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Gene Review

PVALB  -  parvalbumin

Gallus gallus

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Disease relevance of PVALB


High impact information on PVALB

  • We have used an antiserum against carp parvalbumin to isolate from a Drosophila head cDNA library immunopositive expression clones [3].
  • Calbindin-D28K is a 1 alpha,25-dihydroxyvitamin D3-dependent protein that belongs to the superfamily of high affinity calcium-binding proteins which includes parvalbumin, calmodulin, and troponin C. All of these proteins bind Ca2+ ligands by an alpha-helix-loop-alpha-helix domain that is termed an EF-hand [4].
  • The homologies between the nucleotide sequences of TnC, calmodulin, and parvalbumin provide evidence that all three proteins were derived from a common precursor molecule which had four Ca2+-binding sites [5].
  • Isolation and sequence of a cDNA clone for rabbit fast skeletal muscle troponin C. Homology with calmodulin and parvalbumin [5].
  • Parvalbumin could not be localized within isolated myofibrils and also did not accumulate in primary myogenic cell cultures together with proteins forming the myofibrillar structure [6].

Biological context of PVALB


Anatomical context of PVALB


Associations of PVALB with chemical compounds

  • Chicken leg muscle parvalbumin was digested with cyanogen bromide or trypsin or trypsin after citraconylation [12].
  • The use of alternative antibodies for GABA, Calbindin-D28k and parvalbumin in trained and untrained chicks confirmed the double-staining pattern observed in the quantitative experiments [13].
  • In contrast, substance P- and cholecystokinin-immunoreactive neurons were more abundant in the medial division, whereas carbonic anhydrase activity and parvalbumin immunoreactivity were stronger in the lateral division [14].
  • These findings do not exclude the possibility that physiological activity affects the expression of parvalbumin since other factors such as changing patterns of synaptic activity or the appearance of calcium conducting NMDA receptors have yet to be examined [15].
  • The cytoarchitecture of the optic tectum of the Japanese quail, Coturnix coturnix japonica, was studied using the Golgi-Kopsch method, parvalbumin, calbindin and GABA immunohistochemistry and nicotinamide adenine dinucleotide phosphate-diaphorase histochemistry [16].

Other interactions of PVALB


Analytical, diagnostic and therapeutic context of PVALB

  • Tissue in situ hybridization identified a clone that labeled specific neurons and muscles similar to the parvalbumin-like immunohistochemical staining pattern [3].
  • Double labeling immunohistochemistry revealed that tenascin-C is associated with neurons which express the Ca(2+)-binding protein parvalbumin, and displays a staining pattern highly reminiscent of perineuronal nets of the extracellular matrix [19].
  • 3. PA in individual muscles was determined by a sandwich ELISA and was demonstrated by 2-dimensional polyacrylamide-gel electrophoresis [20].
  • To further identify immunocytochemically these GABAA receptor expressing cells, double stainings were undertaken with, on one hand, the monoclonal antibodies directed against the receptor complex, and on the other hand polyclonal antisera directed against cat muscle parvalbumin or chicken calbindin D-28K [21].


  1. Molecular cloning of the thymus-specific parvalbumin known as avian thymic hormone: isolation of a full length cDNA and expression of the recombinant protein in Escherichia coli. Palmisano, W.A., Henzl, M.T. Arch. Biochem. Biophys. (1991) [Pubmed]
  2. Differential co-localization of nicotinic acetylcholine receptor subunits with calcium-binding proteins in retinal ganglion cells. Araki, C.M., Pires, R.S., Britto, L.R., Lindstrom, J.M., Karten, H.J., Hamassaki-Britto, D.E. Brain Res. (1997) [Pubmed]
  3. An invertebrate calcium-binding protein of the calbindin subfamily: protein structure, genomic organization, and expression pattern of the calbindin-32 gene of Drosophila. Reifegerste, R., Grimm, S., Albert, S., Lipski, N., Heimbeck, G., Hofbauer, A., Pflugfelder, G.O., Quack, D., Reichmuth, C., Schug, B. J. Neurosci. (1993) [Pubmed]
  4. Calbindin-D28K, a 1 alpha,25-dihydroxyvitamin D3-induced calcium-binding protein, binds five or six Ca2+ ions with high affinity. Leathers, V.L., Linse, S., Forsén, S., Norman, A.W. J. Biol. Chem. (1990) [Pubmed]
  5. Isolation and sequence of a cDNA clone for rabbit fast skeletal muscle troponin C. Homology with calmodulin and parvalbumin. Zot, A.S., Potter, J.D., Strauss, W.L. J. Biol. Chem. (1987) [Pubmed]
  6. Chicken parvalbumin. Comparison with parvalbumin-like protein and three other components (Mr = 8,000 to 13,000). Heizmann, C.W., Strehler, E.E. J. Biol. Chem. (1979) [Pubmed]
  7. Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence analysis of muscle parvalbumin by tandem mass spectrometry. Kuster, T., Staudenmann, W., Hughes, G.J., Heizmann, C.W. Biochemistry (1991) [Pubmed]
  8. Avian thymic hormone and chicken (muscle) parvalbumin are distinct proteins: isolation of a muscle parvalbumin cDNA fragment by PCR. Palmisano, W.A., Henzl, M.T. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  9. Molecular structure of the chicken vitamin D-induced calbindin-D28K gene reveals eleven exons, six Ca2+-binding domains, and numerous promoter regulatory elements. Minghetti, P.P., Cancela, L., Fujisawa, Y., Theofan, G., Norman, A.W. Mol. Endocrinol. (1988) [Pubmed]
  10. Ontogeny of subunits 2 and 3 of the AMPA-type glutamate receptors in Purkinje cells of the developing chick cerebellum. Pires, R.S., Real, C.C., Hayashi, M.A., Britto, L.R. Brain Res. (2006) [Pubmed]
  11. Prenatal acoustic stimulation influences neuronal size and the expression of calcium-binding proteins (calbindin D-28K and parvalbumin) in chick hippocampus. Chaudhury, S., Nag, T.C., Wadhwa, S. J. Chem. Neuroanat. (2006) [Pubmed]
  12. Comparison of the amino acid sequences of tissue-specific parvalbumins from chicken muscle and thymus and possible evolutionary significance. Brewer, J.M., Arnold, J., Beach, G.G., Ragland, W.L., Wunderlich, J.K. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  13. Learning-related fos-like immunoreactivity in the chick brain: time-course and co-localization with GABA and parvalbumin. Ambalavanar, R., McCabe, B.J., Potter, K.N., Horn, G. Neuroscience (1999) [Pubmed]
  14. Cytochemical characteristics of neurons in the trigeminal mesencephalic nucleus of hatchling chicks. Scott, S.A., Dinowitz, S., Terhaar, K., Sherlock, D., Campbell, M.A., Levine, D. J. Comp. Neurol. (1994) [Pubmed]
  15. Development of parvalbumin immunoreactivity in the chick Edinger Westphal nucleus. Fujii, J.T., Lucaj, Z., Peduzzi, J.D., Crossland, W.J. J. Comp. Neurol. (1995) [Pubmed]
  16. Cytoarchitecture of the tectum opticum in the Japanese quail. Hilbig, H., Roth, G., Brylla, E., Robiné, K.P. Neuroscience (1998) [Pubmed]
  17. Parvalbumin and calretinin in the avian thymus. Király, E., Celio, M.R. Anat. Embryol. (1993) [Pubmed]
  18. Relationship between the concentration of myoglobin and parvalbumin in various types of muscle tissues from chickens. Nishida, J., Nishida, T. Br. Poult. Sci. (1985) [Pubmed]
  19. Regional and cellular distribution of the extracellular matrix protein tenascin-C in the chick forebrain and its role in neonatal learning. Metzger, M., Bartsch, S., Bartsch, U., Bock, J., Schachner, M., Braun, K. Neuroscience (2006) [Pubmed]
  20. Distribution of parvalbumin in specific fibre types of chicken skeletal muscles. Nishida, J., Machida, N.W., Tagome, M., Kasugai, Y. Br. Poult. Sci. (1995) [Pubmed]
  21. Partial colocalization of the GABAA receptor with parvalbumin and calbindin D-28K in neurons of the visual cortex and the dorsal lateral geniculate nucleus of the cat. Arckens, L., Rosier, A., Heizmann, C.W., Orban, G.A., Vandesande, F. J. Chem. Neuroanat. (1994) [Pubmed]
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