High impact information on Maclura

• The conformation of the T-antigen disaccharide bound to Maclura pomifera agglutinin in aqueous solution [1].
• Identification of a 185 kd Maclura pomifera agglutinin binding glycoprotein as a candidate for a differentiation marker for alveolar type II cells in adult rat lung [2].
• Maclura pomifera lectin was used to determine the total amount of IgA1 present on the blots [3].
• Pro-SP-C preferentially co-localized to cells that stained positive for Maclura pomifera antigen [4].
• The type II cell Maclura pomifera agglutinin (MPA)-binding glycoprotein, MPA-gp200, appears to be expressed in an incompletely glycosylated form, whereas other features of differentiated type II cells, such as lamellar bodies, surfactant protein A, and a high percentage of saturated phosphatidylcholine, are absent [5].

Anatomical context of Maclura

• The sugar-specific staining in microvilli areas, where Maclura pomifera agglutinin (MPA)-gold particles bind, indicates the presence of galactose derivatives in these membrane structures [6].
• Studies of tissue sections using the galactose-specific, FITC-conjugated Maclura Pomifera lectin (MPA) demonstrated preferential binding to the superficial layers of intact urothelium [7].
• In the early S-shaped bodies, binding of Maclura pomifera (MPA; specific for galactosaminyl residues of glycoconjugates) could be detected in the presumptive podocyte layer at the apex of these cells, but notably no binding of lectins specific for sialic acid could be seen [8].
• Of twenty lectins tested, eight (Concanavalin A- Con A, Lathyrus odoratus- LOA, Lens culinaris, Pisum sativum-PSA, Vicia faba- VFA, Triticum vulgaris, Maclura pomifera- MPA and Ulex europaeus) specifically reacted with the salivary gland membrane [9].
• Five lectins (from Ricinus communis (RCA-I), Maclura pomifera (MPA), Triticum vulgare (wheat germ-WGA), Bauhinia purpurea (BPA), and Ulex europeus (UEA-I] reacted differentially with the epithelium of pregnant as compared with the non-pregnant uterus [10].

Associations of Maclura with chemical compounds

• Quantitative inhibition assays showing methyl-alpha-D-galactopyranoside and N-acetyl-D-galactosamine to be potent inhibitors of Maclura lectin precipitation by S. telaviv O polysaccharide suggest that the interaction is mediated by D-galactose or N-acetyl-D-galactosamine units of bacterial polysaccharide structure, or both [11].
• Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom [12].
• A reinvestigation of the constituents of the Osage orange (maclura pomifera) yielded, in addition to the previously reported triterpenses (lupeol, butyrospermol, and lupan-3beta,20-diol), the pigments osajin and pomiferin, and a previously unreported constituent [13].
• Five prenylated flavonoids, including one new natural product, were isolated from an ethanol extract of the leaves of Maclura tinctoria (L.) Gaud [14].
• It also cross-reacted with an antibody against the lectin of Osage Orange (Maclura pomifera) [15].

Gene context of Maclura

• This non-invasive transfer of cell sheet resulted in shrinkage of the monolayer, enabling the type II cells to regain their cuboidal morphology and specialized characters like Maclura pomifera lectin binding and surfactant protein A (SP-A) expression [16].
• Antioxidant isoflavones in Osage orange, Maclura pomifera (Raf.) Schneid [17].
• The HSM-Tn completely precipitated Vicia villosa (VVL both B4 and mixture of A and B), Maclura pomifera (MPL), and Artocarpus integrifolia (Jacalin) lectins; less than 2 micrograms of HSM-Tn were required for precipitating 50% of 5.0-6.3 micrograms lectin nitrogen added [18].
• The use of the Thomsen-Friedenreich antigen-specific lectins, jacalin, mushroom and Maclura pomifera agglutinin proved the most useful for ABO reverse grouping [19].
• In severely injured pulmonary parenchyma MEP-1-negative areas occurred, which were also negative with the type II pneumocyte marker Maclura pomifera lectin [20].

References