Influence of edapho-climatic factors on the sporulation and colonization of arbuscular mycorrhizal fungi in two Amazonian native fruit species

Arbuscular mycorrhizal fungi (AMF) colonization and spore numbers in the rhizosphere of two fruit species, Paullinia cupana Mart. and Theobroma grandiflorum Schum., growing in a terra firme ecosystem in Central Amazonia were studied from August 1998 to May 2000. Climatic and edaphic factors were also determined to investigate their influence on mycorrhizal variables. Soil pH, Al, Mn and effective cation exchange capacity exhibited seasonal variations during the investigation period. Temporal variations in mycorrhizal colonization levels and spore numbers occurred, indicating seasonality. Moreover, the patterns of mycorrhizal colonization levels and spore numbers for both host species were similar during the studied period. Mycorrhizal variables were related to climatic and edaphic factors, however, the intensity and type of influence of climatic and soil characteristics on AMF development tended to vary with the season and host plant species in Central Amazonia conditions

The partitioning of carbon in mycorrhizal plants grown at elevated atmospheric CO_2 concentration

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Nonreceptor Tyrosine Kinase c-Yes Interacts with Occludin during Tight Junction Formation in Canine Kidney Epithelial Cells

Occludin is an integral membrane protein that is tyrosine phosphorylated when localized at tight junctions. When Ca(2+) was depleted from the culture medium, occludin tyrosine phosphorylation was diminished from Madin-Darby canine kidney epithelial cells in 2 min. This dephosphorylation was correlated with a significant reduction in transepithelial electrical resistance (TER), indicating a global loss of the tight junction barrier function. Reconstitution of Ca(2+) resulted in a robust tyrosine rephosphorylation of occludin that was temporally associated with an increase in TER. Moreover, we demonstrate in this study that occludin was colocalized with the nonreceptor tyrosine kinase c-Yes at cell junction areas and formed an immunoprecipitable complex with c-Yes in vivo. This complex dissociated when the cells were incubated in medium without Ca(2+) or treated with a c-Yes inhibitor, CGP77675. In the presence of CGP77675 after Ca(2+) repletion, occludin tyrosine phosphorylation was completely abolished and both tight junction formation and the increase of the TER were inhibited. Our study thus provides strong evidence that occludin tyrosine phosphorylation is tightly linked to tight junction formation in epithelial cells, and that the nonreceptor tyrosine kinase c-Yes is involved in the regulation of this process