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PubMed2000

Distribution of parvalbumin, calretinin, and calbindin-D(28k) immunoreactivity in the rat amygdaloid complex and colocalization with gamma-aminobutyric acid.

To understand the organization of inhibitory circuitries in the rat amygdala, the distribution of parvalbumin, calretinin, and calbindin immunoreactivity was investigated in the rat amygdaloid complex. Colocalization of various calcium-binding proteins with the inhibitory transmitter gamma-aminobutyric acid (GABA) was studied by using the mirror technique. Parvalbumin-immunoreactive (-ir) elements were located mostly in the deep amygdaloid nuclei, whereas the calretinin-ir and calbindin-ir staining were most intense in the cortical nuclei as well as in the central nucleus and the amygdalohippocampal area. Second, the distribution of immunopositive neurons largely parallelled the distribution of terminal and neuropil labeling. Third, immunostained neurons could be divided into four major morphologic types (types 1-4) based on the characteristics of the somata and the dendritic trees. The fourth lightly stained neuronal type that had a pyramidal GABA-negative soma was observed only in calretinin and calbindin preparations. Fourth, parvalbumin-ir terminals formed basket-like plexus and cartridges, which suggests that parvalbumin labels GABAergic inhibitory basket cells and axo-axonic chandelier cells, respectively. Colocalization studies indicated that 521 of 553 (94%) of parvalbumin-ir, 419 of 557 (75%) of calbindin-ir, and 158 of 657 (24%) of calretinin-ir neurons were GABA-positive in the deep amygdaloid nuclei. A high density of large GABA-negative calbindin-ir neurons was observed caudally in the medial division of the lateral nucleus and GABA-negative calretinin-ir neurons were observed in the magnocellular division of the accessory basal nucleus as well as in the intermediate and parvicellular divisions of the basal nucleus. These data suggest that in various amygdaloid areas, neuronal excitability is controlled by GABAergic neurons that contain different calcium-binding proteins. The appearance of basket-like plexus and cartridges in the parvalbumin preparations, but not in calretinin preparations, suggests that like in the hippocampus, the distribution of inhibitory terminals in the dendritic and perisomatic regions of postsynaptic neurons in the rat amygdala is organized in a topographic manner.

Amygdala↗
PubMed2002

Postnatal development of parvalbumin- and GABA transporter-immunoreactive axon terminals in monkey prefrontal cortex.

In the primate prefrontal cortex, the axon terminals of the chandelier class of inhibitory local circuit neurons have a distinctive time course of postnatal development. In this study, we sought to determine whether the axon terminals of other classes of local circuit neurons are also refined during postnatal development. We examined postnatal changes in the density of punctate structures immunoreactive for the calcium binding protein parvalbumin, which identifies a subset of gamma-aminobutyric acid (GABA) -containing terminals, in the prefrontal cortex of 35 rhesus monkeys ranging in age from newborn to adult. In area 46, the density of parvalbumin- immunoreactive puncta in the superficial and middle layers was extremely low in the newborn animals, then increased more than 10-fold to adult levels, which were achieved by 3 to 4 years of age. In layer V, a band of labeled puncta present in the newborn animals also increased in density until 3 to 4 years of age. Developmental changes of parvalbumin-immunoreactive puncta in area 9 were similar to those in area 46. In contrast, the density of punctate structures labeled with an antibody against a GABA membrane transporter (GAT-1) did not change across development, suggesting that the number of GABAergic terminals is stable over time, but that the level of parvalbumin protein within the terminals varies. The time course of the observed changes in these parvalbumin-labeled terminals is markedly different from that of parvalbumin-immunoreactive chandelier cell terminal clusters. These findings suggest that morphologically specialized classes of inhibitory interneurons assume prominence within the prefrontal cortical network at different stages of postnatal development.

Aging↗
PubMed1990

Distribution of parvalbumin immunoreactivity in the visual cortex of Old World monkeys and humans.

The macaque visual system has been frequently used as a model for understanding functional aspects of human vision. There are, however, few studies directly comparing biochemically defined neuronal populations in the visual cortex of the two species. In this study we compared the distribution and morphological features of the parvalbumin-immunoreactive neuronal subpopulation within humans and Old World monkeys (Macaca fascicularis and Macaca mulatta) by using monoclonal antibodies against the Ca2(+)-binding protein parvalbumin (PV), a neuronal marker in the vertebrate cerebral cortex. Characteristic laminar density and distribution of PV is observed, matching that seen with cytochrome C-oxidase and gamma-aminobutyric acid (GABA) immunoreactivity. Thus, parvalbumin is prominent in the layers receiving afferents from the dorsal lateral geniculate nucleus. Terminal fields are rich in layer IVA and IVC and moderate in the blob-region of layer II-III of the monkey cortex. In the human visual cortex only layer IVC displays rich terminal fields. Parvalbumin is present in neurons within all layers of the cortex except layer I. Parvalbumin-immunoreactive (PV-ir) axons occur in different lamellae of the white matter containing axons belonging to association or projection neurons. The estimation of PV-ir neurons, determined for 50 microns-wide columns through the thickness of area 17, shows that the percentage of the total neuron number in area 17 of humans containing PV is 6.8 +/- 2.0%, and in the macaque monkey, 11.5 +/- 2.9%. The perikaryal area of PV-ir neurons varies according to the layer and is comparable in humans (109.3 +/- 40.8 microns2) and monkeys (94.3 +/- 29.5 microns2). However, the relative number of large PV-ir neurons is higher in humans. The immunoreactive product fills the thinnest cell processes and the shape of PV-ir neurons can be easily traced with the aid of a camera lucida. The shape of the neurons is similar in the two species studied, and they probably belong to non-spiny stellate, double-bouquet, chandelier, and basket cell classes. This study shows that parvalbumin acts as a marker for a subpopulation of interneurons in area 17, but it is also present in the geniculocortical as well as in corticocortical pathways. Moreover, the Old World monkey and human visual cortices have a similar, but not identical, distribution of this important calcium-binding protein.

Animals↗
PubMed1993

Subpopulations of GABA neurons containing somatostatin, neuropeptide Y, and parvalbumin in the dorsomedial cortex of the lizard Psammodromus algirus.

Different subpopulations of GABA neurons containing the neuropeptides somatostatin and neuropeptide Y, and the calcium binding protein parvalbumin were studied by immunocytochemistry using light and electron microscopy in the dorsomedial cortex of the lizard Psammodromus algirus to investigate the connectivity of different subsets of GABA neurons in the lizard dorsomedial cortical circuitry and to compare cortical regions of reptiles and mammals. GABA neurons were classified into different subsets by using the peroxidase anti-peroxidase immunohistochemical method on adjacent Araldite-embedded semithin sections. GABA neurons in the dorsomedial cortex fall into three major subsets: 1) neurons with somatostatin (and neuropeptide Y), which accounted for about 44% of the GABA population; 2) neurons with parvalbumin, which accounted for about 13% of the GABA neurons; and 3) neurons without parvalbumin or neuropeptides, which represented 40% of all GABA cells. This division of GABA neurons in non-overlapping subpopulations of neuropeptide- and parvalbumin-containing cells is similar to that found in the mammalian hippocampal formation. On the basis of the nerve terminal fields, somatostatin- and parvalbumin-immunoreactive neuronal populations appear to be functionally different, acting on different portions of the projection neurons. Parvalbumin-immunoreactive neurons inhibit the pyramidal neurons at the cell body level, whereas somatostatin-immunoreactive neurons inhibit them on distal dendrites. The results of the present study add more similarities between the lizard dorsomedial cortex and parts of the mammalian hippocampus.

Animals↗
PubMed1994

Postnatal development of parvalbumin immunoreactivity in the cerebral cortex of the cat.

Parvalbumin immunoreactivity in the developing neocortex of the cat progresses following specific laminar, areal, and, in a particular area, roughly anteroposterior gradients. Parvalbumin immunoreactivity first occurs in basket cells and later in chandelier neurons. Pyramid-like immunoreactive neurons are also transitorily observed from the second to the third week in layer V of the auditory association-related areas. Parvalbumin-immunoreactive neurons first appear in the primary somatosensory cortex and primary auditory and visual areas, followed by the primary motor and polysensory association areas and, finally, the auditory association areas and cortical areas related to the limbic system. In addition to cortical neurons, three fiber systems are immunolabeled with antiparvalbumin antibodies: thalamocortical, callosal, and ipsilateral corticocortical. Parvalbumin-immunoreactive thalamocortical fibers appear during the first month of postnatal life. Parvalbumin-immunoreactive callosal and ipsilateral corticocortical fibers are seen from the fourth postnatal week onward. Because all parvalbumin-immunoreactive cortical neurons in adulthood are nonpyramidal inhibitory cells, the present findings suggest that a number of ipsilateral corticocortical and callosal connections may be inhibitory.

Aging↗
PubMed1994

Parvalbumin-containing GABAergic neurons in the basal ganglia output system of the rat.

The output of the basal ganglia is directed through the entopeduncular nucleus (EPN) and the substantia nigra pars reticulata (SNR) and pars lateralis (SNL), which provide a gamma-aminobutyric acidergic (GABAergic) projection to various nuclei of the thalamus and brainstem. Although many neurons within the SNR and EPN have been described as modality specific, the morphological and neurochemical similarities preclude their precise identification. In the present study, the immunocytochemical localization of parvalbumin, a calcium-binding protein, is used in combination with axonal tracing to verify neuronal heterogeneity within the SNR, SNL, and EPN. The results reveal that the majority of neurons in all three centers contain parvalbumin. The parvalbumin-containing neurons are distributed in the caudal two-thirds of the EPN, the rostral part of the SNL, and the lateral two-thirds of the entire rostrocaudal extent of the SNR, the areas involved in sensorimotor function of the basal ganglia. Moreover, the nigrothalamic, nigrocollicular, and EPN-thalamic neurons possess parvalbumin immunoreactivity, whereas the EPN-habenular neurons are devoid of parvalbumin immunoreactivity. The results indicate a neurochemical heterogeneity within the GABAergic output neurons of the basal ganglia and suggest that the parvalbumin-containing neurons of the SNR, SNL, and EPN are the tonically active output neurons that form a major link in the disinhibitory neuronal circuit of the basal ganglia, especially that concerned with sensorimotor function.

Animals↗
PubMed1992

Evidence for commissurally projecting parvalbumin-immunoreactive basket cells in the dentate gyrus of the rat.

The fluorescent retrograde tracer, fluorogold, was used to identify commissurally projecting neurons in the hippocampus and dentate gyrus. After injection of fluorogold into the hippocampus, the contralateral hippocampus was evaluated for fluorogold-immunoreactive or fluorescent neurons. In addition to observing labeled hilar neurons and CA3 pyramidal cells that previously have been reported to send commissurally projecting axons to the contralateral hippocampus, the authors unexpectedly found a population of fluorogold-labeled cells in the granule cell layer with the morphology and location of GABA-immunoreactive basket cells. Immunocytochemical staining revealed that all fluorogold-labeled cells of the granule cell layer were immunoreactive for parvalbumin. However, not all parvalbumin cells, shown previously to be a subset of GABA neurons, were fluorogold-labeled. The association between fluorogold transport and parvalbumin immunoreactivity was unique for these cells of the granule cell layer. In the adjacent hilus, relatively few of the many fluorogold-labeled cells were parvalbumin- or GABA-immunoreactive. These results (1) identify a population of presumed inhibitory neurons that apparently form commissural projections; (2) document that all of these cells contain the calcium-binding protein parvalbumin; and (3) indicate that the vast majority of commissurally projecting hilar neurons are neither parvalbumin- nor GABA-immunoreactive.

Animals↗
PubMed1994

Parvalbumin immunocytochemistry and calcium deposition in muscle fiber necrosis and subsequent regeneration following intramuscular injection of metoclopramide.

We have studied the sequential change of parvalbumin immunocytochemistry and its correlation with intracellular Ca2+ deposition in an animal model of muscle fiber necrosis and regeneration induced by intramuscular injection of metoclopramide. Twenty-four hours after the drug's injection, extensive muscle fiber necrosis, together with dramatic loss of parvalbumin immunoreactivity and intracellular Ca2+ deposition, was observed. Muscle fiber regeneration began on day 4 after the injection and was complete by the end of the third week. Parvalbumin was not detected in the regenerating fibers, but gradually emerged during the second week as muscle fibers increased in size. It can be suggested that loss of parvalbumin in necrotic fibers is secondary to the loss in integrity of the sarcolemma. Alternatively, loss of parvalbumin in degenerating fibers may impair calcium buffering and act as a contributory factor in the necrotic process. The progressive appearance of parvalbumin immunoreactivity in regenerating fibers parallels that found in normal myogenesis.

Animals↗
PubMed1999

Electrospray ionization mass spectrometry: analysis of the Ca2+-binding properties of human recombinant alpha-parvalbumin and nine mutant proteins.

A set of 10 different recombinant human parvalbumins was used to establish a method for the investigation of the Ca2+-binding properties of proteins by electrospray ionization mass spectrometry (ESI-MS). Human PVWT was found to bind 2 mol Ca2+ ions/mol of protein, whereas its mutants (PVE101V, PVD90A, PVE62V, PVD51A, PVD90A,E101V, PVE62V,E101V, PVD51A,D90A, PVD51A,E62V, PVD51A,E62V, D90A,E101V) containing inactivating substitutions in the Ca2+-binding loops bind 0 or 1 Ca2+ ion per protein molecule, depending on the degree of inactivation. These findings fully agree with previously reported results obtained by flow dialysis experiments. The RP-HPLC desalted metal-free proteins were analyzed in 10 mM ammonium acetate at pH 7.0. The experimental conditions were optimized with the recombinant parvalbumin test system before analyzing the Ca2+-binding properties of rat and murine parvalbumins in muscle tissue extracts. ESI-MS revealed that (i) rat and murine alpha-parvalbumins each bind specifically two Ca2+ ions per protein molecule and (ii) both extracted parvalbumins were found to be posttranslationally modified; each protein is acetylated at the N-terminus. Finally, during our investigations of the murine parvalbumin a sequencing error was detected at the C-terminus where the amino acid at position 109 is Ser and not Thr as mentioned in the SwissProt data base (Accession No. P32848). This work demonstrates the great potential of the ESI-MS technique as a sensitive, specific, and rapid method for direct identification and determination of the stoichiometry of Ca2+-binding proteins and other metalloproteins.

Animals↗
PubMed1994

Carp parvalbumin binds to and directly interacts with the sarcoplasmic reticulum for Ca2+ translocation.

Interaction between two relaxing factors, the sarcoplasmic reticulum and parvalbumin, in carp fast skeletal muscle was investigated. Immunoblotting using an anti-parvalbumin antibody revealed that parvalbumin bound to the light sarcoplasmic reticulum isolated from carp fast skeletal muscle in the presence of Ca2+. Parvalbumin enhanced Ca2+ uptake activity of the light sarcoplasmic reticulum. Furthermore, using a photoreactive cross-linker, we detected a protein in the light sarcoplasmic reticulum which bound to parvalbumin in a Ca(2+)-dependent manner. These results suggest that parvalbumin may directly interact with the sarcoplasmic reticulum in contraction-relaxation cycle of carp fast skeletal muscle.

Animals↗
PubMed1995

Changes in shape and motility of cells transfected with parvalbumin cDNA.

Parvalbumin is thought to act as a Ca2+ buffer in skeletal muscle fibers, but its physiological role in brain, kidney, and testis remains unclear. We have transfected parvalbumin cDNA into a human ovarian adenocarcinoma cell line, which normally does not express this protein. The induced expression of parvalbumin under the control of three different promoters causes: (1) changes in the morphology of the cells from epitheloid to fusiform, (2) an increase in motility of whole cell clusters, and (3) a decrease in the mitotic rate. Transfection with a mutated cDNA of rat parvalbumin incapable of binding Ca2+ had no effect on these three parameters. Our results indicate that ectopic expression of parvalbumin influences not only cell division [Rasmussen and Means (1989) Mol. Endocrinol. 3, 588-596], but also cell shape and motility by modulating intracellular Ca2+ handling. This may be a basic function of parvalbumin when it is intrinsically expressed in differentiated nonmuscle cells.

Cell Line, Transformed↗
PubMed1993

Postnatal development of parvalbumin and calbindin D28K immunoreactivities in the cerebral cortex of the rat.

Parvalbumin and calbindin D28k immunoreactivities were examined in the neocortex of the rat during postnatal development. Parvalbumin-immunoreactive nonpyramidal neurons first appear in layer V and later in layers VI and IV, and then in II and III. Immunoreactive terminals forming baskets surrounding unlabelled somata appear about 2 days later. The first parvalbumin-immunoreactive neurons appear in the retrosplenial and cingulate cortices, and the rostral region of the primary somatosensory cortex at postnatal days 8 or 9 (P8-P9). These regions are followed by the primary visual, primary auditory and motor cortices at P11. Parvalbumin immunoreactivity appears last in the secondary areas of the sensory regions and association cortices. Adult patterns are reached at the end of the 3rd week. Calbindin D28K-immunoreactive nonpyramidal neurons are found at birth in all cortical layers excepting the molecular layer. The intensity of the immunoreaction increases during the first 8 or 11 days of postnatal life, first in the inner and later in the upper cortical layers, following, therefore, an "inside-out" gradient. Heavily-labelled calbindin D28K-immunoreactive nonpyramidal cells dramatically decrease in number from P11 to P15 due mainly to a decrease of the multipolar subtypes. This suggests that two populations of calbindin D28k-immunoreactive nonpyramidal neurons are produced in the neocortex during postnatal development: one population of neurons transitorily expresses calbindin D28k immunoreactivity; the other population is composed of neurons that are permanently calbindin D28k immunoreactive. In addition to heavily labelled nonpyramidal cells, a band of weakly labelled pyramid-like neurons progressively appears in layers II and III throughout the cerebral cortex, beginning in layer IV in the somatosensory cortex by the end of the 2st week. Adult patterns are reached at the end of the 3rd week. These results indicate that parvalbumin and calbindin D28k immunoreactivities in the cerebral neocortex follow different characteristic patterns during postnatal development. The appearance of parvalbumin immunoreactivity correlates with the appearance of the related functional activity in the different cortical regions, and, probably, with the appearance of inhibitory activity in the neocortex. On the other hand, the early appearance of calbindin D28k immunoreactivity in the neocortex may be related to the early appearance of calbindin immunoreactivity in many other brain regions, and suggests another, as yet unknown, role for this calcium-binding protein during development of the cerebral cortex.

Animals↗
PubMed1991

Ontogeny of the calcium binding protein parvalbumin in the rat nervous system.

In the adult rat brain, the calcium-binding protein parvalbumin is preferentially associated with spontaneously fast-firing, metabolically active neurons and coexists with gamma-amino-butyric acid (GABA) in cortical inhibitory interneurons. Whether this is so in developing neurons has not been explored. To this end, we have used parvalbumin immunohistochemistry to study expression of this protein in the rat nervous system during pre- and postnatal life. Our results indicate that parvalbumin first appears at embryonic day 13 in sensory system of the spinal cord, in the vestibular (VIII), the trigeminal (V) and the visuomotor (III, IV, VI) systems, and develops rapidly during the following days. In these locations the expression of parvalbumin coincides with the beginning of physiological activity in nerve cells. In the gamma-aminobutyric acid (GABA)-containing interneurons of the cerebral cortex and the hippocampus, as well as in the Purkinje cells of the cerebellum, parvalbumin only appears postnatally. It lags behind the development of GABA-immunoreactivity by 1 to 2 weeks. The beginning of its expression, in the cerebellum at least, coincides with the arrival of excitatory synaptic input and the onset of spontaneous activity. Thus, during the development of the nervous system, the expression of parvalbumin is subordinate to the establishment of physiological activity.

Animals↗
PubMed1994

An immunohistochemical study of parvalbumin containing interneurons in the gerbil hippocampus after cerebral ischemia.

We investigated postischemic changes of non-pyramidal neurons in the gerbil hippocampus 1 h - 7 days after 10 min of cerebral ischemia, with parvalbumin and microtubule-associated protein 2 (MAP2)-immunohistochemistry. Parvalbumin-immunoreactive interneurons in the hippocampus were unaffected up to 24 h after ischemia. A slight reduction of the immunoreactivity in neuronal processes was seen in the hippocampal CA1 sector 48 h after ischemia. Seven days after ischemia, a marked loss of parvalbumin-immunoreactive interneurons was observed in the hippocampal CA1 and CA3 sectors. Furthermore, reduced staining in the dentate granular and molecular layers was observed. MAP2-immunoreactive pyramidal neurons in the hippocampus were unchanged up to 48 h after ischemia. Seven days after ischemia, a severe loss of MAP2 immunoreactivity was found in the hippocampal CA1 and CA3 neurons and dentate hilar neurons. However, scattered CA1 neurons, most likely interneurons, preserved MAP2 immunoreactivity. The results demonstrate that transient cerebral ischemia can cause a loss of parvalbumin-immunoreactive interneurons in the hippocampus. Furthermore, some interneurons seem to lose parvalbumin synthesis. Although dentate granule cells are resistant to ischemia, considerable reductions of afferent input was suggested by parvalbumin staining.

Animals↗
PubMed2002

Parvalbumin 3 is an abundant Ca2+ buffer in hair cells.

Ca2+ signaling serves distinct purposes in different parts of a hair cell. The Ca2+ concentration in stereocilia regulates adaptation and, through rapid transduction-channel reclosure, underlies amplification of mechanical signals. In presynaptic active zones, Ca2+ mediates the exocytotic release of afferent neurotransmitter. At efferent synapses, Ca2+ activates the K+ channels that dominate the inhibitory postsynaptic potential. A copious supply of diffusible protein buffer isolates the three signals by restricting the spread of free Ca2+ and limiting the duration of its action. Using cDNA subtraction and a gene expression assay based on in situ hybridization, we detected abundant expression of mRNAs encoding the Ca2+ buffer parvalbumin 3 in bullfrog saccular and chicken cochlear hair cells. We cloned cDNAs encoding this protein from the corresponding inner-ear libraries and raised antisera against recombinant bullfrog parvalbumin 3. Immunohistochemical labeling indicated that parvalbumin 3 is a prominent Ca2+-binding protein in the compact, cylindrical hair cells of the bullfrog's sacculus, and occurs as well in the narrow, peanut-shaped hair cells of that organ. Using quantitative Western blot analysis, we ascertained that the concentration of parvalbumin 3 in saccular hair cells is approximately 3 mM. Parvalbumin 3 is therefore a significant mobile Ca2+ buffer, and perhaps the dominant buffer, in many types of hair cell. Moreover, parvalbumin 3 provides an early marker for developing hair cells in the frog, chicken, and zebrafish.

Amino Acid Sequence↗
PubMed2006

Reduction in parvalbumin expression in the zona incerta after 6OHDA lesion in rats.

In an effort to understand better the neurochemical changes that occur in Parkinson disease, we have examined the expression patterns of the calcium-binding protein parvalbumin in the zona incerta in parkinsonian rats. Sprague-Dawley rats had small volumes of either saline (control) or 6 hydroxydopamine (6OHDA) injected into the medial forebrain bundle, the major tract carrying dopaminergic nigrostriatal axons. After various post-lesion survival periods, ranging from 2 hrs to 84 days, rats were perfused with formaldehyde and their brains processed for routine tyrosine hydroxylase (TH) or parvalbumin immunocytochemistry. In the 3 to 84 days post-lesion cases, there was an overall 50% reduction in the number of parvalbumin(+) cells in the zona incerta on the 6OHDA-lesioned side when compared to control. In the 2 hrs post-lesion cases, there was no substantial loss of parvalbumin(+) cells in the zona incerta after 6OHDA lesion, although in these cases (unlike the longer survival periods), there was limited loss of TH(+) cells in the midbrain on the lesion side. The loss of parvalbumin(+) cells from the zona incerta was due to a loss of antigen expression rather than a loss of the cells themselves, since the number of Nissl-stained cells in the zona incerta was similar on the control and 6OHDA-lesioned sides. In summary, our results indicate that a loss of the midbrain dopaminergic cells induces a major change in parvalbumin expression within the zona incerta. This change may have key functional and clinical implications.

Animals↗
PubMed1978

Radioelectrophoresis: a specific microassay for parvalbumins. Application to muscle biopsies from man and other vertebrates.

A two-dimensional radioelectrophoretic method is described, by which parvalbumins from minute biopsy samples (approx. 50 mg) can be detected and quantitated by their 45Ca2+-binding properties. In the first dimension, parvalbumins are purified by sieving through a gradient polyacrylamide gel and collected at the bottom of the electrophoresis tubes. The second dimension is a disc electrophoresis in the presence of 45Ca2+. Parvalbumins can thus be identified and quantitated by three criteria: low molecular weight, acidic character and calcium-binding properties, since they are never exposed to denaturing conditions. Validity of the technique was demonstrated on carp myogen, and on extracts from rabbit psoas and heart muscles. Application of this method to the shrew fast beating myocardium shows that it does contain parvalbumin, in agreement with the proposed role of soluble relaxing factor (Pechère et al. (1977) FEBS Lett. 75, 111--1141. When applied to human muscle biopsies, radioelectrophoresis points to an uneven distribution of parvalbumin among different skeletal muscles. For the human limb muscles tested in this study, the parvalbumin content is similar to that of rabbit psoas muscle.

Animals↗
PubMed1993

Intracellular concentration of parvalbumin in nerve cells.

Parvalbumin is supposed to function as an intracellular Ca2+ buffer in the brain, but its concentration in nerve cells is unknown. We combined radioimmunoassay of parvalbumin in rat brain extracts, together with image analysis of area fractions immunostained with the parvalbumin antibody on sections, to deduce the intracellular concentration of parvalbumin. We found that the average amount of parvalbumin varied between 6 microM in the caudatoputamen and 45 microM in the cerebellum. Although these values are only rough averages and do not demonstrate a Ca2+ buffering role for parvalbumin in neurons, the concentration of the protein is at least in the appropriate range for such a function.

Animals↗