High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif.

The RGD tripeptide sequence, a cell adhesion motif present in several extracellular matrix proteins of mammalians, is involved in numerous plant processes. In plant-pathogen interactions, the RGD motif is believed to reduce plant defence responses by disrupting adhesions between the cell wall and plasma membrane. Photoaffinity cross-linking of [125I]-azido-RGD heptapeptide in the presence of purified plasma membrane vesicles of Arabidopsis thaliana led to label incorporation into a single protein with an apparent molecular mass of 80 kDa.

[Use of the Fibroxy mask for bronchial fibroscopy and resuscitation].

Bronchial fibrescopy in intensive therapy patients raises the problem of oxygenation during the procedure. The Fibroxy mask allows fibrescopy with simultaneous O2 administration and manual or mechanical ventilation. This study, which included ten patients, assessed the benefits of this device.

High affinity RGD-binding sites at the plasma membrane of Arabidopsis thaliana links the cell wall.

The heptapeptide Tyr-Gly-Arg-Gly-Asp-Ser-Pro containing the sequence Arg-Gly-Asp (RGD--the essential structure recognised by animal cells in substrate adhesion molecules) was tested on epidermal cells of onion and cultured cells of Arabidopsis upon plasmolysis. Dramatic changes were observed on both types of cells following treatment: on onion cells, Hechtian strands linking the cell wall to the membrane were lost, while Arabidopsis cells changed from concave to convex plasmolysis. A control heptapeptide Tyr-Gly-Asp-Gly-Arg-Ser-Pro had no effect on the shape of plasmolysed cells.