Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Parvalbumins”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 397 records · Page 22Linked to original sources
PubMed2006

Assessment of calcium-binding proteins (Parvalbumin and Calbindin D-28K) and perineuronal nets in normal and scrapie-affected adult sheep brains.

Scrapie is a prion disease in small ruminants that manifests itself with neurological clinical signs amongst which are ataxia and tremors. These signs can be explained partially by an imbalance in central inhibitory innervation. The study of the brain's inhibitory neuronal GABAergic populations and of their extracellular matrix has been used to define, in part, the pathogenesis of human prion diseases and scrapie models in rodents. The brain's distribution of neuronal GABAergic subpopulations has been monitored carefully using, as markers, antibodies against the calcium binding proteins parvalbumin and calbindin D-28K. The distribution of this perineuronal net marker was evaluated by means of affinity histochemistry with W. floribunda agglutinin. These techniques were performed on the brains of nine scrapie-positive sheep and on four infection-free sheep. These animals had undergone previously a clinical follow-up as well as a lesion profile and an immunohistochemical profile of the scrapie-associated prion protein deposition in the brain. The study of calcium-binding proteins revealed an alteration of the parvalbumin positive GABAergic neuronal subpopulation. In scrapie-positive cases, a reduction in stained neuronal perykaria was observed, along with a marked reduction of neurite labelling. This finding was noticeable in regions such as the neocortex, particularly the motor frontal cortex, and was concomitant with a moderate PrPsc deposition and a mild degree of lesion. No changes were observed in the extracellular matrix study. The results of the present study provide a partial explanation for the mechanisms of scrapie clinical signs due to a disturbance of the parvalbumin-positive inhibitory neuronal population.

Animals↗
PubMed2004

Differential distribution of parvalbumin immunoreactive neurons in the striatum of cocaine sensitized rats.

Intermittent administration of psychostimulants such as cocaine and amphetamine can result in behavioral sensitization, which is believed to model the onset of drug addiction, as well as possible neural adaptations that lead to addictive behaviors. The dorsal striatum and the nucleus accumbens (NAc) have been shown to play an integral role in this phenomenon. However, these structures comprise a complex neuroanatomical organization, and few studies have correlated anatomical differentiation within these brain regions with functional (i.e. behavioral) outcome, particularly after psychostimulant exposure. Parvalbumin (PV)-containing GABAergic interneurons are a key neuronal cell population that can significantly regulate input-output functions in these brain regions. The present study quantified parvalbumin-immunoreactive cells in subterritories of the striatum and NAc in animals behaviorally sensitized to cocaine. Rats received a sensitization-inducing regimen of cocaine (twice-daily injections of 15 mg/kg i.p. for 5 consecutive days). Two or 14 days following the last injection, rats were given a challenge injection of cocaine (15 mg/kg i.p.), and killed 2 h later. Sections through the striatum (including the NAc) were processed for parvalbumin immunoreactivity, and the number of immunoreactive neurons was quantified. Repeated cocaine administration resulted in robust sensitization that correlated with transient increases in the number of PV immunoreactive neurons in the ventrolateral, dorsolateral and dorsomedial striatum. After a 2-week withdrawal period, sensitized animals showed a significant decrease in the number of PV+ neurons in the ventrolateral shell of the NAc and dorsomedial striatum, and no significant difference in any other area examined. These data suggest a dichotomous role for PV interneurons in different subterritories of the striatum and NAc during the short-term (induction) vs. long-term (expression) phases of cocaine sensitization.

Animals↗
PubMed2005

Circadian and light regulation of oxytocin and parvalbumin protein levels in the ciliated ependymal layer of the third ventricle in the C57 mouse.

The walls of the third ventricle have been proposed to serve as a bidirectional conduit for exchanges between the neural parenchyma and the cerebrospinal fluid. In immunohistochemical studies of mice, we observed that light exposure and circadian phase affected peptide staining surrounding the third ventricle at the level of the suprachiasmatic nuclei. Under high magnification, we observed robust staining for the neurohormone oxytocin and the calcium-binding protein parvalbumin associated with cilia extending into the third ventricle from the surrounding ventricular wall; no similar staining was observed for vasopressin or calbindin. Retinal illumination had opposite effects on levels of parvalbumin and oxytocin in the cilia: light exposure during late subjective night increased oxytocin staining, but decreased parvalbumin staining in the cilia. Preventing cellular transport with colchicine eliminated immunohistochemical staining for oxytocin in the cilia. There was also a significant daily rhythm of oxytocin immunostaining in the third ventricle wall, and in magnocellular neurons in the anterior hypothalamus. The results suggest that environmental lighting and circadian rhythms regulate levels of oxytocin in the cerebrospinal fluid, possibly by regulating movement of oxytocin through the third ventricle wall.

Animals↗
PubMed2005

A role for L-type calcium channels in the maturation of parvalbumin-containing hippocampal interneurons.

While inhibitory interneurons are well recognized to play critical roles in the brain, relatively little is know about the molecular events that regulate their growth and differentiation. Calcium ions are thought to be important in neuronal development and L-type voltage gated Ca(+2) channels have been implicated in activity-dependent mechanisms of early-life. However, few studies have examined the role of these channels in the maturation of interneurons. The studies reported here were conducted in hippocampal slice cultures and indicate that the L-type Ca(+2) channel agonists and antagonists accelerate and suppress respectively the growth of parvalbumin-containing interneurons. The effects of channel blockade were reversible suggesting they are not the result of interneuronal cell death. Results from immunoblotting showed that these drugs have similar effects on the expression of the GABA synthetic enzymes, glutamic acid decarboxylase65, glutamic acid decarboxylase67 and the vesicular GABA transporter. This suggests that L-type Ca(+2) channels regulate not only parvalbumin expression but also interneuron development. These effects are likely mediated by actions on the interneurons themselves since the alpha subunits of L-type channels, voltage-gated calcium channel subunit 1.2 and voltage-gated calcium channel subunit 1.3 were found to be highly expressed in neonatal mouse hippocampus and co-localized with parvalbumin in interneurons. Results also showed that while these interneurons can contain either subunit, voltage-gated calcium channel subunit 1.3 was more widely expressed. Taken together results suggest that an important subset of developing interneurons expresses L-type Ca(+2) channels alpha subunits, voltage-gated calcium channel subunit 1.2 and especially voltage-gated calcium channel subunit 1.3 and that these channels likely regulate the development of these interneurons in an activity-dependent manner.

Animals↗
PubMed1977

Non-cooperative Ca(II) removal and terbium(III) substitution in carp muscle calcium binding parvalbumin.

Close coorelation of atomic absorption measurements for Ca(II) contents indicates that from pH 5.8-7.4 a twentyfold excess of EGTA1 removes but one of two Ca(II) from carp parvalbumin. Thus binding of the two Ca(II) appears to be noncooperative. The maximum in emission intensity observed at a nonintegral 1.4-1.7 equivs of added Tb(III) is shown to be due to quenching by excess Tb(III). The emission intensity at the maximum increased 40% upon dialysis to remove Tb(III) not bound in the CD or EF sites. Atomic absorption results show that both Ca(CD) and Ca(EF) of native parvalbumin are easily replaced by Tb(III). Emission of Tb(EF) is not quenched by Tb(CD), but by solution Tb(III) bound at a third site, perhaps the single water molecule bound to Tb(EF). Labeling of the single sulfhydryl group with a trifluoroacetonyl gorup yields a protein with ultraviolet circular dichroism, emission, and circularly polarized emission spectra closely similar to those of native parvalbumin.

Animals↗
PubMed2002

Interspecific differences in the expression of the AMPA-type glutamate receptors and parvalbumin in the nucleus of Edinger-Westphal of chicks and pigeons.

The distribution of AMPA-type glutamate receptor (GluR) subunits was studied in the Edinger-Westphal nucleus (EW) of chicks and pigeons. GluR1, GluR2, GluR3 and GluR4 subunits appeared to be present in EW neurons of both species, but interspecific differences were observed in the abundance of the different types of subunits found in EW neurons. Of particular note, GluR2 immunoreactivity was present in the vast majority (ca. 80%) of neurons of pigeon EW but was found in only a small fraction (ca. 15%) of chick EW neurons. Scarcity of the GluR2 subunit in chick EW was confirmed by in situ hybridization. Because of the tendency for parvalbumin to be localized to neurons that are selectively deficient in GluR2, we also studied the localization of parvalbumin, as well as other calcium-binding proteins, in EW of chick and pigeon. Parvalbumin was found in more than 50% of chick EW neurons but was not detected in pigeon EW neurons. Our results suggest that there are major glutamatergic inputs to EW neurons in both pigeons and chicks. Furthermore, there are likely to be more AMPA-type calcium-permeable glutamate receptors in EW neurons of chick than in pigeon, since it is known that the subtype containing the edited GluR2 subunit is not calcium permeable.

Animals↗
PubMed1996

Differential age-dependent effects of retinal deafferentation upon calbindin- and parvalbumin-immunoreactive neurons in the superficial layers of the rat's superior colliculus.

Several recent studies have reported varied effects of different forms of visual deprivation on the expression of calcium-binding proteins in the CNS. Most of these studies have surveyed only a single protein from this family and have not systematically evaluated the influence of the age of the animal upon the effects observed. The present study combined immunocytochemistry and quantitative morphometry to determine the effects of eye removal in fetal life, at birth, or in adulthood upon the expression of calbindin and parvalbumin by neurons in the retinorecipient laminae (the stratum griseum superficiale (SGS) and stratum opticum (SO)) of the rat's superior colliculus (SC). Both fetal and neonatal enucleation significantly reduced the total number of neurons in the SGS. Eye removal at any age did not significantly affect the number of neurons in the SO or the proportion of SGS or SO cells that expressed calbindin. Adult enucleation produced a significant increase in the percentage of SGS cells expressing parvalbumin. These results suggest that calbindin expression is highly stable in visual neurons while parvalbumin expression is more plastic and appears to be suppressed by retinal input.

Age Factors↗
PubMed1997

Parvalbumin- and calbindin-containing neurons express c-fos protein in primary and secondary (mirror) epileptic foci of the rat neocortex.

The present experiments aimed at the description and further immunocytochemical characterization of activated neocortical neurons expressing the c-fos gene. Focal seizures were induced by the topical application of isotonic, isohydric 4-aminopyridine solution to the frontal neocortex of adult anesthetized Wistar rats. The EEG of both hemispheres was recorded from the surface of the skull. The animals were perfused with fixative, coronal plane vibratome sections were cut and stained with cocktails containing polyclonal c-fos and monoclonal calbindin or parvalbumin antibodies. The polyclonal c-fos antibody was tested with Western blotting and the diffusion of 4-aminopyridine investigated with autoradiography of [3H]4-aminopyridine. The c-fos protein was detected in every layer of the neocortex (primary focus) and in some allocortical areas of the treated hemisphere. Scattered immunostained nuclei were observed in layers II, III, IV and VI of the contralateral neocortex (mirror focus). Several parvalbumin- and calbindin-positive neurons contained the c-fos protein in both foci. The medium-sized non-pyramidal parvalbumin neurons were found in layers II-IV and VI of the neocortex and in stratum multiforme of the prepiriform cortex. The c-fos protein was colocalized with calbindin mainly in layers II and III in small and medium-sized non-pyramidal neurons. The results prove that focal epileptiform activity of the neocortex activates diverse inhibitory neuronal populations. As concluded, the inhibitory control is probably more effective in the contralateral hemisphere (mirror focus) than on the side of 4-APY treatment (primary focus).

Animals↗
PubMed1999

Conformational stabilities of the rat alpha- and beta-parvalbumins.

It is widely believed that beta-parvalbumin (PV) isoforms are intrinsically less stable than alpha-parvalbumins, due to greater electrostatic repulsion and an abbreviated C-terminal helix. However, when examined by differential scanning calorimetry, the apo-form of the rat beta-PV (i.e. oncomodulin) actually displays greater thermal stability than the alpha-PV. Whereas the melting temperature of the a isoform is 45.8 degrees C at physiological pH and ionic strength, the Tm for the beta isoform is more than 7 degrees higher (53.6 degrees C). This result suggests that factors besides net charge and C-terminal helix length strongly influence parvalbumin conformational stability. Extension of the F helix in the beta-PV, by insertion of Ser-109, has a modest stabilizing effect, raising the Tm, by 1.1 degrees. Truncation of the alpha-PV F helix, by removal of Glu-108, has a more profound impact, lowering the Tm by 4.0 degrees.

Animals↗
PubMedDate not supplied

Age-related changes of calbindin-D28k, calretinin, and parvalbumin mRNAs in the hamster brain.

Changes of three different cytosolic Ca2+ binding proteins, calbindin-D28k, calretinin, and parvalbumin mRNA expression in the brain of the hamster during aging were investigated by in situ hybridization using brains from hamsters aged 4, 9, 13, 19, to 24 months old. In cerebellum area, calbindin-D28k transcripts showed about 50% to 68% decrease in content in aged-hamster (19 and 24 months old) compared with young (4 months) and adult (9 months), whereas calretinin and parvalbumin mRNA expression remain unchanged throughout the ages examined. Calbindin-D28k gene expression was decreased during aging also in the hippocampus (approximately 60% reduction) and striatum (approximately 25%). In the same areas, striatum and hippocampus, calretinin and parvalbumin mRNA expression in the equivalent sections were not significantly changed with age. These data raise the possibility that CNS calbindin-D28k expression may be selectively down-regulated during aging. The statistically significant decrease of calbindin-D28k mRNA in the normal aging process also suggests and provides further support for the hypothesis that this calcium binding protein may have an important role in neuronal degeneration.

Aging↗
PubMed1979

Parvalbumins from the lungfish (Protopterus dolloi).

Five parvalbumins have been isolated from the white muscles of the lungfish. They can be divided into two sub families showing typical amino acid compositions, C-terminal amino acid residues, peptide maps and immuno-reactivity. The red muscles including the cardiac muscle also contain parvalbumins in amounts roughly inversely related to the concentration of myoglobin in the muscle. Parvalbumins have also been detected in the brain and kidney.

Amino Acids↗
PubMed1979

Calcium, magnesium and the conformation of parvalbumin during muscular activity.

The conformation of perch parvalbumin in the Ca-, Mg- and metal-free state was studied by intrinsic fluorescence, trypsin susceptibility, thiol titration and circular dichroism. The data reveal that Ca-parvalbumin has a more compact structure than the metal-free protein, with a high alpha-helical content and a buried thiol. No difference in conformation could be detected between Mg- and Ca-parvalvumin, indicating that the Ca-Mg exchange that may take place during muscular activity is accompanied by little or no structural changes. Furthermore, recently published kinetic parameters can now be interpreted as meaning that, during the contraction-relaxation cycle, parvalbumin often stays in the Mg-form instead of switching to the Ca-form which is predominant in vitro.

Calcium↗
PubMed1999

Subfield- and layer-specific changes in parvalbumin, calretinin and calbindin-D28K immunoreactivity in the entorhinal cortex in Alzheimer's disease.

The entorhinal cortex, which is involved in neural systems related to memory, is selectively degenerated in early Alzheimer's disease. Here, we examined neuropathological changes in the eight entorhinal subfields in post mortem Alzheimer's disease subjects using Thionin and Bielschowsky stains and parvalbumin, calretinin and calbindin-D28k immunohistochemistry. Both histological stains revealed the most dramatic cell loss and neurofibrillary tangle formation to be in layers II and V of the lateral, intermediate and caudal subfields. In accordance, immunohistochemical staining showed that neurons and fibres that contain calcium-binding proteins were also more frequently altered in these subfields than in the rostromedial subfields. Detailed analysis further revealed that non-principal cells containing parvalbumin or calbindin-D28k showed morphological alterations early in the entorhinal pathology of Alzheimer's disease, whereas non-principal neurons containing calretinin were better preserved even in Alzheimer's disease patients with severe entorhinal pathology. The degeneration of parvalbumin-immunoreactive neurons and basket-like networks and calbindin-positive non-principal neurons was observed mainly in layer II, where the calretinin-positive non-principal neurons formed aggregates especially at late stages of the disease. The pyramidal-shaped neurons containing either calretinin or calbindin-D28k were often preserved, although morphological alterations were observed. Our findings indicate that specific subfields of the entorhinal cortex involving neurons that contain distinct calcium-binding proteins are differentially vulnerable in Alzheimer's disease. This could have an impact on the topographically organized inputs and outputs of the entorhinal cortex in Alzheimer's patients.

Aged↗
PubMed2001

Distribution of calbindin, parvalbumin and calretinin in the lateral geniculate nucleus and superior colliculus in Cebus apella monkeys.

We studied the distribution of the calcium-binding proteins calbindin, parvalbumin and calretinin, in the superior colliculus and in the lateral geniculate nucleus of Cebus apella, a diurnal New World monkey. In the superior colliculus, these calcium-binding proteins show different distribution patterns throughout the layers. After reaction for calretinin one observes a heavy staining of the neuropil with few labeled cells in superficial layers, a greater number of large and medium-sized cells in the stratum griseum intermediale, and small neurons in deep layers. The reaction for calbindin revealed a strong staining of neuropil with a large number of small and well stained cells, mainly in the upper half of the stratum griseum superficiale. Intermediate layers were more weakly stained and depicted few neurons. There were few immunopositive cells and little neuropil staining in deep layers. The reaction for parvalbumin showed small and medium-sized neurons in the superficial layers, a predominance of large stellate cells in the stratum griseum intermediale, and medium-sized cells in the deep layers. In the lateral geniculate nucleus of Cebus, parvalbumin is found in the cells of both the P and M pathways, whereas calbindin is mainly found in the interlaminar and S layers, which are part of the third visual pathway. Calretinin was only found in cells located in layer S. This pattern is similar to that observed in Macaca, showing that these calcium-binding proteins reveal different components of the parallel visual pathways both in New and Old World monkeys.

Animals↗
PubMed1997

Colocalization of parvalbumin and calbindin D-28k in neurons including chandelier cells of the human temporal neocortex.

Chandelier cells are cortical GABAergic interneurons with a unique synaptic specificity enabling them to exert a strong inhibitory influence on pyramidal cells. By using immunocytochemistry for the calcium-binding protein calbindin D-28k in the human temporal neocortex, we have found numerous immunoreactive processes that were identified as chandelier cell axon terminals. This was a striking find since in previous immunocytochemical studies of the primate neocortex, chandelier cell axon terminals had been shown to be immunoreactive for another calcium-binding protein, parvalbumin, and colocalization studies indicate that parvalbumin and calbindin are present in almost completely separate neuronal populations. Here, we present double-label immunofluorescence experiments showing that parvalbumin and calbindin immunoreactivities are colocalized in certain neurons that include a subpopulation of chandelier cells whose cell bodies are located mainly in layers V and VI of the human temporal neocortex. The results suggest a selective laminar distribution of neurochemical subtypes of chandelier cells which is a peculiar feature of the organization of the human neocortex.

Adolescent↗
PubMed1999

Cellular distribution of the calcium-binding proteins parvalbumin, calbindin, and calretinin in the neocortex of mammals: phylogenetic and developmental patterns.

The three calcium-binding proteins parvalbumin, calbindin, and calretinin are found in morphologically distinct classes of inhibitory interneurons as well as in some pyramidal neurons in the mammalian neocortex. Although there is a wide variability in the qualitative and quantitative characteristics of the neocortical subpopulations of calcium-binding protein-immunoreactive neurons in mammals, most of the available data show that there is a fundamental similarity among the mammalian species investigated so far, in terms of the distribution of parvalbumin, calbindin, and calretinin across the depth of the neocortex. Thus, calbindin- and calretinin-immunoreactive neurons are predominant in layers II and III, but are present across all cortical layers, whereas parvalbumin-immunoreactive neurons are more prevalent in the middle and lower cortical layers. These different neuronal populations have well defined regional and laminar distribution, neurochemical characteristics and synaptic connections, and each of these cell types displays a particular developmental sequence. Most of the available data on the development, distribution and morphological characteristics of these calcium-binding proteins are from studies in common laboratory animals such as the rat, mouse, cat, macaque monkey, as well as from postmortem analyses in humans, but there are virtually no data on other species aside of a few incidental reports. In the context of the evolution of mammalian neocortex, the distribution and morphological characteristics of calcium-binding protein-immunoreactive neurons may help defining taxon-specific patterns that may be used as reliable phylogenetic traits. It would be interesting to extend such neurochemical analyses of neuronal subpopulations to other species to assess the degree to which neurochemical specialization of particular neuronal subtypes, as well as their regional and laminar distribution in the cerebral cortex, may represent sets of derived features in any given mammalian order. This could be particularly interesting in view of the consistent differences in neurochemical typology observed in considerably divergent orders such as cetaceans and certain families of insectivores and metatherians, as well as in monotremes. The present article provides an overview of calcium-binding protein distribution across a large number of representative mammalian species and a review of their developmental patterns in the species where data are available. This analysis demonstrates that while it is likely that the developmental patterns are quite consistent across species, at least based on the limited number of species for which ontogenetic data exist, the distribution and morphology of calcium-binding protein-containingneurons varies substantially among mammalian orders and that certain species show highly divergent patterns compared to closely related taxa. Interestingly, primates, carnivores, rodents and tree shrews appear closely related on the basis of the observed patterns, marsupials show some affinities with that group, whereas prototherians have unique patterns. Our findings also support the relationships of cetaceans and ungulates, and demonstrates possible affinities between carnivores and ungulates, as well as the existence of common, probably primitive, traits in cetaceans and insectivores.

Animals↗
PubMed1997

Parvalbumin-immunoreactive neurons are reduced in the prefrontal cortex of schizophrenics.

Recent studies have provided evidence for a functional impairment of gamma-aminobutyric acid (GABA)-containing interneurons in the prefrontal cortex of schizophrenics. This evidence includes reported deficits of basket and chandelier cells, which are known to contain the calcium-binding protein parvalbumin. Using a monoclonal antibody against parvalbumin we investigated possible changes in this subpopulation of neurons in the prefrontal cortex of schizophrenic cases and controls. Significantly reduced numbers of parvalbumin-immunoreactive neurons were observed in laminae III and IV, while no difference was detected in cortical width. Our findings are consistent with damage following a toxic insult, occurring during a developmental 'window of vulnerability' and specifically affecting this subpopulation of GABAergic neurons.

Aged↗
PubMed1999

Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin.

BACKGROUND: The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision. RESULTS: We have determined the structures of parvalbumin mutants designed to explore the role of the last coordinating residue of the Ca(2+)-binding loop. An E101D substitution has been made in the parvalbumin EF site. The substitution decreases the Ca(2+)-binding affinity 100-fold and increases the Mg(2+)-binding affinity 10-fold. Both the Ca(2+)- and Mg(2+)-bound structures have been determined, and a structural basis has been proposed for the metal-ion-binding properties. CONCLUSIONS: The E101D mutation does not affect the Mg(2+) coordination geometry of the binding loop, but it does pull the F helix 1.1 A towards the loop. The E101D-Ca(2+) structure reveals that this mutant cannot obtain the sevenfold coordination preferred by Ca(2+), presumably because of strain limits imposed by tertiary structure. Analysis of these results relative to previously reported structural information supports a model wherein the characteristics of the last coordinating residue and the plasticity of the Ca(2+)-binding loop delimit the allowable geometries for the coordinating sphere.

Animals↗