Expression of a Ca2+/calmodulin-dependent protein kinase, CaM kinase-Gr, in human T lymphocytes. Regulation of kinase activity by T cell receptor signaling.

Ca2+/calmodulin-dependent protein kinase type Gr (CaM kinase-Gr) is a Ca2+/calmodulin-dependent protein kinase which is enriched in the brain and thymus. In this study, we examined the expression of CaM kinase-Gr in human lymphocytes and the regulation of its catalytic activity by antigen receptor signaling. CaM kinase-Gr was found selectively expressed in T lymphocytes in a developmentally regulated manner.

Expression of a neuronal Ca2+/calmodulin-dependent protein kinase, CaM kinase-Gr, in rat thymus.

The regional and tissue-specific expression of the Ca2+/calmodulin-dependent protein kinase, CaM kinase-Gr, were examined. The Mr 65,000 alpha-polypeptide of CaM kinase-Gr is expressed ubiquitously in different anatomical regions of rat brain, whereas an additional Mr 67,000 beta-polypeptide is observed solely in the cerebellum. The alpha-polypeptide appears in the neonatal rat forebrain and cerebellum, whereas the beta-polypeptide appears by the second postnatal week and may reflect cerebellar granule cell differentiation.

A brain-specific Ca2+/calmodulin-dependent protein kinase (CaM kinase-Gr) is regulated by autophosphorylation. Relevance to neuronal Ca2+ signaling.

A neuronal Ca2+/calmodulin-dependent protein kinase (CaM kinase-Gr) undergoes autophosphorylation on a serine residue(s) in response to Ca2+ and calmodulin. Phosphate incorporation leads to the formation of a Ca(2+)-independent (autonomous) activity state, as well as potentiation of the Ca2+/calmodulin-dependent response. The autonomous enzyme activity of the phosphorylated enzyme approximately equals the Ca2+/calmodulin-stimulated activity of the unphosphorylated enzyme, but displays diminished affinity toward ATP and the synthetic substrate, syntide-2.

Furosemide- and bumetanide-sensitive ion transport and volume control in primary astrocyte cultures from rat brain.

K+ and Cl- transport using 42K+ and 36Cl- was studied in primary astrocyte cultures prepared from neonatal rat brains. A component of 42K+ uptake was sensitive to both furosemide and bumetanide with maximum inhibition being obtained at 1 and 0.01 mM concentrations of the inhibitors, respectively.

Desensitization of beta-receptors on primary astrocyte cultures by norepinephrine but not by tricyclic antidepressants.

Primary astrocyte cultures from neonatal rat cerebral hemispheres were treated chronically for up to 3 weeks with the tricyclic antidepressants amitryptyline (AMT) or desipramine (DMI), or acutely with AMT and DMI added at the same time as the agonist, norepinephrine (NE). AMT and DMI were added at concentrations from 10(-9) to 10(-5) M. Both types of treatment did not decrease the increase in cyclic AMP (cAMP) content of these cells in response to a 10 min exposure to 10(-5) M NE.