited PE-induced contraction in an endothelium-dependent manner, although rutin-induced relaxation was milder in the endothelium-denuded aorta. ROSE-70 significantly increased the phosphorylation (at Ser1177) of eNOS in HUVECs. Moreover, ROSE-70 potently suppressed high glucose-and H 2 O 2 -induced accumulation of tumor necrosis factorα (TNFα) and nuclear factor-kappa B (NF-κB) were investigated in human umbilical vein endothelial cells (HUVECs). In this study, we defined the mechanism of ROSE-70-induced vasorelaxation in rat aorta and demonstrated that ROSE-70 has antiinflammatory effects in endothelial cells. Practical applicationsEndothelial cells play a role in vascular homeostasis. Endothelial dysfunction is caused by a variety of risk factors such as hypertension, arteriosclerosis, hyperglycemia, and oxidative stress. ROSE-70 is a food ingredient and the powdered form of an extract from the rose petal with >70% of the content corresponding to rose petal polyphenols such as rutin, quercetin, and protocatechuic acid. This study revealed that vasorelaxation effects of ROSE-70 and the protective role of ROSE-70 on the dysfunction of endothelial cells by high glucose and superoxides were investigated for the first

Extracellular vesicles (EVs) are biomarkers and mediators of intercellular communication. In biological samples, EVs are secreted by various types of cells. The proteomic identification of proteins expressed in EVs has potential to contribute to research and clinical applications, particularly for cancer. In this study, the proximity-labeling method-based proteomic approach was used for EV identification, labeling membrane components proximal to a given molecule on the EV membrane surface. Due to the small labeling range, proteins on the surface of the same EVs are likely to be labeled by selecting a given EV surface antigen. The protein group of cancer cell-secreted EV (cEV), which abundantly expresses a close homologue of L1 (CHL1), was examined using a model mouse for lung cancer (LC). cEV-expressed proteins were identified by proteomic analysis of enzyme-mediated activation of radical sources by comparing serum EVs from wild-type and LC mice. SLC4A1 was found to be co-expressed in CHL1-expressing EVs, highlighting EVs expressing both CHL1 and SLC4A1 as candidates for cEVs. Serum EVs expressing both CHL1 and caspase 14 were significantly elevated in LC patients compared with healthy individuals. Thus, the combination of proximity labeling and proteomic analysis allows for effective EV identification.