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PubMed1983

Calcium binding proteins: optical stopped-flow and proton nuclear magnetic resonance studies of the binding of the lanthanide series of metal ions to parvalbumin.

Optical stopped-flow techniques have been used to determine the dissociation rate constants (koff) for the lanthanide(III) ions from carp (pI 4.25) parvalbumin. For most of the 13 different lanthanides studied, the release kinetics were diphasic, composed of both a fast phase (whose rate varied across the series, La3+ leads to Lu3+, between the limits -1.2 less than or equal to log kFAST less than or equal to -0.7) and a slower phase (whose rate varied across the series, La3+ leads to Lu3+, between the limits -1.2 greater than or equal to log kSLOW greater than or equal to -2.9). In addition, the La3+- and Lu3+-induced changes in the 270-MHz proton nuclear magnetic resonance spectrum of parvalbumin were used to calculate the dissociation constants for these specific lanthanides from the two high-affinity Ca2+ binding sites. The KD for one site appears to remain constant across the lanthanide series, determined to be 4.8 X 10(-11) M for both La3+ and Lu3+. The other site, however, is evidently quite sensitive to the nature of the bound Ln3+ ion and shows a strong preference for La3+ (KD,La = 2.0 X 10(-11) M; KD,Lu = 3.6 X 10(-10) M). We conclude from these observations that reports of nearly indistinguishable CD/EF binding site affinities for parvalbumin complexes of the middle-weight lanthanides (i.e., Eu3+, Gd3+, and Tb3+) are quite reasonable in view of the crossover in relative CD/EF site affinities across the lanthanide series.

Animals↗
PubMed1985

Stopped-flow kinetic studies of metal ion dissociation or exchange in a tryptophan-containing parvalbumin.

The rates of dissociation of 2 equiv of various metal ions [Ca(II), Cd(II), Pr(III), Nd(III), Sm(III), Eu(III), Gd(III), Tb(III), Dy(III), Ho(III), Er(III), Yb(III), and Lu(III)] from the primary CD and EF metal ion binding sites of parvalbumin (isotype pI = 4.75) from codfish (Gadus callarius L) were measured by stopped-flow techniques. The removal or replacement of metal ions was monitored by changes in sensitized Tb(III) luminescence or in intrinsic protein tryptophan fluorescence as quenching ions [Eu(III) or Yb(III)] were bound or removed or as the apoprotein was formed. In experiments wherein the bound metal ions were removed by mixing the parvalbumin with an excess of 1,2-diaminocyclohexanetetraacetic acid (DCTA), the kinetic traces were best fit by a double exponential with koff rate constants of 1.07 and 5.91 s-1 for Ca(II), 1.54 and 10.5 s-1 for Cd(II), and approximately 0.05 and approximately 0.5 s-1 for all of the trivalent lanthanide ions. In experiments wherein the bound metal ions were exchanged with an excess of a different metal ion, pseudo-first-order rate constants were proportional to the concentration of excess attacking metal ion for both the fast and slow processes in most experiments. In these cases, extrapolation of the rate constants to zero concentration of attacking metal ion gave values which agree well with the DCTA scavenging results. This finding demonstrates that the off rate constants do not depend on the occupancy of the neighboring site and therefore implies that there is no significant cooperativity in metal ion binding between the two sites in parvalbumin.

Animals↗
PubMed1988

Lifetime and quenching of tryptophan fluorescence in whiting parvalbumin.

The fluorescence lifetime of the single tryptophan in whiting parvalbumin has been measured by time-correlated single-photon counting. In the presence of saturating calcium, greater than 2 mol/mol of protein, the decay of fluorescence is accurately single exponential with a lifetime of 4.6 ns (0.1 M KCl, 20 mM borate, 1 mM dithiothreitol, 20 degrees C, pH 9). Upon complete removal of calcium from parvalbumin with ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid the emission decay becomes biphasic, and a second more rapid decay process with a lifetime of 1.3 ns comprising approximately 18% of the fluorescence emission at 350 nm is observed. The fluorescence emission of the calcium-saturated form is not measurably quenched by iodide. In contrast, upon complete removal of calcium, the fluorescence is completely quenchable as shown by extrapolation of the data to infinite iodide concentration. These results indicate that there is a large increase in the accessibility of the tryptophan residue in the protein to solvent upon removal of calcium. Stern-Volmer plots of the quenching data are nonlinear and indicate that there is more than one quenchable conformation of the calcium-free protein. The lifetime and quenching results are consistent with the presence of significant concentrations of only two stoichiometric species, apoparvalbumin and parvalbumin--Ca2, at partial occupancy of the calcium binding sites.

Animals↗
PubMed1981

Lanthanide ion luminescence probes. Characterization of metal ion binding sites and intermetal energy transfer distance measurements in calcium-binding proteins. 1. Parvalbumin.

Eu(III) laser excitation spectroscopy of the 7F0 leads to 5D0 transition reveals spectral features characteristic of the occupation of the CD and EF Ca(II)-binding sites of parvalbumin by Eu(III) ions. In addition, at pH 6.5, a signal attributable to binding at a third site is observed. This feature is abolished upon lowering the pH to 3.8. At pH 6.5, the appearance of this feature correlates with the decrease in luminescence intensity during titrations of parvalbumin with Eu(III) or Tb(III) after more than approximately 1.8 equiv of either of these ions has been added. Eu(III) ions in the primary sites coordinate zero to two H2O molecules while the third site involves about three coordinated H2O molecules. Parvalbumins in which mixed pairs of lanthanide ions, Ln(III), occupy the CD and EF sites were prepared. Nonradiative energy transfer between Eu(III) and Tb(III) acting as luminescent donors and various other Ln(III) ions serving as acceptors was observed by monitoring the excited-state lifetimes of the donor ions using a pulsed dye laser apparatus. With the assumption of a Förster-type dipole--dipole mechanism, inter-binding-site distance estimates were made from our measurements and are in reasonable agreement with the distance (11.8 A) obtained by X-ray crystallography, especially when Eu(III) is the donor. R0 values (critical distances for 50% energy transfer) in H2O solution range from 9.2 A for the Tb(III)--Ho(III) donor-acceptor pair down to 5.7 A for the Eu(III)--Ho(III) pair.

Animals↗
PubMed2004

Rat alpha- and beta-parvalbumins: comparison of their pentacarboxylate and site-interconversion variants.

Introduction of a fifth carboxylate into the ligand array of the CD site (via the combined S55D and E59D mutations) or the EF site (G98D) of rat alpha-parvalbumin substantially increases divalent ion affinity. This behavior, in conflict with that seen in model peptide systems, agrees with existing data for rat beta-parvalbumin [Henzl et al. (1996) Biochemistry 35, 5856-5869]. The complete analysis of the S55D/E59D double variant necessitated characterization of alpha E59D. Whereas the D59E mutation has minimal influence on beta CD site affinity, E59D has a major impact on the alpha CD site, lowering the apparent association constant by a factor of 14. The thermodynamic consequences of exchanging the rat alpha CD and EF site ligand arrays, which differ at the +z and -x coordination positions, were also examined. When the alpha CD array is imported into the EF site, it acquires a low-affinity phenotype, in agreement with previous findings for beta [Henzl et al. (1998) Biochemistry 37, 9101-9111]. However, when the EF ligand array is introduced into the alpha CD binding loop, it retains a high-affinity signature. This result, contrary to that observed in beta, suggests that the influence of the parvalbumin CD site environment supersedes the intrinsic behavior of the ligand array, a conclusion further supported by the disparate impact of the beta D59E and alpha E59D mutations.

Amino Acid Sequence↗
PubMed2002

A new oligomeric parvalbumin allergen of Atlantic cod (Gad mI) encoded by a gene distinct from that of Gad cI.

BACKGROUND: The major allergen of Baltic cod (Gadus callarias) is a 12.3-kDa parvalbumin with two calcium-binding sites corresponding to EF-hand motifs. Our group found a 24-kDa IgE-reactive band that was also recognized by a monoclonal antiparvalbumin antibody in Atlantic cod (Gadus morhua). Our purpose was to purify and to determine the cDNA deduced sequence of this new cod allergen. METHODS: Proteins from pre rigor mortis Atlantic cod were separated by gel filtration and the eluted peaks were analysed by SDS-PAGE and Western blotting with sera of sensitized patients and with antiparvalbumin. Protein bands were microsequenced, RNA transcripts were amplified by reverse transcription and polymerase chain reaction (RT-PCR) using primer combinations overlapping the open reading frame. RESULTS: Four IgE and antiparvalbumin reactive proteins(12.5, 24, 38 and 51 kDa) were detected in gel filtration eluate. The cDNA deduced sequence of the 24 kDa protein had 109 amino acid residues with a molecular weight of 11.5 kDa and a theoretical pI of 4.34. The 24 kDa band corresponded therefore to a dimer of a beta-parvalbumin. Its homology was higher with Sal sI than with Gad cI. This new allergen was named Gad mI. CONCLUSION: We have characterized a new parvalbumin allergen in Gadus morhua. This protein formed oligomers in native and in reducing conditions. Gad mI and Gad cI may correspond to two distinct genes of Gadus species.

Allergens↗
PubMed2002

Recombinant fish parvalbumins: Candidates for diagnosis and treatment of fish allergy.

Fish and fish products represent one of the most important causes of IgE-mediated food hypersensitivity. In sensitized individuals contact with and consumption of fish can lead to severe health problems, ranging from urticaria and dermatitis to angiedema, diarrhoea, asthma and, at worst, systemic anaphylactic reactions and death. Parvalbumin, a small calcium-binding protein present in the muscles of vertebrates, was identified as the major fish allergen. We describe the isolation and characterization of cDNA clones coding for carp parvalbumin by IgE immunoscreening of a carp muscle expression library. These clones will be the basis for the production of recombinant carp parvalbumin, a useful tool for in vitro and in vivo diagnosis of fish allergy.

Allergens↗
PubMed1993

Time course of hippocampal glucose utilization and persistence of parvalbumin immunoreactive neurons after ibotenic acid-induced lesions of the rat dentate area.

The effects of ibotenic acid induced lesions of the dentate gyrus on hippocampal glucose utilization and parvalbumin-positive neurons were evaluated in male Wistar rats. Ibotenic acid was injected in the right dorsal dentate gyrus. Quantification of glucose utilization was performed 3 days, 3 weeks, or 3 months after the lesion using the 14C-2-deoxyglucose method. Nissl-stained sections and sections stained for acetylcholinesterase were used as references for anatomical delineation of the hippocampal cytoarchitecture. Additional sections were stained for parvalbumin. The results revealed widespread reductions of glucose utilization in all layers and sectors of the hippocampus in the ipsilateral lesioned hemisphere and also in the nonlesioned contralateral hemisphere. The reductions occurred as early as 3 days after the lesion and persisted up to 3 months. In neither hippocampal structure did glucose utilization return to control levels. Immunohistochemical visualization of parvalbumin-containing neurons revealed that these putatively inhibitory neurons persisted in the otherwise granule-cell-depleted area. The data show that interruption of the excitatory trisynaptic pathway from the entorhinal cortex to the CA1 at the level of the dentate gyrus affects hippocampal glucose utilization irreversibly and uniformly. Since some inhibitory neurons seem to survive the ibotenic acid lesion, we suggest that the reductions of hippocampal glucose utilization reflect an imbalance in favor of inhibitory neurons in the ipsilateral hippocampus after the lesion, which manifests also in the contralateral hemisphere via the commissural pathways.

Animals↗
PubMed2001

Parvalbumin is constantly expressed in chromophobe renal carcinoma.

Chromophobe renal carcinoma is composed of neoplastic cell showing several features similar to those found in the intercalated cells of the collecting ducts. Because the distal nephron expresses calcium-binding proteins playing a role in calcium homeostasis, we reasoned that these proteins could be expressed by chromophobe carcinoma and therefore represent a diagnostic marker. We studied the immunohistochemical expression of different calcium-binding proteins (parvalbumin, calbindin-D28K, and calretinin) in 140 renal tumors, including 75 conventional (clear cell) carcinomas, 32 chromophobe carcinomas, 17 papillary renal cell carcinomas, and 16 oncocytomas. Parvalbumin was strongly positive in all primary chromophobe carcinomas and in one pancreatic metastasis; it was positive in 11 of 16 oncocytomas and absent in conventional (clear cell) and papillary renal cell carcinomas, either primary or metastatic. Calbindin-D28K and calretinin were negative in all tumors, with the exception of two chromophobe carcinomas, four oncocytomas, and two papillary renal cell carcinomas showing inconspicuous calretinin expression. Our data demonstrate that parvalbumin may be a suitable marker for distinguishing primary and metastatic chromophobe carcinoma from conventional (clear cell) and papillary renal cell carcinoma. Moreover, they suggest a relationship between chromophobe renal carcinoma and renal oncocytoma and indicate that chromophobe carcinoma exhibits differentiation toward the collecting-duct phenotype.

Calbindin 1↗
PubMed2005

Chronic stress decreases the number of parvalbumin-immunoreactive interneurons in the hippocampus: prevention by treatment with a substance P receptor (NK1) antagonist.

Previous studies have demonstrated that stress may affect the hippocampal GABAergic system. Here, we examined whether long-term psychosocial stress influenced the number of parvalbumin-containing GABAergic cells, known to provide the most powerful inhibitory input to the perisomatic region of principal cells. Adult male tree shrews were submitted to 5 weeks of stress, after which immunocytochemical and quantitative stereological techniques were used to estimate the total number of hippocampal parvalbumin-immunoreactive (PV-IR) neurons. Stress significantly decreased the number of PV-IR cells in the dentate gyrus (DG) (-33%), CA2 (-28%), and CA3 (-29%), whereas the CA1 was not affected. Additionally, we examined whether antidepressant treatment offered protection from this stress-induced effect. We administered fluoxetine (15 mg/kg per day) and SLV-323 (20 mg/kg per day), a novel neurokinin 1 receptor (NK1R) antagonist, because the NK1R has been proposed as a possible target for novel antidepressant therapies. Animals were subjected to a 7-day period of psychosocial stress before the onset of daily oral administration of the drugs, with stress continued throughout the 28-day treatment period. NK1R antagonist administration completely prevented the stress-induced reduction of the number of PV-IR interneurons, whereas fluoxetine attenuated this decrement in the DG, without affecting the CA2 and CA3. The effect of stress on interneuron numbers may reflect real cell loss; alternatively, parvalbumin concentration is diminished in the neurons, which might indicate a compensatory attempt. In either case, antidepressant treatment offered protection from the effect of stress and appears to modulate the hippocampal GABAergic system. Furthermore, the NK1R antagonist SLV-323 showed neurobiological efficacy similar to that of fluoxetine.

Animals↗
PubMed2003

Abnormal neuronal expression of the calcium-binding proteins, parvalbumin and calbindin D-28k, in aged dogs.

Disturbances of the gamma-aminobutyric acid (GABA) neurotransmitter system have been implicated in chronic degenerative neurological disease. Cognitive dysfunction and neuron loss are features in older dogs. GABAergic neurons also show immunoreactivity for specific calcium-binding proteins. Immunohistochemistry was used to study the neuronal expression of calbindin D-28k and parvalbumin in different areas of the brain in 13 dogs, aged between 2 and 13.5 years. Calbindin expression was found only in the cerebellum. There were significant differences in the quantity and distribution of neurons expressing these proteins between geriatric and adult brains. Parvalbumin- and calbindin-expressing neurons are relatively sensitive to degeneration in the cerebellum of older dogs. Parvalbumin labelling was associated with dystrophic structures that are commonly associated with ageing.

Aging↗
PubMed1997

Isoform distribution of parvalbumins and of some myofibrillar proteins in adult and developing Chrysichthys auratus (Geoffroy St. Hilaire, 1808) (Pisces, Claroteidae).

Polyacrylamide gel electrophoresis was used to analyse the distribution of parvalbumin, myosin light chain, and troponin I isoforms in white muscles of larval, juvenile, and adult Chrysichthys auratus (catfish, siluriforms) and to study the kinetics of their synthesis. Parvalbumin isoform PA II was first detected from day 5 post-hatching and was the main "larval" isoform in this species. PA III appeared at the beginning of the juvenile stage but always remained the minor isoform, even in adult fish. Young mature specimens (approximately 12 cm long) displayed the highest total parvalbumin content. Adult-type myosin light chains were detected from day 8. Densitometric analysis confirmed the light-chain distribution typical of fish muscles, with a relatively high amount of LC3 and a low amount of LC1. We evidenced a "larval" form of troponin-I and its progressive replacement by an "adult" form.

Animals↗
PubMed2002

Postnatal development of neurons expressing NADPH-diaphorase and parvalbumin in the parietal cortex of male and female rats.

Expression of the enzyme nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) and the calcium-binding protein parvalbumin was studied in the parietal cortex of male and female rats during postnatal development at 20, 60 and 90 days of age. First, localization of the activity of NADPH-d was combined with the immunohistochemical localization of parvalbumin to facilitate recognition of morphological details and distribution patterns of these two types of cortical neurons. Double staining of neurons for parvalbumin and NADPH-d was never found. Second, it was found that NADPH-d is a simple and proper marker for quantitative studies. Morphometric analysis revealed sexual dimorphism in the density of NADPH-d-positive neurons in 20 days-old prepubertal rats. Females showed higher amounts of NADPH-d-positive neurons than males. No sex-dependent differences were detected in 60 days-old pubertal and 90 days-old postpubertal rats. The present results suggest that sex differences in the number of NADPH-d-positive neurons in the rat parietal cortex may be related to epigenetic effects of gonadal hormones in the early prepubertal period of postnatal development.

Animals↗
PubMed2000

Rapid determination of parvalbumin amino acid sequence from Rana catesbeiana (pI 4.78) by combination of ESI mass spectrometry, protein sequencing, and amino acid analysis.

The complete amino acid sequence of beta-type parvalbumin (PA) from bullfrog Rana catesbeiana (pI 4.78) was determined by tandem mass spectrometry in combination with amino acid analysis and peptide sequencing following Arg-C and V(8) protease digestion. The primary structure of the protein was compared with that of beta-type PA from R. esculenta (pI 4.50), with which it is highly homologous. Compared with R. esculenta beta-type PA4.50, R. catesbeiana beta-type parvalbumin (PA 4.78) differed in 15 out of 108 amino acid residues (14% displacement), PA4.78 had Cys at residue 64 and was acetylated at the amino terminus, but 25 residues of the carboxyl terminus were completely conserved. Several amino acid displacements were found between residues 51 and 80 (30% displacement), although the functionally important sequence of PA was completely conserved. The amino acids residues of putative calcium-binding sites were Asp-51, Asp-53, Ser-55, Phe-57, Glu-59, Glu-62, Asp-90, Asp-92, Asp-94, Lys-96, and Glu-101, which were conserved in all a and b-types of R. catesbeiana as well as other parvalbumins. In addition, Arg-75 and Glu-81, which are thought to form a salt bridge located in the interior of the molecule [Coffee, C.J. et al. (1976) Biochim. Biophys. Acta 453, 67-80], were also conserved in PA4.78.

Amino Acid Sequence↗
PubMed1986

Steady-state properties of calcium binding to parvalbumins from bullfrog skeletal muscle: effects of Mg2+, pH, ionic strength, and temperature.

To improve our understanding of the physiological roles of parvalbumins, PA-1 (pI 4.78) and PA-2 (pI 4.97) parvalbumins were prepared from bullfrog skeletal muscle and their calcium binding properties were examined in a medium of constant ionic strength (I = 0.106, pH 6.80, at 20 degrees C) containing various concentrations of Mg2+ by using a metallo-indicator, tetramethylmurexide. Apparent binding constants for Ca2+ in the presence of Mg2+ changed in the manner expected if Ca2+ and Mg2+ compete for two independent homogeneous binding sites. The following values were obtained: for PA-1, KCa = 1 X 10(7) M-1, KMg = 900 M-1; for PA-2, KCa = 6 X 10(6) M-1, KMg = 830 M-1 (I = 0.106, pH 6.80, at 20 degrees C). The apparent binding constants are strongly dependent on temperature: at 10 degrees C for PA-1, KCa = 2 X 10(8) M-1, KMg = 10(4) M-1; for PA-2, KCa = 5 X 10(7) M-1, KMg = 5 X 10(3) M-1 (I = 0.106, pH 6.80). The dependence of the affinities for Ca2+ on ionic strength is similar to or less than that of GEDTA (EGTA). The affinities for Ca2+ and Mg2+ of parvalbumins are unchanged between pH 6.5 and 7.2.

Amino Acids↗
PubMed1986

Kinetic studies of calcium binding to parvalbumins from bullfrog skeletal muscle.

In addition to steady-state properties of calcium binding to parvalbumins, kinetic studies are required for adequate evaluation of the physiological roles of parvalbumins. By using a dual-wavelength spectrophotometer equipped with a stopped-flow accessory, the transient kinetics of calcium binding to parvalbumins (PA-1 and 2) from bullfrog skeletal muscle was examined at 20 degrees C in medium containing 20 mM MOPS-KOH, pH 6.80, 0.13 mM tetramethylmurexide, 25 microM CaCl2, metal-deprived PA-1 or PA-2, various concentrations of Mg2+, and KCl to adjust the ionic strength of the medium to 0.106. The results can be explained in terms of the following rate constants under the conditions mentioned above when a second-order kinetic scheme is assumed. For PA-1, the association and apparent dissociation rate constants for Ca2+ are 1.5 X 10(7) M-1 X s-1 and 1.5 s-1, respectively, or more. The rate constants for Mg2+ are 7,500 M-1 X s-1 and 5-6 s-1, respectively. For PA-2, the rate constants for Ca2+ are 7 X 10(6) M-1 X s-1 and 1.16 s-1, respectively, and those for Mg2+ are 3,500 M-1 X s-1 and 3.5-4 s-1, respectively. Increased affinities for Ca2+ and Mg2+ at 10 degrees C are largely due to decreased apparent dissociation rate constants for these divalent cations, because no significant change in the association rate constants was found.

Animals↗
PubMed1995

Parvalbumin is a marker of ALS-resistant motor neurons.

The selective vulnerability of limb and bulbar motor neurons is a hallmark of degenerative human motor neuron diseases such as amyotrophic lateral sclerosis (ALS). Currently, there are no known molecular characteristics to distinguish between motor neuron pools which are highly susceptible to degeneration in ALS and those populations which are resistant. Using in situ hybridization on adult rat tissue, we demonstrated that ALS-resistant motor pools robustly express mRNA for the calcium binding protein parvalbumin, while no measurable parvalbumin expression is found in ALS-sensitive motor neuron populations. In contrast, mRNA expression for each of several other calcium binding proteins such as calbindin-D28K, calretinin and calmodulin appears similar in the various motor pools. Thus, parvalbumin represents a biochemical marker of ALS-resistant motor neurons, and may provide insight into the mechanisms of resistance of certain motor neurons to disease.

Amyotrophic Lateral Sclerosis↗
PubMed2000

Parvalbumin-immunoreactive neurons in the human anteroventral thalamic nucleus.

We immunohistochemically characterised the expression of the calcium-binding protein parvalbumin in the normal human anteroventral thalamic nucleus (AVN). Two morphologically distinct neuronal populations were found to be parvalbumin-immunoreactive (PV-IR): a large population of lightly staining PV-IR neurons and a smaller population of intensely PV-IR neurons. This second type of neuron, which displayed many characteristics normally associated with GABAergic interneurons, has not previously been described in human thalamus. Thus, presumptive thalamic interneurons in the human brain can be further subtyped on the basis of immunoreactivity to parvalbumin. This may have implications for the understanding of thalamocortical function in the normal state and in dysfunctional conditions such as Wernicke-Korsakoff syndrome and schizophrenia.

Adult↗