14 research outputs found
The PKD1 family of proteins as exemplified by the 10 SpREJs and five hPKD1 protein architectures
<p><b>Copyright information:</b></p><p>Taken from "The 10 sea urchin receptor for egg jelly proteins (SpREJ) are members of the polycystic kidney disease-1 (PKD1) family"</p><p>http://www.biomedcentral.com/1471-2164/8/235</p><p>BMC Genomics 2007;8():235-235.</p><p>Published online 13 Jul 2007</p><p>PMCID:PMC1934368.</p><p></p> The predicted secondary structures are shown. Domain boundaries were taken from the Pfam database. The REJ domain is split into two sections in SpREJ7 and partial REJ domains occur in SpREJ8 and 9, and hPKD1L2. hPKD1L3 does not contain a REJ domain. Most of these predicted structures show a GPS domain upstream of transmembrane helix 1 (TM1) and a PLAT/LH2 domain immediately after the first TM
自然と科学 後期(第2章 自然と科学,III. サイエンスリテラシープロジェクトII -問題発見・解決型の学習を通して多元的な思考力と探究心を育む-)
2010-01-25数学・社会(歴史)・理科(物理)の教員により、三つのグループに分かれて行う授業である。ここでは、科学的思考を身近で体験するためのアプローチとして、数学的・理科的・社会科学的観点から三つのグループに分かれ、様々な観点から科学的リテラシーを身につけさせるための授業を展開している。departmental bulletin pape
LC/MS<sup>n</sup> structural analysis of HNK-1 epitope on aggrecan.
<p>(A) PA-labeled <i>O</i>-linked glycans were prepared from aggrecan-Fc co-expressed with HNK-1ST in COS-1 cells. The base peak chromatogram of the glycans was obtained using selected ion monitoring (SIM) (<i>m/z</i> 782.5–832.5) in the negative ion mode (<i>upper panel</i>). An extracted ion chromatogram (EIC) of the ion at <i>m/z</i> 807.0–807.4 (<i>lower panel</i>). (B) MS/MS spectra (<i>upper panel</i>) of the ion [M-H]<sup>-</sup> (<i>m/z</i> 807.2) detected in peak A and MS/MS/MS spectra (<i>lower panel</i>) of the predominant product ion (<i>m/z</i> 727.2) in the MS/MS. S, sulfate group; HexA, hexuronic acid; Hex, hexose; Xyl-PA, xylose labeled with 2-aminopyridine.</p
Expression of a novel HNK-1 epitope on aggrecan in COS-1 cells.
<p>(A) Schematic diagram of the Fc-tagged short aggrecan used in this study. (B) Aggrecan-Fc with or without HNK-1ST was heterologously expressed into COS-1 cells. Aggrecan-Fc in the culture medium was purified using a Protein G Sepharose column and digested with 100 μU/ml chABC and then blotted with anti-Fc pAb, HNK-1 mAb and anti-CS antibodies (CS56 and clone IIH6). (C) Aggrecan-Fc and/or phosphacan-myc-Fc were transiently expressed with HNK-1ST-EGFP into COS-1 cells. Aggrecan-Fc and phosphacan-myc-Fc in the culture medium were precipitated with ethanol and digested with 200 μU/ml chABC, subjected to SDS-PAGE and then blotted with anti-Fc pAb, HNK-1 mAb, aggrecan pAb and phosphacan pAb.</p
HNK-1 carbohydrate and aggrecan are expressed in the PNNs.
<p>Sagittal sections of cerebral cortex from 6-week-old WT (A-C) and PKO mice (D-L) were singly (for WT) or doubly (for PKO) immunostained with HNK-1 mAb (A, D), 6B4 mAb (B, G), or Cat-315 mAb (C, J), and aggrecan pAb (E, H, K). F, I and L are overlaid images. High magnification images of HNK-1-, 6B4- or Cat-315- and aggrecan-positive PNNs are shown in the insets. Scale bars, 200 μm (A-C), 100 μm (D-L) and 20 μm (insets).</p
Biosynthetic model for HNK-1 epitope on aggrecan in PNNs.
<p>GlcAT-I is responsible for synthesis of a linkage region of GAG, which is usually further elongated into a long GAG chain (e.g., CS chain). HNK-1ST transfers a sulfate group to GlcA of the linkage region of aggrecan, which likely results in the expression of the linkage type HNK-1 epitope, HSO<sub>3</sub>-GlcA-Gal-Gal-Xyl, in PNNs. The expression of the HNK-1 epitope on aggrecan suppresses the CS polymerization that starts from GlcA of the linkage region.</p
