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 217 records · Page 12Linked to original sources
PubMed1996

Expression of the calcium-binding protein, parvalbumin, in cultured cortical neurons using a HSV-1 vector system enhances NMDA neurotoxicity.

Calcium-binding proteins (CaBPs) are a family of proteins having a unique distribution in the brain and are thought to be important in buffering intracellular calcium. Glutamate neurotoxicity is a process by which the over-activation of glutamate receptors can cause the influx of excessive extracellular calcium and neuronal cell death. It has been proposed that neurons containing CaBP may be more resistant to glutamate neurotoxicity due to their increased ability to buffer calcium. Using a herpes simplex virus-1 (HSV-1) vector system we packaged the CaBP gene, parvalbumin, or the marker gene, beta-galactosidase (beta-gal), correctly in viron particles, which were found upon infection to express mRNA specific to these vectors. PC12 and neocortical cultures showed strong immunohistochemical staining for either beta-gal or parv. The cortical cultures stained positively for endogenous glutamate decarboxylase, a marker for GABAergic neurons, but not for endogenous parvalbumin, indicating that parvalbumin was being expressed ectopically from the HSV-1 vector. Interestingly, the expression of parvalbumin increased cortical culture's susceptibility to N-methyl-D-aspartate-induced neurotoxicity. This increase in neurotoxicity was not due to the wild-type virus or the helper virus which accompanies the packaging of these vectors. We speculate that the ectopic expression of parvalbumin in cortical cultures may be increasing glutamate release which in turn increases cell death.

Animals↗
PubMed1989

Calbindin D-28K and parvalbumin immunoreactivity is confined to two separate neuronal subpopulations in the cat visual cortex, whereas partial coexistence is shown in the dorsal lateral geniculate nucleus.

Calbindin D-28K-immunoreactive cells were localized in the supragranular layers of the striate cortex of the cat, while parvalbumin-stained cells occurred from the bottom half of layer II through layer VI, making the two distributions almost complementary. Calbindin- and parvalbumin-positive cells occurred throughout the 3 layers of the dorsal lateral geniculate nucleus (dLGN), but calbindin-immunoreactive cells outnumbered parvalbumin-positive cells. Double labeling on single sections was performed in order to determine the possible coexistence of calbindin and parvalbumin in single cells of cat visual cortex and dLGN. Calbindin and parvalbumin immunoreactivity was found in two separate neuronal populations in the visual cortex, while in the dLGN about 50% of the cells were doubly stained.

Animals↗
PubMed1991

Muscle inactivity reduces the content of parvalbumin in rat thymic myoid cells in vitro.

We investigated the influence of muscle inactivity by the addition of 1 microM tetrodotoxin in culture medium (complete abolishment of spontaneous firings); feeding with 50 mM KCl in the culture medium (inactivation of action potentials by depolarization) and the addition of 50 microM dantrolene sodium in culture medium (excitation-contraction uncoupling) on the content of parvalbumin in a cultured rat thymic myoid cell line (R615B2: M cells) using a highly sensitive enzyme immunoassay for rat parvalbumin. This is the first report of the content of parvalbumin in thymic myoid cells. Our studies clearly show that the content of parvalbumin is significantly decreased in paralyzed M cells compared with controls which had continuous muscle contractions. It is strongly suggested that muscle contractile activity plays an important role on the expression of parvalbumin in thymic myoid cells.

Action Potentials↗
PubMed1990

Purification and characterization of the parvalbumin from monkey skeletal muscle.

1. A high affinity Ca2+ binding and low mol. wt protein, parvalbumin, was purified from monkey skeletal muscle. 2. As compared with other animals, only one component and a lower content of monkey parvalbumin were found. 3. This may suggest that both the component and the content of parvalbumin decreases with biological evolution. 4. The parvalbumin was found to have a mol. wt of 11,400, a pI of 5.1, a high aspartic acid and lysine content, maximum absorption at around 260 nm, a blocked amino-terminal, an immunological distinction, 2 mol Ca2+ binding/mol, and a conformational change by Ca2+ binding. 5. Parvalbumin was shown to have alpha type properties.

Amino Acids↗
PubMed1990

Calcium-binding proteins calbindin and parvalbumin in the superficial dorsal horn of the rat spinal cord.

Neurons containing the calcium-binding proteins, calbindin or parvalbumin, were studied by immunohistochemistry in the superficial dorsal horn of the rat spinal cord. Calbindin-containing cells were found in laminae I, II and III, being more abundant in laminae I and II. Some of the neurons in lamina I containing calbindin projected to the supraspinal area. Parvalbumin-containing neurons were mainly distributed in laminae IIi and III. Calbindin and parvalbumin were not detected in the same cells. Some 75% of the neurotensin-like immunoreactive neurons contained calbindin, which corresponded to 13% of the calbindin-containing neurons. Calbindin was sometimes found in the same cells with substance P, enkephalin or somatostatin but less frequently (44-46% of the peptide-containing neurons). Parvalbumin was not found together with these peptides. Electron microscopy showed that the immunoreactive products of calbindin or parvalbumin were mostly in the dendrites or cell bodies. Immunoreactive axon terminals were relatively few. In rhizotomized animals, neurons containing one of these proteins in laminae II and III were found to receive direct inputs of primary afferent fibers. These findings indicate that neurons containing these two proteins belong to different subpopulations of dorsal horn neurons. They may be important in primary afferent processing.

Animals↗
PubMed1991

Cytochrome oxidase immunohistochemistry in rat brain and dorsal root ganglia: visualization of enzyme in neuronal perikarya and in parvalbumin-positive neurons.

Histochemical detection of cytochrome oxidase activity has been widely used to deduce patterns of neuronal electrical activity in the CNS. Here we investigated the utility of cytochrome oxidase localization by immunohistochemistry and compared immunostaining with histochemical staining patterns in dorsal root ganglia of the rat. In addition, a limited survey of cytochrome oxidase immunostaining density within what are thought to be highly active parvalbumin-immunoreactive neurons was conducted. The immunohistochemical approach produced granular cytoplasmic immunolabelling in neuronal cell bodies and allowed identification of individual labelled cells in all brain regions including those within dense immunoreactive networks of neuropil. Neuronal somata exhibited a wide range of staining densities which were particularly evident in the hippocampus and dorsal root ganglia. The distribution of neurons intensely immunoreactive for cytochrome oxidase within various structures was consistent with previous histochemical descriptions of enzyme activity. Densitometric measurements of immunohistochemical reaction product in individual neurons of hippocampus, substantia nigra, cerebellum and dorsal root ganglia showed that the rate of product deposition was linear with time under conditions chosen for comparisons of staining density. Quantitative analysis of cytochrome oxidase immunohistochemical and histochemical staining densities within the same cells in adjacent sections of dorsal root ganglion gave a correlation coefficient of r = 0.75 (P less than 0.001). In sections processed immunohistochemically for both cytochrome oxidase and parvalbumin, most but not all parvalbumin-containing cells displayed dense cytochrome oxidase immunolabelling. Conversely, many examples were found of neurons that were densely stained for cytochrome oxidase, but lacked parvalbumin. Immunohistochemistry for cytochrome oxidase reveals the enzyme in neuronal cell bodies with a clarity not usually seen with the histochemical method. Combination of this immunohistochemical approach with simultaneous immunolabelling of other neuronal markers, as shown here in the case of parvalbumin, is expected to assist the elucidation of patterns of activity in neurochemically identified cell types and anatomically defined neural systems.

Animals↗
PubMed1991

Parvalbumin and calbindin-D28K immunoreactivity as developmental markers of auditory and vocal motor nuclei of the zebra finch.

The posthatch developmental profiles of parvalbumin and calbindin-D28K immunoreactivity were compared for the auditory nucleus mesencephalicus lateralis pars caudalis in the midbrain, n. ovoidalis in the thalamus, and telencephalic field L, as well as for the telencephalic vocal motor nuclei hyperstriatum ventrale pars caudalis and n. robustus archistriatalis. The two calcium-binding proteins showed specific temporal patterns of expression in each nucleus, without following an ascending or descending sequence. Calbindin-D28K immunoreactivity usually preceded parvalbumin immunoreactivity. Onset of expression, especially of parvalbumin-immunostaining, was earlier in auditory nuclei than in vocal motor nuclei. The developmental order of appearance of immunoreactivity in somata, dendrites and axons was different in various brain regions. In some structures parvalbumin or calbindin-D28K immunoreactivity occurred only transiently. The two antibodies bound to separate but spatially complementary groups of cells in the nucleus mesencephalicus lateralis pars dorsalis and n. ovoidalis, as has previously been described in visual nuclei. This pattern was maintained into adulthood. These hitherto unknown subcompartments may reflect internal functional organization in these nuclei. A transitory neostriatal zone containing parvalbumin-positive neurons and fibres was observed between the immature field L and the emerging hyperstriatum ventrale pars caudalis. Some comparative aspects are discussed as to the way in which neurons distinguished by the two Ca-binding proteins may differ in energy metabolism, activity pattern and other functional mechanisms.

Animals↗
PubMed1996

Immunohistochemical studies of GABA and parvalbumin in the developing human cerebellum.

The localization of GABA and parvalbumin was studied in the developing cerebellum of human fetuses from 16 to 28 weeks of gestation. The avidin-biotin complex immunohistochemical method combined with silver staining were used to reveal the presence of GABA- and parvalbumin-positive neurons and nerve fibres. As early as the 16th week of gestation, GABA immunopositivity was observed in the cerebellar cortex and the deep nuclei. GABA-positive neurons included Purkinje cells, stellate and basket cells of the cerebellar cortex and neurons in the deep nuclei. The gradient of immunoreactivity increased with the maturing cells, being weak at 16 weeks and becoming markedly pronounced at 28 weeks of gestation. GABA-immunopositive mossy fibres were observed in the granular cell layer at 16 weeks, and by 28 weeks, a robust fibre network was present in the cortex and deep nuclei. Immunohistochemical localization for parvalbumin indicates that weak immunoreactivity was observed in Purkinje cells, stellate and basket cells at 16 weeks of gestation, increasing in intensity with advancing age, notably in the Purkinje cells which had acquired an elaborate arbor of neurites at 28 weeks of gestation. In the deep nuclei, parvalbumin-positive cells and nerve fibres were observed throughout the 16 to 28 week period. These results indicate that GABA- and parvalbumin-positive neurons and fibres appeared as early as 16 weeks of gestation, expressing a high degree of immunoreactivity by the 28 week of fetal age.

Cerebellum↗
PubMed2004

Non-serotonergic dorsal and median raphe projection onto parvalbumin- and calbindin-containing neurons in hippocampus and septum.

The median raphe nucleus is involved in controlling and maintaining hippocampal activity through its projection to inhibitory neurons in medial septum and hippocampus. It has been shown that anterogradely axonal-traced fibers originating in the median raphe nucleus project onto calbindin-containing neurons in hippocampus and parvalbumin-containing neurons in medial septum. Parallel immunohistochemistry studies showing serotonin fibers contacting calbindin- and parvalbumin-positive neurons have led to the assumption that raphe fibers projecting on these types of neurons are mainly serotonergic. However, in both dorsal and median raphe nucleus there is a large amount of non-serotonergic neurons which also are projecting neurons, indicating that a part of the raphe fibers projecting to hippocampus and septum may be non-serotonergic. Our aim was to determine whether there is a non-serotonergic projection from the raphe nucleus onto calbindin- and parvalbumin-containing neurons in hippocampus and septum. Biotin dextran amine was used as the anterograde neuronal tracer and injected into either dorsal or median raphe nucleus. By use of triple immunofluorescence-labeling we analyzed the serotonergic content of the biotin dextran amine-labeled fibers contacting parvalbumin- and calbindin-positive neurons. Surprisingly, we found a significant non-serotonergic projection from both dorsal and median raphe nuclei onto calbindin- and parvalbumin-containing interneurons in septum and hippocampus, with a preference in hippocampus for projecting onto calbindin-positive neurons. These results indicate that the raphe nuclei may exert their control on hippocampal and septal activity not only through a serotonergic projection, but also through a significant non-serotonergic pathway.

Animals↗
PubMed2006

Short-term sensory learning does not alter parvalbumin neurons in the barrel cortex of adult mice: a double-labeling study.

We have previously reported that a classical conditioning paradigm involving stimulation of a row of facial vibrissae produced expansion of the cortical representation of the activated vibrissae ("trained row"), this was demonstrated by labeling with 2-deoxyglucose in layer IV of the barrel cortex. We have also shown that functional reorganization of the primary somatosensory cortex is accompanied by an increase in the density of small GABAergic cells and glutamate decarboxylase 67-positive neurons in the hollows of barrels representing the "trained row." GABA neurons of the rat neocortex co-localize with calcium-binding proteins [parvalbumin, carletinin, calbindin D28k] and neuropeptides (vasoactive intestinal polypeptide, somatostatin). In the present study we have examined GABAergic parvalbumin-positive, interneurons in the cortical representation of "trained" facial vibrissae after short-term aversive training, in order to determine whether the observed changes in glutamate decarboxylase 67-positive neurons are accompanied by changes in parvalbumin-positive neurons. Using double immunofluorescent staining, it was found that (i) all parvalbumin-positive neurons in the barrel hollows were glutamate decarboxylase 67-positive, (ii) following aversive training density of glutamate decarboxylase 67-positive neurons in barrel hollows increased significantly compared with controls and (iii) density glutamate decarboxylase 67-positive/parvalbumin-positive neurons in "trained" barrel hollows did not change compared with controls. This study is the first to demonstrate that the density of double-labeled glutamate decarboxylase 67-positive/parvalbumin-positive neurons does not alter during cortical plasticity, thus suggesting that some other population (i.e. parvalbumin negative) of GABAergic interneurons is involved in learning-dependent changes in layer IV of the barrel cortex.

Animals↗
PubMed1997

The isolation of parvalbumin isoforms from the tail muscle of the American alligator (Alligator mississipiensis).

Multiple parvalbumin isoforms have been detected in the tail (skeletal) muscle of the American alligator (Alligator mississipiensis). One of these isoforms (APV-1) has been highly purified and partially characterized. Protein purification involved mainly gel filtration and anion exchange chromatography, and characterization included gel electrophoresis, amino acid composition analysis, metal ion analysis, MALDI-TOF and ESI mass spectrometry, ultraviolet and fluorescence spectroscopy, and one- and two-dimensional 500 MHz proton NMR spectroscopy. The alligator isoforms are rich in phenylalanine and deficient in the other aromatic residues as is typical for parvalbumins. In fact, the one highly purified isoform that forms the basis of this study has only phenyl-alanine as an aromatic residue. Ion exchange chromatography further indicates that this isoform has a relatively high isoelectric point (pl approximately 5.0), indicating that it is an alpha-lineage parvalbumin. This alligator parvalbumin isoform is unusual in that it has an atypically high Ca2+ content (almost 3.0 mole of Ca2+ per mole of protein) following purification, a fact supported by terbium fluorescence titration experiments. Preliminary comparative analysis of the highly purified alligator parvalbumin isoform (in the Ca2-loaded state) by two-dimensional 1H-NMR (2D 1H TOCSY and 2D 1H NOESY) indicates that there is considerable similarity in structure between the alligator protein and a homologous protein obtained from the silver hake (a saltwater fish species).

Alligators and Crocodiles↗
PubMed2000

Species-specific expression of parvalbumin in the entorhinal cortex of the Mongolian gerbil: dependence on local activity but not extrinsic afferents.

Mongolian gerbils are genetically predisposed to develop epileptic seizures in limbic structures. A species-specific property of the Mongolian gerbil is the expression of the calcium-binding protein parvalbumin in the perforant path where it is predominantly concentrated in nerve terminals. To test the hypothesis that this atypical expression of parvalbumin is induced by seizure-correlated hyperactivity in the entorhinohippocampal loop, we investigated whether it is dependent on extrinsic afferents to the entorhinal cortex. We cultivated organotypic slice cultures of neonate gerbil entorhinal cortex, isolated from all regions it is normally connected with in vivo. In these cultures, parvalbumin-expressing neurons demonstrated their characteristic features like in vivo. Blockade of spontaneous local activity with the sodium-channel blocker tetrodotoxin, however, considerably reduced the number of parvalbumin-expressing neurons in culture. These results indicate that spontaneous local activity, but not activity mediated by extrinsic afferents, is an essential factor for the expression of parvalbumin in the entorhinal cortex of the Mongolian gerbil.

Afferent Pathways↗
PubMed1999

Vermectomy enhances parvalbumin expression and improves motor performance in weaver mutant mice: an animal model for cerebellar ataxia.

In the Weaver mutant mouse (wv/wv), an animal model for hereditary cerebellar ataxia, electrophysiological experiments have revealed a disorganized output of cerebellar Purkinje cells (the latter using GABA as an inhibitory transmitter) which, by a cascade of mechanisms, was thought to be the cause of the poor motor abilities. In Purkinje cell degeneration mice (pcd/pcd) lacking nearly all Purkinje cells and displaying milder motor deficiencies than wv, in comparison to wild-type mice, a strong increase in parvalbumin- and (co-localized with parvalbumin) glycine-immunopositive somata in the deep cerebellar and vestibular nuclei has recently been found. It was therefore intriguing to investigate whether motor performance in weaver mutants could be ameliorated by applying cerebellar lesions to eliminate the faulty output and to look for a change in transmitter weighting, indicated by a strong increase in parvalbumin-positive somata in areas (the respective target areas) which were formerly devoid of it. Ten Weaver mutants were subjected to cerebellar lesions. After removal of the vermis a total abolition of tremor, a definite improvement in the balance of affected body parts, an increase in locomotor activity when tested in an open-field matrix, and a strong increase in parvalbumin expression in Weaver mutant deep cerebellar and vestibular nuclei in comparison to wild-types have indeed been found. Increase in motor activity (or explorative behaviour) has been placed in relation to learning mechanisms. The increase in parvalbumin expression and the observed improvement in motor abilities and mechanisms probably related to learning underline the hypothesis that any change in the physiological equilibrium of the brain function by removal of input or output related to an assembly of nerve cells leads to a cascade of changes at the transmitter and neuronal level in near or distant connected brain structures.

Animals↗
PubMed2003

Expression of myofibrillar proteins and parvalbumin isoforms during the development of a flatfish, the common sole Solea solea: comparison with the turbot Scophthalmus maximus.

Developmental changes in myofibrillar protein and parvalbumin isoform composition were investigated in the myotomal muscle of the flatfish Solea solea, characterized by a very brief metamorphic stage. Results were compared with previously obtained data on another pleuronectiform teleost, the turbot (Scophthalmus maximus), displaying prolonged metamorphosis. Electrophoretically measurable changes in myofibrillar proteins and parvalbumins were detected late in the sole, after completion of metamorphosis. In the course of development, muscles showed the usual sequential synthesis of isoforms of the myofibrillar proteins myosin light chain LC2, troponin-T, and troponin-I. An adult parvalbumin isoform (PA III) was found to predominate during sole growth. The two flatfish were characterized by highly species-specific parvalbumin isoforms. Compared with turbot, the profiles of the myofibrillar subunits and parvalbumin isoforms varied little in the course of sole development. The early appearance of adult traits might be correlated with the brevity of metamorphosis of this fish.

Aging↗
PubMedDate not supplied

Projection status of calbindin- and parvalbumin-immunoreactive neurons in the superficial layers of the rat's superior colliculus.

Immunocytochemistry and retrograde labeling were used to define the thalamic projections of calbindin- and parvalbumin-containing cells in superficial layers of the rat's superior colliculus (SC). Quantitative analysis revealed that 90.8 +/- 2.2% (mean +/- standard deviation) of the calbindin-immunoreactive neurons in the stratum griseum superficiale (SGS) projected to the dorsal lateral geniculate nucleus (LGNd) and that 91.3 +/- 4.3% of calbindin-immunoreactive neurons in the stratum opticum (SO) projected to the lateral posterior nucleus (LP). In contrast, only 17.3 +/- 2.5% of parvalbumin-immunoreactive neurons in the SGS were found to project to the LGNd and 16.5 +/- 3.1% of the parvalbumin-immunoreactive SO cells were retrogradely labeled after LP injections. Few of the parvalbumin-immunoreactive neurons in either the SGS (7.2 +/- 2.5%) or the SO (9.2 +/- 2.5%) were GABA positive. The retrograde-labeling results suggest that parvalbumin-immunoreactive neurons in the rat's SO and SGS may either be primarily interneurons or have descending projections, while calbindin-containing cells are primarily thalamic projection neurons. These results are consistent with data from other rodents, but almost exactly the opposite of data that have been reported for the cat for these same populations of SC projection neurons. Such interspecies differences raise questions regarding the functional importance of expressing one calcium-binding protein versus another in a specific neuronal population.

Animals↗
PubMed1987

Heat capacity and entropy changes of the two major isotypes of bullfrog (Rana catesbeiana) parvalbumins induced by calcium binding.

The possible structural changes of the two major isotypes (PA1 and PA2) of parvalbumins from bullfrog (Rana catesbeiana) skeletal muscle caused by Ca2+ binding have been analyzed by microcalorimetric titrations. Titrations of the parvalbumins with Ca2+ have been made in both the absence and presence of Mg2+ at pH 7.0 and at 5, 15, and 25 degrees C. The reactions of the parvalbumins with Ca2+ are exothermic in both the presence and absence of Mg2+ and at every temperature. But the contributions of enthalpy and entropy changes are variable; Mg2+-Ca2+ exchange on PA1 at 25 degrees C is driven almost entirely by a favorable enthalpy change, whereas Ca2+ binding to PA2 at 5 degrees C is driven for the most part by a favorable entropy change. The magnitudes of the hydrophobic and internal vibrational contributions to the heat capacity and entropy changes of the parvalbumins on Ca2+ binding and Mg2+-Ca2+ exchange have been estimated by the empirical method of Sturtevant [Sturtevant, J. M. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 2236-2240]. Although PA1 (beta) and PA2 (alpha) belong to genetically different lineages, the parvalbumins indicate very similar conformational changes to each other on both Ca2+ binding and Mg2+-Ca2+ exchange. On Mg2+-Ca2+ exchange, the vibrational as well as hydrophobic entropy is slightly increased in a parallel manner. In contrast, on Ca2+ binding, the hydrophobic entropy increases but the vibrational entropy decreases. The increase in the hydrophobic entropy indicates the sequestering of nonpolar groups from the surface to the interior of molecules, while the changes in the vibrational entropy suggest that the overall structures are tightened on Ca2+ binding but loosened on Mg2+-Ca2+ exchange.

Animals↗
PubMed1989

Fluorescence studies of the conformational dynamics of parvalbumin in solution: lifetime and rotational motions of the single tryptophan residue.

The fluorescence properties of the single tryptophan residue in whiting parvalbumin were used to probe the dynamics of the protein matrix. Ca2+ binding caused a blue-shift in the emission (from lambda max = 339 to 315 nm) and a 2.5-fold increase in quantum yield. The fluorescence decay was nonexponential in both Ca2(+)-free and Ca2(+)-bound parvalbumin and was best described by Lorentzian lifetime distributions centered around two components: a major long-lived component at 2-5 ns and a small subnanosecond component. Raising the temperature from 8 to 45 degrees C resulted in a decrease in both the center (average) and width (dispersion) of the major lifetime distribution component, whereas the center, width, and fractional intensity of the fast component increased with temperature. Arrhenius activation energies of 1.3 and 0.3 kcal/mol were obtained in the absence and in the presence of Ca2+, respectively, from the temperature dependence of the center of the major lifetime distribution component. Direct anisotropy decay measurements of local tryptophan rotations yielded an activation energy of 2.3 kcal/mol in Ca2(+)-depleted parvalbumin and indicated a correlation between rotational rates and lifetime distribution parameters (center and width). Ca2+ binding produced a decrease in the width of the major lifetime distribution component and a decrease in tryptophan rotational mobility within the protein. There was a rough correlation between these two parameters with changes in Ca2+ and temperature, so that both measurements may be taken to indicate that the structure of Ca2(+)-bound parvalbumin was more rigid than in Ca2(+)-depleted parvalbumin.

Calcium↗
PubMed1990

A calcium-specific conformational response of parvalbumin.

The single tryptophan containing isotype III parvalbumin from codfish (Gadus callarius) was purified by a modified procedure and was shown to be homogeneous by a number of biochemical techniques. Sequence analysis established the location of the single tryptophan in position 102 of the 108 amino acid primary sequence. Atomic absorption spectroscopy showed that trichloroacetic acid (TCA) precipitation was more effective in parvalbumin decalcification compared to the more commonly used method of EGTA treatment. Magnesium induced steady-state fluorescence spectral changes of the EGTA-treated, but not the TCA-treated, parvalbumin. Steady-state fluorescence and circular dichroism spectra showed that calcium, but not magnesium, induced a conformational response in the TCA-treated protein. The fluorescence decay of the calcium-loaded native (holo) cod III parvalbumin was best described by two decay time components. By contrast, three lifetime components were necessary to describe the fluorescence decay of the metal-free (apo) protein. The decay-associated spectra of each temporal component were obtained. Collectively, these results demonstrate that it is possible for a parvalbumin to display a calcium-specific response.

Amino Acid Sequence↗