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PubMed1993

Parvalbumin-immunoreactive structures of the adult human entorhinal and transentorhinal region.

Parvalbumin-immunoreactive structures in the entorhinal and transentorhinal region of the adult human brain were studied using the avidin-biotin-peroxidase technique. Parvalbumin-immunoreactive neurons and fibers (axons) were present in all layers (layer nomenclature according to Rose, 1927). The density of fibers was high in the islands of the superficial cell layer pre-alpha and in layer pre-beta and still heavier in pre-gamma. In the subjacent lamina dissecans it diminished abruptly and remained low in all layers of the internal principal stratum (layers pri-alpha, -beta, -gamma). This low density of fibers facilitated recognition of axon cartridges in layers pri-alpha and pri-gamma. Axon cartridges were also present within layers pre-beta and pre-gamma but were obscured by the dense fiber network there. Parvalbumin immunoreactivity was observed in the nerve cell soma and throughout the dendritic tree allowing the distinction of numerous nerve cell types. All parvalbumin-immunoreactive neurons belonged to the class of nonpyramidal neurons. Their lipofuscin pigment patterns differed distinctly from that of the pyramidal and modified pyramidal neurons. Based on their location, soma size, and dendritic arborization, they were grouped as large, medium-sized, and small neurons either of the multipolar or bipolar (vertical or horizontal) type. One type could be identified as an axo-axonic neuron, more specifically as a chandelier neuron generating axon cartridges. The dense fiber net within layer pre-gamma suggested the existence of another neuronal type, probably a neuron with an extended axonal ramification. The identified neurons were compared to neuronal types described in the literature from Golgi studies.

Adult↗
PubMed1996

Intrathymic distribution of the two avian thymic parvalbumins.

Although parvalbumins are generally viewed as intracellular Ca2- buffers/transporters, avian species express two thymus-specific isoforms that may play alternative biological roles. These proteins, known as avian thymic hormone (ATH) and chicken parvalbumin 3 (CPV3), are conjectured to influence thymopoiesis. In this paper, we compare their intrathymic distributions. Isoform-specific monoclonal antibodies against ATH and CPV3 were labeled with fluorescein and Cy5, respectively, and then used to probe paraffin sections of chicken thymus tissue. Confocal microscopy of the stained sections reveals that ATH and CPV3 are both confined to the thymic cortex and that they are frequently coexpressed by a subset of epithelial cells. However, their expression patterns are not completely superimposible. Cortical epithelial cells are also observed that stain for just one of the two avian parvalbumin isoforms, albeit at lower frequency. Significantly, a subset of cortical thymocytes exhibits peripheral staining for one or both of the proteins. This result may imply the existence of plasma membrane receptors for the two proteins on select T-cell precursors. Alternatively, it may signal low level expression of the thymic parvalbumins by the thymocytes population.

Animals↗
PubMed1999

Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease.

GABA-interneurons immunoreactive (IR) for the calcium-binding protein parvalbumin are lost during the early stages of Creutzfeldt-Jakob disease (CJD) and diminution in their number may partially account for the neurological disturbances manifested in patients suffering from this condition. The disease is characterized by a transformation of the prion protein, PrP(c)-a host-coded sialoglycoprotein-to its protease-resistant and putatively pathological form, PrP(CJD). And since this conversion is likely to take place at the cell surface, we were curious to know whether the "perineuronal net"-a characteristic accumulation of extracellular matrix in intimate contact with the surface of parvalbumin-IR neurons-is implicated in the early disappearance of the mantled cells. Using various lectins and antibodies as markers for the perineuronal net in brains of 21 CJD victims, we observed that this meshwork of extracellular matrix molecules is lost before the embraced parvalbumin-IR neurons themselves disappear. Hence, an interaction of PrP(c) and/or PrP(CJD) with components of the extracellular matrix around this subpopulation of nerve cells precipitates a sequence of as yet unknown events which culminates in the replacement of perineuronal nets by deposits of insoluble PrP(CJD). This change in the environment of the GABA-interneurons IR for parvalbumin may ultimately provoke their death.

Aged↗
PubMed1985

Ultrastructural localization of the calcium-binding protein parvalbumin in neurons of the song system of the zebra finch, Poephila guttata.

The distribution of parvalbumin (PV) within neurons of the vocal motor nucleus hyperstriatum ventralepars caudalis (HVc) was investigated in the forebrain of adult male zebra finches by means of light and electron microscopy using the indirect immunoperoxidase technique. Parvalbumin-reaction product was located in the amorphous material of perikarya, dendrites and nuclei, and associated to microtubuli, postsynaptic densities and intracellular membranes; it was found in some axons and Gray type-2 boutons, but rarely in type-1 boutons and never in the Golgi apparatus. These observations suggest that parvalbumin may regulate calcium-dependent processes at the postsynaptic membrane and in the cytosol. Furthermore, the partial association of parvalbumin to microtubuli points to an involvement in calcium-dependent tubular functions. Calcium currents and microtubular assembly or transport may be relevant for the known functions of HVc in song learning.

Animals↗
PubMed1989

Localization of parvalbumin mRNA in rat brain by in situ hybridization histochemistry.

Parvalbumin mRNA was localized in rat brain by in situ hybridization using a 35S labelled rat parvalbumin cDNA and a synthetic oligodeoxyribonucleotide (corresponding to base sequences 140 to 183 of rat parvalbumin cDNA). Strongest hybridization signals were detected in the Purkinje cells of the cerebellum and in neurones of the reticular nucleus of the thalamus. Signal was also detected in the cerebral cortex, hippocampus, basal ganglia and brain stem in agreement with the distribution of parvalbumin immunoreactivity.

Animals↗
PubMed1991

Parvalbumin-immunoreactive structures in the hippocampus of the human adult.

Parvalbumin-immunoreactive structures in the fascia dentata and Ammon's horn of the adult human brain were studied using the avidin-biotin-peroxidase technique. Thin fibres (probably axons) were found to form dense networks throughout the cellular layers. Parvalbumin immunoreactivity is observed in even distal portions of nerve cell processes. The excellent quality of the immunoreaction renders the distinction of a large number of possible neuronal types. All parvalbumin-immunoreactive neurons belong to the class of non-granule cells in the fascia dentata and non-pyramidal neurons in Ammon's horn. The fascia dentata harbours four types of neurons in the molecular layer, one type within the granule cell layer and four types in the plexiform layer. The frequently described basket cells are contained in the group of immunoreactive non-granule cells in the plexiform layer. In field CA4 two neuronal types can be distinguished. Field CA3 reveals a slender cell type in the stratum radiatum, three types in the pyramidal cell layer and three types in the stratum oriens. In field CA2 three neuronal types can be differentiated in the stratum pyramidale. The extended field CA1 is endowed with two types of nerve cells within the stratum moleculare, two types in the stratum radiatum, five neuronal types in the stratum pyramidale, and one spindle-shaped type in the stratum oriens. The morphological features of parvalbumin-immunoreactive neuronal types in the adult human brain are compared with those found in Golgi-studies of mostly young animals or in labelling experiments. This study serves as a basis for further analyzes involving specific diseases such as Alzheimer's disease or epilepsy, where it needs to be clarified to which extent certain neuronal types are afflicted.

Adult↗
PubMed1992

Distribution of calbindin and parvalbumin in the developing somatosensory cortex and its primordium in the rat: an immunocytochemical study.

Immunocytochemical techniques were used to analyze the distribution of the calcium-binding proteins calbindin and parvalbumin during the pre- and postnatal development of the rat somatosensory cortex. Calbindin occurs in most early differentiated neurons that form the primordial plexiform layer at embryonic day 14. This expression in transient; during the perinatal period, calbindin becomes immunologically undetectable within the structures derived from the primordial plexiform layer, i.e., the prospective layers I and VIb. Immunoreactive neurons are also absent from adult layers I and VIb. Calbindin is also detected in a second population of neurons which, from embryonic day 18 onwards, distributes diffusely within the cortical plate. Some neurons of this population show morphological traits of immaturity, while others show complete dendritic arborization. The definitive pattern of distribution of calbindin-immunoreactive neurons is achieved by postnatal day 22. Infragranular layers contain intensely-immunoreactive cells whose numerical density decreases during postnatal development, whereas in supragranular layers similar neurons are interspersed among numerous faintly-stained neurons. Parvalbumin is detected for the first time at postnatal day 6, within a small group of neurons located in cortical layer V, and extends afterwards through the whole thickness of the cerebral cortex. At this same postnatal stage, groups of immunoreactive puncta are also found in layer IV of the somatosensory cortex; these puncta increase in density progressively and, at embryonic day 13, immunoreactive cells appear also grouped at this level. At this postnatal age, parvalbumin immunostaining delineates the somatosensory map in cortical layer IV. From this stage to adulthood, the number of immunoreactive neurons increases in the whole thickness of the somatosensory cortex. Barrels in layer IV become less distinct as immunoreactive cells and processes invade the septa. Layer IV in the adult somatosensory cortex appears more densely populated by parvalbumin immunoreactive neurons and puncta than in the surrounding areas.

Aging↗
PubMed1988

Calcium-binding parvalbumin in Drosophila testis in connection with in vivo irradiation.

Assuming a possible role of calcium in the function of the germinal proliferation centre in the testis of Drosophila melanogaster, the distribution of Ca2+-binding protein parvalbumin and structural related proteins in male gonads was tested by several biochemical and immunohistochemical methods. The two dimensional PAGE analysis on 3000 gonads of pupal stages suggests the presence of parvalbumin in this tissue. Immunohistochemical studies confirmed this finding. Parvalbumin-immunoreactivity was located in (or near) membraneous systems, like mitochondria and (or) microtubuli. The immunohistochemical analysis of irradiated gonads showed no radiation damage effect on the distribution of parvalbumin in certain cells and cell components.

Animals↗
PubMed1991

Parvalbumin in the cardiac muscle of normal and haemoglobin-myoglobin-free antarctic fish.

Three parvalbumin isotypes were isolated from the white muscle of haemoglobin-myoglobin-free antarctic fish Channichthys rhinoceratus. Antibodies against the parvalbumin mixture were raised in rabbits and used for discovery, quantitation and isolation by affinity chromatography of parvalbumin in the cardiac muscle of three antarctic fish species: Channichthys rhinoceratus, Champsocephalus gunnari and Notothenia neglecta. The cardiac muscle of these species contains parvalbumin in concentration close to 1 mumol per kg wet weight.

Animals↗
PubMed1995

Parvalbumin-immunoreactive proteins in the nervous system of planarians.

1. Using immunological methods, we have identified parvalbumin-like material in the triclade flatworms, Polycelis nigra, Polycelis auriculata, Crenobia alpina, Dugesia tahitiensis, and Dugesia polychroa. 2. Western immunoblot analysis of these five species revealed heat stable parvalbumin-immunoreactive proteins between 32 kD and 44 kD. 3. Proteins at 19 and 32 kD revealed intense labeling with 45Ca2+. 4. Double immunodiffusion of planarian supernatants showed complete fusion of precipitates, indicating immunological relatedness of the parvalbumin-like material among the species investigated. 5. Immunocytochemical studies exhibit parvalbumin-immunoreactive material exclusively in neurons supporting the notion of an early evolutionary appearance of these proteins in the nervous system.

Animals↗
PubMed1990

The parvalbumin-containing nonpyramidal neurons in the rat hippocampus.

The calcium-binding protein parvalbumin is considered to be involved in the control of intracellular ion homeostasis of highly active inhibitory neurons. A review of the light and electron microscopical features as well as the identified synaptic connections of these neurons is presented. Parvalbumin-containing neurons are mostly located within or in the vicinity of the granule or pyramidal cell layer. They form a subgroup of GABAergic neurons that has a target specificity for the cell body region. Their fine structural characteristics are identical to those known for hippocampal inhibitory neurons. Parvalbumin-containing neurons are involved in several inhibitory pathways: feed-back inhibition, feed-forward inhibition and disinhibition. The functional implications of our own as well as published data are discussed. Special consideration is given to the possible physiological role of parvalbumin in these neurons.

Animals↗
PubMed1998

Comparison of the rat dorsal and ventral striatopallidal system. A study using the GABA(A)-receptor alpha1-subunit and parvalbumin immunolabeling.

The ventral striatum is more closely related to limbic brain regions than the dorsal striatum in spite of the remarkable similarities in the structural organization between these two brain regions. The present study is focused on the comparison of ventral striatopallidal territories and the dorsal striatopallidal system regarding the GABA(A)-receptor alpha1-subunit and parvalbumin immunoreactivity, as these markers showed specific distribution patterns and coexpression sites in the more intensely studied dorsal regions. Our investigations revealed that: (1) Parvalbumin single-labeled cells and a moderate number of neurons single-labeled with the GABA(A)-receptor alpha1-subunit exist not only in the dorsal but also in the ventral striatum, including the striatal cell bridges. In addition, morphologically similar neurons positive for the alpha1-subunit were also found in the corpus callosum and anterior commissure. (2) A small number of double-labeled neurons was seen not only in dorsal but also in ventral striatal regions. Such cells were mainly located near the border with the globus pallidus and ventral pallidum. They are likely to represent a further type of striatal neuron. (3) The vast majority of neurons in the entopeduncular nucleus, the homologue of the primate internal globus pallidus segment, coexpressed alpha1-subunit and parvalbumin immunoreactivity, as reported previously for the other pallidal compartments. (4) The islands of Calleja adjoining the ventral pallidal extensions in the olfactory tubercle exhibited a strong alpha1-subunit immunoreactivity in the neuropil as well as somata single- or double-labeled for both markers. Our findings indicate that the dorsal and ventral striatopallidal compartments are similarly organized in general with respect to the occurrence and distribution of single- and double-labeled parvalbumin-immunoreactive and GABA(A)-receptor alpha1-subunit-immunoreactive neurons.

Animals↗
PubMed2000

Calcium-binding proteins calbindin D28K, calretinin, and parvalbumin immunoreactivity in the rabbit visual cortex.

The distribution and morphology of neurons containing three calcium-binding proteins, calbindin D28K, calretinin, and parvalbumin in the adult rabbit visual cortex were studied. The calcium-binding proteins were identified using antibody immunocytochemistry. Calbindin D28K-immunoreactive (IR) neurons were located throughout the cortical layers with the highest density in layer V. However, calbindin D28K-IR neurons were rarely encountered in layer I. Calretinin-IR neurons were mainly located in layers II and III. Considerably lower densities of calretinin-IR neurons were observed in the other layers. Parvalbumin-IR neurons were predominantly located in layers III, IV, V, and VI. In layers I and II, parvalbumin-IR neurons were only rarely seen. The majority of the calbindin D28K-IR neurons were stellate, round or oval cells with multipolar dendrites. The majority of calretinin-IR neurons were vertical fusiform cells with long processes traveling perpendicularly to the pial surface. The morphology of the majority of parvalbumin-IR neurons was similar to that of calbindin D28K: stellate, round or oval with multipolar dendrites. These results indicate that these three different calcium-binding proteins are contained in specific layers and cells in the rabbit visual cortex.

Animals↗
PubMed1983

Comparative study of physiochemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence.

Physicochemical properties of two pike parvalbumins (pI 5.0 and 4.2), belonging to two different gene lineages, have been studied by their intrinsic tyrosine and phenylalanine fluorescence. The CD sites of these paravalbumins have similar affinities to Ca2+ (and Mg2+) ions, but the EF sites of the proteins have very different affinities to these ions. This results in differing stabilities of these parvalbumins to pH-, urea-, and temperature-induced denaturation. The structure of pike parvalbumin pI 5.0, which binds Ca2+, and Mg2+ ions more tightly, is more stable than that of parvalbumin pI 4.2. Both proteins have higher affinities for Na+ ions than for K+ ions.

Animals↗
PubMed1984

Calmodulin and parvalbumin: activators of human liver glucocerebrosidase.

Lysosomal glucocerebrosidase of human tissues is reversibly inactivated by extraction with sodium cholate and n-butanol. Enzyme activity can be restored in the glucocerebrosidase assay by the incorporation of small amounts of phosphatidylserine (1 micrograms/assay) and a heat-stable factor obtained from the spleen of patients with Gaucher's disease. In the present report, we show that two heat-stable, low-molecular-weight, acidic, calcium-binding proteins, namely calmodulin and parvalbumin, are relatively potent activators of human liver glucocerebrosidase. A third structurally related, calcium-binding protein, troponin-C, does not stimulate glucocerebrosidase significantly. Removal of calcium from these proteins by treatment with 5 mM ethylene glycol bis(beta-aminoethylether)-N,N'-tetraacetic acid greatly decreases the quantity of material needed to stimulate enzyme activity. Parvalbumin stimulation of glucocerebrosidase activity is dependent on the presence of phosphatidylserine whereas the ability of calmodulin to activate the enzyme is not dependent on the acidic phospholipid. In terms of the level of glucocerebrosidase activity they support and under optimal conditions, parvalbumin and calmodulin are about 50 and 30%, respectively, as effective as the heat-stable factor from Gaucher spleen. On the other hand, on a molar basis, it takes about 35 times more parvalbumin than calmodulin to achieve maximum stimulation of glucocerebrosidase activity.

Calmodulin↗
PubMed1991

Differential sensitivity of calbindin and parvalbumin immunoreactive cells in the striatum to excitotoxins.

The neurotoxic effects of ibotenic acid, quinolinic acid and kainic acid on cells in the rat striatum were investigated using immunocytochemistry with antibodies to the calcium binding proteins, calbindin and parvalbumin. The results showed that both ibotenic acid and quinolinic acid affected calbindin and parvalbumin cells to the same extent. However, parvalbumin immunopositive neurons were more sensitive than calbindin immunopositive neurons to the neurotoxic effects of kainic acid. Although the reason for this increased sensitivity of parvalbumin striatal neurons to kainic acid is unclear, these results suggest that the neurotoxicity produced by kainic acid is different to that occurring with quinolinic acid and ibotenic acid.

Animals↗
PubMed1994

Neural parvalbumin and calretinin in the tooth pulp.

Parvalbumin- and calretinin-immunoreactivities (CR-irs) were examined in the molar tooth pulp of the rat using immunohistochemical methods. CR-ir fibers were further classified based on the tachykinin-ir revealed by a double immunofluorescence method. The rat root pulp contained three types of nerve fibers; parvalbumin-ir smooth fibers, CR-ir (TK-negative) smooth fibers and CR-ir (TK-ir) varicose fibers. These fibers projected toward the roof of the pulp chamber and pulp horn without marked ramification. In the subodontoblastic layer at the roof of the pulp chamber and pulp horn, parvalbumin-ir smooth fibers repeatedly ramified and extended varicose terminals into the odontoblastic layer. CR-ir (TK-negative) smooth fibers reached the subodontoblastic layer without marked ramification and gave rise to varicose terminals that appeared to terminate within the subodontoblastic layer. On the other hand, CR-ir (TK-ir) varicose fibers proceeded to the subodontoblastic layer at the roof of the pulp chamber and pulp horn, where they ramified and penetrated the odontoblastic layer. The present study indicates that the rat tooth pulp contains myelinated parvalbumin-ir and CR-ir (TK-negative) fibers, and unmyelinated CR-ir (TK-ir) fibers, and that they project varicose terminals to the subodontoblastic and odontoblastic layers. The central projection sites of these sensory fibers have yet to be revealed.

Animals↗
PubMed1995

Parvalbumin- and calretinin-immunoreactive trigeminal neurons innervating the rat molar tooth pulp.

Calcium-binding proteins and neuropeptides were examined in trigeminal neuronal cell bodies retrogradely labeled with Fast blue (FB) from the maxillary molar tooth pulp of the rat. FB-labeled cells were located in the maxillary division of the trigeminal ganglion. Approximately 30 and 50% of the labeled cells were immunoreactive for parvalbumin and calcitonin gene-related peptide (CGRP), respectively. The coexpression of these substances was observed in 9.5% of FB-labeled cells. On the other hand, 2.4% of FB-labeled cells exhibited calretinin-immunoreactivity (CR-ir) and 20% tachykinin (TK)-ir. The coexpression of CR and TK was observed in 1.9% of FB-labeled cells, i.e., most of CR-ir FB-labeled neurons coexpressed TK-ir. An immuno-EM method revealed that all parvalbumin-ir nerve fibers in the root pulp were myelinated and that CGRP-ir nerve fibers were both myelinated (15%) and unmyelinated (85%). The present study indicated that primary nociceptors innervating the rat molar tooth pulp contained parvalbumin and CR and coexpressed these calcium-binding proteins and neuropeptides. It was suggested that peripheral axons of parvalbumin-ir tooth pulp primary neurons are all myelinated. Most peripheral CR-ir axons are probably unmyelinated because TK-ir myelinated axons have never been demonstrated in any peripheral organ.

Animals↗