73 research outputs found
Coexpression of vesicular glutamate transporters 1 and 2, glutamic acid decarboxylase and calretinin in rat entorhinal cortex
We studied the distribution and coexpression of vesicular glutamate transporters (VGluT1, VGluT2), glutamic acid decarboxylase
(GAD) and calretinin (CR, calcium-binding protein) in rat entorhinal cortex, using immunofluorescence staining and multichannel
confocal laser scanning microscopy. Images were computer processed and subjected to automated 3D object recognition, colocalization
analysis and 3D reconstruction. Since the VGluTs (in contrast to CR and GAD) occurred in fibers and axon terminals only, we
focused our attention on these neuronal processes. An intense, punctate VGluT1-staining occurred everywhere in the entorhinal
cortex. Our computer program resolved these punctae as small 3D objects. Also VGluT2 showed a punctate immunostaining pattern,
yet with half the number of 3D objects per tissue volume compared with VGluT1, and with statistically significantly larger
3D objects. Both VGluTs were distributed homogeneously across cortical layers, with in MEA VGluT1 slightly more densely distributed
than in LEA. The distribution pattern and the size distribution of GAD 3D objects resembled that of VGluT2. CR-immunopositive
fibers were abundant in all cortical layers. In double-stained sections we noted ample colocalization of CR and VGluT2, whereas
coexpression of CR and VGluT1 was nearly absent. Also in triple-staining experiments (VGluT2, GAD and CR combined) we noted
coexpression of VGluT2 and CR and, in addition, frequent coexpression of GAD and CR. Modest colocalization occurred of VGluT2
and GAD, and incidental colocalization of all three markers. We conclude that the CR-containing axon terminals in the entorhinal
cortex belong to at least two subpopulations of CR-neurons: a glutamatergic excitatory and a GABAergic inhibitory
PKR deficiency alters E. coli-induced sickness behaviors but does not exacerbate neuroimmune responses or bacterial load
Nicotinic acetylcholine receptors in attention circuitry: the role of layer VI neurons of prefrontal cortex
Spectroscopic investigations of Panulirus interruptus hemocyanin in the crystalline state
The structure of arthropod hemocyanins
Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly striking in the second domain of the subunit that contains the six histidines which ligate the two oxygen-binding copper atoms. The polypeptide architecture of spiny lobster hemocyanin appears to be the same in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, about 540 to 600 million years ago
Primary structure of the neutral carbohydrate chains of hemocyanin from Panulirus interruptus
Identification of two antibody-interaction sites on the surface of Panulirus interruptus hemocyanin
Primary and tertiary structures of the first domain of Panulirus interruptus hemocyanin and comparison of arthropod hemocyanins
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