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S C Bose

Publications and source records attributed to S C Bose.

6 recordsLinked to original sources

Distribution of G-protein alpha subunits and neurotransmitter activation of g(alphai) and g(alphaq) in the brain of the lobster Homarus americanus.

Immunocytochemistry using antisera specific for the G-protein alpha subunits G(alphai), G(alphaq), and G(alphas) revealed similar patterns of immunoreactivity in the lobster brain. Immunoreactivity was strongest in neuropil, especially the olfactory and accessory lobes, and was characterized by bundles of fine threads leading to dense concentrations of punctate staining in the glomeruli. This may reflect the concentration of G-protein alpha subunits at synapses. The major differences between the antisera were distinct patterns of staining intensity in subregions of glomeruli of the olfactory and accessory lobes. This result is potentially correlated with previous evidence that these subregions are neurochemically distinct. Neuronal cell bodies contained moderate levels of immunoreactivity at the plasma membrane and faint staining in the cytoplasm. The olfactory globular tract was moderately immunoreactive, but other fiber tracts were weakly immunoreactive. Immunoreactivity in the deutocerebral commissure consisted of small oval cell bodies and strands that formed a reticulated pattern, suggestive of glia. Photoaffinity labelling by using an analog of GTP demonstrated that histamine activated G(alphai) in brain homogenates. Further evidence of G-protein activation was obtained by showing that stimulation with a mixture of neuroactive substances increased the amount of phospholipase C-beta associated with membranes, G(alphaq), and G(beta). The lobster brain, especially in its neuropil regions, is richly endowed with neuromodulatory biochemical pathways involving G(alphai), G(alphaq), and G(alphas).

Animals↗

Lobster G-protein coupled receptor kinase that associates with membranes and G(beta) in response to odorants and neurotransmitters.

A cDNA clone (lobGRK2) encoding a protein of 690 amino acids with significant similarity to the GRK2 subfamily of G-protein coupled receptor kinases was isolated. lobGRK2 was widely expressed as a 9-kb major transcript and a protein of 80 kDa. It was most abundant in the brain and the olfactory organ but was absent in the eye/eyestalk. Immunocytochemistry revealed lobGRK2 immunoreactivity in the outer dendritic segments of the olfactory receptor neurons, the site of olfactory transduction. LobGRK2 immunoreactivity was observed in most neuronal structures in the brain, although with varying intensity. It was strongest in neuropil, especially the olfactory and accessory lobes but was also detectable in neuronal cell bodies. Stimulation of brain homogenates with a mixture of neurotransmitters increased the association of lobGRK2 with membranes and with G(beta). Similarly, stimulation of olfactory dendrite homogenates with an odorant mixture caused lobGRK2 to associate with G(beta). These results support the conclusion that lobGRK2 responds to odorants and to neurotransmitters and may act to initiate desensitization by phosphorylating G-protein-coupled receptors in the olfactory organ and the brain, respectively.

Animals↗