BIOMAT Database Logo BIOMAT Database Logo

Cellular localization of type II Ca2+/calmodulin-dependent protein kinase in the rat basal ganglia and intrastriatal grafts derived from fetal striatal primordia, in comparison with that of Ca2+/calmodulin-regulated protein phosphatase, calcineurin. 1994

S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Department of Neurosurgery, Kumamoto University Medical School, Japan.

We investigated immunohistochemically the cellular localization of multifunctional type II Ca2+/calmodulin-dependent protein kinase in the rat basal ganglia and intrastriatal grafts derived from fetal striatal primordia, in comparison with that of calcineurin, a reliable marker for striatal medium-sized spinous neurons. The type II Ca2+/calmodulin-dependent protein kinase-positive neurons were of medium size, with a mean diameter of 16.1 +/- microns (average +/- S.D., n = 72, range 13.6-18.3 microns) and comprised approximately 70% of the total neuronal population in the striatum. Light microscopy showed that the type II Ca2+/calmodulin-dependent protein kinase-positive cells had round, triangular or polygonal cell bodies with relatively little cytoplasm. Analysis of serial sections showed that type II Ca2+/calmodulin-dependent protein kinase and calcineurin immunoreactivities were co-localized in the striatal neurons examined with a similar distribution pattern. Type II Ca2+/calmodulin-dependent protein kinase-positive cells were always immunoreactive for calcineurin and cells negative for type II Ca2+/calmodulin-dependent protein kinase showed no apparent calcineurin immunoreactivity. Type II Ca2+/calmodulin-dependent protein kinase-positive nerve fibers in the globus pallidus and substantia nigra almost disappeared following striatal ischemic injury produced by transient middle cerebral artery occlusion and cerebral hemitransection, respectively, suggesting that these immunopositive fibers were striatal projections. Thus, most type II Ca2+/calmodulin-dependent protein kinase-positive neurons in the rat striatum are considered to be of the medium-sized spinous type. Type II Ca2+/calmodulin-dependent protein kinase or calcineurin immunoreactivity was also observed in a large number of neurons in transplants derived from fetal striatal primordia grafted into striatal ischemic lesions. In addition, type II Ca2+/calmodulin-dependent protein kinase- or calcineurin-immunoreactive nerve fibers appeared in the deafferented globus pallidus of the host rats, suggesting that the striatopallidal pathway was reformed by striatal projection neurons of the transplants. This finding may also indicate that Ca2+/calmodulin-regulated enzymes are useful for tracing striatal projection fibers as endogenous marker proteins.

UI MeSH Term Description Entries
D008297 Male Males
D009419 Nerve Tissue Proteins Proteins, Nerve Tissue,Tissue Proteins, Nerve
D009474 Neurons The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM. Nerve Cells,Cell, Nerve,Cells, Nerve,Nerve Cell,Neuron
D010749 Phosphoprotein Phosphatases A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase
D002148 Calmodulin-Binding Proteins Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases. Caldesmon,Calspectin,CaM-BP(80),Caldesmon (77),Calmodulin Binding Proteins,Proteins, Calmodulin-Binding
D002545 Brain Ischemia Localized reduction of blood flow to brain tissue due to arterial obstruction or systemic hypoperfusion. This frequently occurs in conjunction with brain hypoxia (HYPOXIA, BRAIN). Prolonged ischemia is associated with BRAIN INFARCTION. Cerebral Ischemia,Ischemic Encephalopathy,Encephalopathy, Ischemic,Ischemia, Cerebral,Brain Ischemias,Cerebral Ischemias,Ischemia, Brain,Ischemias, Cerebral,Ischemic Encephalopathies
D003342 Corpus Striatum Striped GRAY MATTER and WHITE MATTER consisting of the NEOSTRIATUM and paleostriatum (GLOBUS PALLIDUS). It is located in front of and lateral to the THALAMUS in each cerebral hemisphere. The gray substance is made up of the CAUDATE NUCLEUS and the lentiform nucleus (the latter consisting of the GLOBUS PALLIDUS and PUTAMEN). The WHITE MATTER is the INTERNAL CAPSULE. Lenticular Nucleus,Lentiform Nucleus,Lentiform Nuclei,Nucleus Lentiformis,Lentiformis, Nucleus,Nuclei, Lentiform,Nucleus, Lenticular,Nucleus, Lentiform,Striatum, Corpus
D004525 Efferent Pathways Nerve structures through which impulses are conducted from a nerve center toward a peripheral site. Such impulses are conducted via efferent neurons (NEURONS, EFFERENT), such as MOTOR NEURONS, autonomic neurons, and hypophyseal neurons. Motor Pathways,Efferent Pathway,Pathway, Efferent,Pathways, Efferent
D005917 Globus Pallidus The representation of the phylogenetically oldest part of the corpus striatum called the paleostriatum. It forms the smaller, more medial part of the lentiform nucleus. Paleostriatum,Pallidum,Pallidums
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Cellular reaggregation in vivo: modular patterns in intrastriatal grafts derived from fetal striatal primordia.
January 1990, Progress in brain research,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Intrastriatal grafts derived from fetal striatal primordia: II. Reconstitution of cholinergic and dopaminergic systems.
May 1990, The Journal of comparative neurology,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Intrastriatal grafts derived from fetal striatal primordia. I. Phenotypy and modular organization.
September 1989, The Journal of neuroscience : the official journal of the Society for Neuroscience,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Haloperidol induces Fos and related molecules in intrastriatal grafts derived from fetal striatal primordia.
October 1990, Brain research,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Ca2+/calmodulin-dependent protein kinase II in the rat cranial sensory ganglia.
April 2004, Brain research,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Intrastriatal grafts derived from fetal striatal primordia--IV. Host and donor neurons are not intermixed.
July 1993, Neuroscience,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Phosphorylation and activation of Ca2+/calmodulin-dependent protein kinase phosphatase by Ca2+/calmodulin-dependent protein kinase II.
August 1999, FEBS letters,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
A novel protein phosphatase that dephosphorylates and regulates Ca2+/calmodulin-dependent protein kinase II.
January 1998, The Journal of biological chemistry,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Immunohistochemical localization of Ca2+/calmodulin-dependent protein kinase II in the rat retina.
January 1994, Brain research,
S Goto, and K Yamada, and T Oyama, and K Korematsu, and S Nagahiro, and Y Ushio, and K Fukunaga, and E Miyamoto, and W Hofer
Intrastriatal grafts derived from fetal striatal primordia. III. Induction of modular patterns of fos-like immunoreactivity by cocaine.
January 1991, Experimental brain research,
Copied contents to your clipboard!