Shoko Kido

High prevalence of vitamin K and D deficiency and decreased BMD in inflammatory bowel disease.

SummaryVitamin K and D deficiency and decreased bone mineral density (BMD) were highly prevalent in patients with inflammatory bowel disease (IBD), especially Crohn’s disease (CD). Dietary intakes of these vitamins, however, were above the Japanese adequate intakes in IBD patients, suggesting that malabsorption is the basis for hypovitaminosis K and D and decreased BMD.IntroductionWe have studied the possible involvement of vitamin K and D deficiency in the pathogenesis of decreased BMD in IBD.MethodsSeventy patients with IBD were evaluated for their BMD; plasma levels of vitamin K; phylloquinone (PK), menaquinone-7 (MK-7), and 25OH-D; serum PTH, protein induced by vitamin K absence (PIVKA-II), and undercarboxylated osteocalcin (ucOC) levels; and their food intake.ResultsCompared with ulcerative colitis (UC) patients, CD patients had significantly lower plasma vitamin K and 25OH-D concentrations; significantly higher serum levels of PTH, PIVKA-II, and ucOC; and significantly lower BMD scores at almost all measurement sites. More IBD patients were vitamin K deficient in bone than in liver. Multiple regression analyses revealed that low plasma concentrations of vitamin K and 25OH-D were independent risk factors for low BMD and that they were associated with the patients’ fat intake, but not with their intake of these vitamins.ConclusionIBD patients have high prevalence of decreased BMD and vitamin K and D deficiency probably caused by malabsorption of these vitamins.

Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry.

The crystal structure of vitelline membrane outer layer protein I (VMO-I), which is isolated from the vitelline membrane outer layer of hens eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I.

CLONING AND SEQUENCING OF HEN MAGNUM CDNAS ENCODING VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I)

Two cDNAs encoding hen vitelline membrane outer layer protein I (VMO-I), which is classified as a new type of multi-beta-sheet assembly, were cloned and sequenced. Northern blot analysis using vmo-I cDNA as a probe showed the presence of three mRNA species. Strikingly, expression of these mRNAs was restricted to a specific region of the hen oviduct, the area joining the infundibulum to the magnum.

Characterization of progressive changes in ZPC of the vitelline membrane of quail oocyte following oviductal transport

The inner layer of the vitelline membrane of avian oocyte is equivalent to the zona pellucida of mammalian oocytes or to the vitelline envelope of amphibian oocytes. One of the two major glycoproteins in the inner layer of quail vitelline membrane, formerly called 33‐kDa glycoprotein, is homologous to mammalian ZPC, one of the components of zona pellucida. Quail ZPC is found to have different mobilities on SDS‐polyacrylamide gel electrophoresis depending on whether it is obtained from the preovulatory follicle or from the laid eggs. In order to characterize the progressive changes in the molecular size of quail ZPC during the oviductal transport, the inner layer isolated from the follicle was incubated in vivo in various regions of the oviduct and subjected to Western blot analysis with anti‐quail ZPC antiserum. The quail ZPC of the inner layer incubated in infundibulum reduced its apparent molecular weight, exhibiting the same electrophoretic mobility as that of laid eggs. The similar reduction in molecular weight was observed after the in vitro incubation of the inner layer with the extracts of infundibulum. From the comparison of the N‐terminal amino acid sequences, it was found that the first 26 residues of the quail ZPC in follicular oocytes are missing from the ZPC of laid eggs. In addition, lectin blot analysis suggested the modification of oligosaccharide chains during the oviductal transport. These results represent the first description in the avian oviduct of the presence of protease, which is similar to oviductin, a trypsin‐like protease involved in the hydrolysis of a major component of the vitelline envelope of amphibian oocytes. Mol. Reprod. Dev. 55:175–181, 2000.

Guar Foaming Albumin : A Low Molecular Mass Protein with High Foaming Activity and Foam Stability Isolated from Guar Meal

The water extract of guar meal ( Cyamopsis tetragonolobus) was examined for its foamability. Compared with egg white, the extract showed an extraordinary foam stability: no drainage after 3 h of standing in contrast to 65% drainage for egg white at the same protein concentration. The acid-precipitated protein from the extract was responsible for the high foamability and designated guar foaming albumin (GFA). The foaming activity of GFA was 20 times higher than that of egg white. GFA consisted of two subunits with molecular masses of 6 and 11 kDa linked to each other through disulfide bonds. The cleavage of disulfide bonds in GFA affected the foamability only slightly. GFA remarkably decreased the surface tension of water at low protein concentrations. Immunoblotting analysis demonstrated that GFA did not react to the antisera from allergic patients against plant food. These results suggest that GFA serves as an effective food additive in developing protein-stabilized foam.

Distribution and properties of water-soluble arabinogalactan proteins in vegetables.

先にキャベツ葉について著者らが開発した新しい水可溶性成分の抽出法を13種類の野菜に適応し, 得られた水可溶性成分の中に含まれるアラビノガラクタンプロテイン (AGP) の分子量分布と化学組成分析を行い, 以下のことが明らかになった。1) 試料として用いたすべての野菜には分子量の異なる2種のAGP (A-IおよびA-II) が存在する。また, これらA-IおよびA-IIの溶出パターンはタイプA [茎菜類, 淡色葉菜類, 果菜類, 豆類 (莢) および根菜類], タイプB [豆類 (種子) およびフキ (茎)] およびタイプC (緑色葉菜類) の三つに分類できる。これらのデータの比較検討から葉のA-IおよびA-IIの分布状態は緑化またはそれに伴う繊維化によって影響されていることが示唆された。2) 各野菜から分取したA-IおよびA-IIの化学的性質を分析した結果, A-Iは分子量20～60万, 中性糖含量75～85%, タンパク質含量15～25%であり, A-IIは分子量9～13万, 中性糖含量80～90%, タンパク質含量10～20%であることがわかった。A-IおよびA-IIの糖部分はいずれもアラビノースとガラクトースで構成されるアラビノガラクタンであり, A-IおよびA-IIともにそのガラクトース/アラビノースの比は野菜の種類により大きく変動した (0.5～2.0)。また, A-IおよびA-IIはいずれもAGPに特有なヒドロキシプロリンとセリンを含み, かつグリシンおよびアラニン含量が高い点で特徴的であるが, ヒドロキシプロリン含量は野菜の種類によって大きく変動した。