High resolution channeling contrast microscopy and channeling analysis of SiGe quantum well structures

High resolution channeling contrast microscopy (CCM) and channeling measurements were carried out to characterize SiGe quantum well structures on micron thick graded layers (i.e. virtual substrates). The virtual substrates were grown by gas source molecular beam epitaxy at a pressure of 10⁻⁵ mbar and low pressure chemical vapor deposition at 10⁻² mbar on boron doped Si(0 0 1) substrates respectively. A homoepitaxial silicon buffer layer was grown prior to the deposition. The nominal structure is a 20 nm Si_0.75Ge_0.25 layer at the surface, followed by 10 nm pure Si, 500 nm Si_0.75Ge_0.25 and a 1000 nm thick graded SiGe (0–26%) layer. RBS was used to measure the depth profiles, and angular scans around the (1 0 0) axis were carried out to assess crystal and interface quality. CCM was used to acquire depth resolved images of micron-sized lateral inhomogenities (‘cross-hatch') present on both samples.     

Excitatory amino acid receptors in glial progenitor cells: molecular and functional properties

We have analyzed the molecular and biophysical properties of glutamate-gated channels in cells of the oligodendrocyte lineage, using both the CG-4 primary cell line (Louis et al: J. Neurosci. Res. 31:193-204, 1992a) and oligodendrocyte progenitors purified from the rat cerebral cortex. CG-4 progenitor cells, as well as primary progenitors, were stained with a specific anti-GABA antibody. In whole-cell patch-clamp recordings, rapid perfusion of the agonists L-glutamate, kainate, and AMPA produced rapidly desensitizing currents in CG-4 cells. NMDA was ineffective. Both rapidly desensitizing and steady-state components of responses to kainate were inhibited by the kainate/AMPA receptor antagonist CNQX. Northern blot analysis of total mRNA isolated from CG-4 cells revealed co-expression of both AMPA- and kainate-preferring glutamate receptor subunits. The activation of glutamate receptors in CG-4 cells caused a rapid and transient elevation of mRNAs for the immediate early gene NGFI-A.     

Signal transduction through the CD19 receptor during discrete developmental stages of human B-cell ontogeny

We present evidence that the CD19 receptor is functionally operative and transmits pleiotropic signals throughout the pro-B, pre-pre-B, pre-B, early B, and mature B cell stages of human B-cell ontogeny. The signaling ability of CD19 does not depend on the existence of a functional B-cell antigen receptor complex (ARC). In B-cell precursors (BCP) lacking a functional ARC, CD19 is physically and functionally associated with Src family protein tyrosine kinases (PTK). The engagement of the CD19 receptor on BCP with a high affinity anti-CD19 monoclonal antibody (mAb) or its homoconjugate rapidly activates the associated PTK and results in tyrosine phosphorylation of CD19. Moreover, this proximal PTK activation step triggers downstream stimulation of several different intracellular messenger systems. Remarkably, CD19 becomes rapidly phosphorylated on tyrosine residues upon engagement of several other surface receptors as well, suggesting that it may function as a common response element linked via tyrosine phosphorylation to multiple BCP/B-cell receptors and signaling pathways. Furthermore, in all B-lineage lymphoid cell populations, co-approximation of the receptors CD19 and CD72 (ligand for the CD5 T-cell receptor) generates a stronger signal than the engagement of either individual receptor. These convergent observations constitute a strong argument for an important regulatory function of CD19 in human BCP and prompt the hypothesis that the CD19 receptor may play an important role in cognate interactions between B- and T-lineage lymphoid compartments as well as the coordinate production of BCP at multiple stages of human B-cell ontogeny.