Neurochemical properties of enkephalinergic neurons in lumbar spinal dorsal horn revealed by preproenkephalin–green fluorescent protein transgenic mice
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J. Neurochem. (2010) 113 , 1555–1564. Abstract Enkephalin (ENK) has been implicated in nociceptive transmission in the spinal cord while its functional role is not clear because of difficulties in ideally visualizing ENKergic neurons. We thus developed preproenkephalin–green fluorescent protein transgenic mice to better identify ENKergic neurons. Real‐time reverse transcriptase‐polymerase chain reaction (RT‐PCR) together with immunohistochemistry and in situ hybridization were first employed to confirm the successful transgenic manipulation and its application in showing spinal ENKergic neurons. The proportions of ENKergic neurons in the spinal cord laminae I, II, III and IV–VI among dorsal horn neurons were 15.8 ± 3.1%, 39.5 ± 3.3%, 11.8 ± 1.9% and 10.7 ± 2.1%, respectively. Double labeling with other molecules was then performed to further clarify the neurochemical properties of spinal ENKergic neurons. GABA was found to exist in 42.9 ± 2.8% of ENKergic neurons that were mainly located in lamina I–III. The proportions of parvalbumin‐, calretinin‐, calbindin‐ and neuronal nitric oxide synthase‐positive cells among the ENKergic neurons were 5.2 ± 0.7%, 42.6 ± 2.3%, 25.8 ± 2.2% and 11.1 ± 1.6%, respectively. Compared with previously findings obtained with ENK antibody labeling, this line of newly generated mice can be a reliable tool for the study of specific spinal ENKergic neuronal population.Keywords:
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Parvalbumin, calretinin, and calbindin-D28k are calcium-binding proteins that are located in largely nonoverlapping neuronal populations in the brain. The authors studied the distribution of parvalbumin-, calretinin-, and calbindin-D28k-immunoreactive (ir) cells, fibers, terminals, and neuropil in the eight subfields of the human entorhinal cortex. The distribution of each of the three calcium-binding proteins largely followed the cytoarchitectonic borders of the eight entorhinal subfields, although the regional and laminar distributions of the three proteins were segregated rather than overlapping. The highest density of parvalbumin-ir neurons and terminals was found in the caudal and lateral subfields of the entorhinal cortex. Calretinin and calbindin-D28k immunoreactivities were high rostromedially, although a large number of calretinin and calbindin-D28k neurons were also found in the caudal subfields. All parvalbumin-ir cells had a morphological appearance of nonpyramidal neurons. Parvalbumin-ir terminals formed basket-like formations around unstained somata and cartridges, suggesting that parvalbumin neurons compose a subpopulation of gamma-aminobutyric acid (GABA)ergic basket cells and chandelier cells, respectively. Although calretinin and calbindin-D28k were also found in numerous nonpyramidal neurons, both were also located in pyramidal-shaped neurons in layers V and VI (calretinin) and in layers II and III (calbindin) of the entorhinal cortex, suggesting that they play roles in projection neurons as well. Moreover, the high density of nonpyramidal neurons containing calcium-binding proteins in layers II and III of the entorhinal cortex suggests that they form an integral component of a network that controls the entorhinal outputs to the hippocampus. Furthermore, the largely nonoverlapping distributions of the parvalbumin-, calretinin-, and calbindin-ir neuronal populations in the entorhinal cortex indicate that each of them may modulate a different subset of topographically organized entorhinal outputs.
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Entorhinal cortex
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Transient (computer programming)
Developmental Biology
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Lateral geniculate nucleus
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Colocalization
Medial geniculate body
Neuropil
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Nitric Oxide (NO) actively participates in the regulation of neuronal intracellular Ca(2+) levels by modulating the activity of various channels and receptors. To test the possibility that modulation of Ca(2+) buffer protein expression level by NO participates in this regulatory effect, we examined expression of calbindin-D28k, calretinin, and parvalbumin in the cerebellum of neuronal NO synthase knock-out (nNOS((-/-))) mice using immunohistochemistry. We observed that in the cerebellar cortex of the nNOS((-/-)) mice, expression of calbindin-D28k and parvalbumin were significantly increased while expression of calretinin was significantly decreased. These results suggest another mechanism by which NO can participate in the regulation of Ca(2+) homeostasis.
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Neocortex
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Parvalbumin, calretinin, and calbindin-D28k are calcium-binding proteins that are located in largely nonoverlapping neuronal populations in the brain. The authors studied the distribution of parvalbumin-, calretinin-, and calbindin-D28k–immunoreactive (ir) cells, fibers, terminals, and neuropil in the eight subfields of the human entorhinal cortex. The distribution of each of the three calcium-binding proteins largely followed the cytoarchitectonic borders of the eight entorhinal subfields, although the regional and laminar distributions of the three proteins were segregated rather than overlapping. The highest density of parvalbumin-ir neurons and terminals was found in the caudal and lateral subfields of the entorhinal cortex. Calretinin and calbindin-D28k immunoreactivities were high rostromedially, although a large number of calretinin and calbindin-D28k neurons were also found in the caudal subfields. All parvalbumin-ir cells had a morphological appearance of nonpyramidal neurons. Parvalbumin-ir terminals formed basket-like formations around unstained somata and cartridges, suggesting that parvalbumin neurons compose a subpopulation of gamma-aminobutyric acid (GABA)ergic basket cells and chandelier cells, respectively. Although calretinin and calbindin-D28k were also found in numerous nonpyramidal neurons, both were also located in pyramidal-shaped neurons in layers V and VI (calretinin) and in layers II and III (calbindin) of the entorhinal cortex, suggesting that they play roles in projection neurons as well. Moreover, the high density of nonpyramidal neurons containing calcium-binding proteins in layers II and III of the entorhinal cortex suggests that they form an integral component of a network that controls the entorhinal outputs to the hippocampus. Furthermore, the largely nonoverlapping distributions of the parvalbumin-, calretinin-, and calbindin-ir neuronal populations in the entorhinal cortex indicate that each of them may modulate a different subset of topographically organized entorhinal outputs. J. Comp. Neurol. 388:64–88, 1997. © 1997 Wiley-Liss, Inc.
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Introduction: The human nervous system consists of neurons that build neuron circuits in which interneurons also take part. They enable the communication between the central nervous system and the motor or sensor neurons. Also, they express proteins that bind calcium such as parvalbumin, calretinin and calbindin. Gangliosides are glycosphingolipids that can be found in tissues, but the biggest number of them is in the brain. They interact with receptors with the aim of regulating proliferation, apoptosis and differentiation. In the cell nucleus, they take part in balancing calcium ions. Deficiency in the synthesis of gangliosides and interneurons leads to neurological disorders. Goals: The aim of this study was to determine expression of interneurons in striatum of a genetically modified mouse B4Galnt1 (KO) and a wild type (WT) by using antibodies for parvalbumin, calbindin and calretinin interneurons, and to determine if there is a difference in the expression of interneurons between a wild type mouse and a genetically modified mouse. Materials and methods: In this research, brain tissue samples from a genetically modified mouse and a wild type of mouse were used. After determining the genotype, the animals were done away with, and the brains were cut on cryostat. An immunohistochemical analysis was carried out by using specific antibodies for parvalbumin, calbindin and calretinin interneuorns, and the results were analysed in two softwares: ImageJ and Statistica 12. Results: The expression of interneurons in the striatum of the genetically modified mouse was reduced in comparison with the expression of interneurons in the wild type mouse. The research confirmed that there is a statistically significant difference in expression of calbindin, but not parvalbumin and calretinin. Conclusion: These results confirm the theory that gangliosides serve as protein modulators that bind calcium and impact binding ligand properties. The disorders in the synthesis of gangliosides lead to a reduced expression of interneurons in the striatum.
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