Parvalbumin Explained

Parvalbumin (PV) is a calcium-binding protein with low molecular weight (typically 9-11 kDa). In humans, it is encoded by the PVALB gene. It is a member of the albumin family; it is named for its size (parv-, from Latin which means "small") and its ability to coagulate.

It has three EF hand motifs and is structurally related to calmodulin and troponin C. Parvalbumin is found in fast-contracting muscles, where its levels are highest, as well as in the brain and some endocrine tissues.

Parvalbumin is a small, stable protein containing EF-hand type calcium binding sites. It is involved in calcium signaling. Typically, this protein is broken into three domains, domains AB, CD and EF, each individually containing a helix-loop-helix motif.[1] The AB domain houses a two amino-acid deletion in the loop region, whereas domains CD and EF contain the N-terminal and C-terminal, respectively.

Calcium binding proteins like parvalbumin play a role in many physiological processes, namely cell-cycle regulation, second messenger production, muscle contraction, organization of microtubules and phototransduction.[2] Therefore, calcium-binding proteins must distinguish calcium in the presence of high concentrations of other metal ions. The mechanism for the calcium selectivity has been extensively studied.[3]

Location and function

In neural tissue

Parvalbumin is present in some GABAergic interneurons in the nervous system, especially the reticular thalamus,[4] and expressed predominantly by chandelier and basket cells in the cortex. In the cerebellum, PV is expressed in Purkinje cells and molecular layer interneurons.[5] In the hippocampus, PV+ interneurons are subdivided into basket, axo-axonic, and bistratified cells, each subtype targeting distinct compartments of pyramidal cells.[6]

PV interneurons' connections are mostly perisomatic (around the cell body of neurons). Most of the PV interneurons are fast-spiking. They are also thought to give rise to gamma waves recorded in EEG.

PV-expressing interneurons represent approximately 25% of GABAergic cells in the primate DLPFC.[7] [8] Other calcium-binding protein markers are calretinin (most abundant subtype in DLPFC, about 50%) and calbindin. Interneurons are also divided into subgroups by the expression of neuropeptides such as somatostatin, neuropeptide Y, cholecystokinin.

In muscular tissue

PV is known to be involved in relaxation of fast-twitch muscle fibers.[9] [10] This function is associated with PV role in calcium sequestration.

During muscle contraction, the action potential stimulate voltage-sensitive proteins in T-tubules membrane. These proteins stimulate the opening of Ca2+ channels in the sarcoplasmic reticulum, leading to release of Ca2+ in the sarcoplasm. The Ca2+ ions bind to troponin, which causes the displacement of tropomyosin, a protein that prevents myosin walking along actin. The displacement of tropomyosin exposes the myosin-binding sites on actin, permitting muscle contraction.[11]

This way, while muscle contraction is driven by Ca2+ release, muscle relaxation is driven by Ca2+ removal from sarcoplasm. Along with Ca2+ pumps, PV contributes to Ca2+ removal from cytoplasm: PV binds to Ca2+ ions in the sarcoplasm, and then shuttles it to the sarcoplasmic reticulum.[12]

Clinical significance

Decreased PV and GAD67 expression was found in PV+ GABAergic interneurons in schizophrenia.[13] [14]

Parvalbumin has been identified as an allergen causing fish allergy (but not shellfish allergy).[15] [16] [17] [18] Bony fishes manifest β-parvalbumin and cartilaginous fishes such as sharks and rays manifest α-parvalbumin; allergenicity to bony fishes has a low cross-reactivity to cartilaginous fishes.

History

The protein was discovered in 1965 as a component of the fast-twitching white muscle of fish. It was described as a low molecular-weight "albumin".[19] It is unknown who coined the term parvalbumin, but the word is already in use by 1967.[20]

External links

Notes and References

  1. Cates MS, Teodoro ML, Phillips GN . Molecular mechanisms of calcium and magnesium binding to parvalbumin . Biophysical Journal . 82 . 3 . 1133–46 . March 2002 . 11867433 . 1301919 . 10.1016/S0006-3495(02)75472-6 . 2002BpJ....82.1133C .
  2. Cates MS, Berry MB, Ho EL, Li Q, Potter JD, Phillips GN . Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin . Structure . 7 . 10 . 1269–78 . October 1999 . 10545326 . 10.1016/S0969-2126(00)80060-X . free .
  3. Dudev T, Lim C . Competition among metal ions for protein binding sites: determinants of metal ion selectivity in proteins . Chemical Reviews . 114 . 1 . 538–56 . January 2014 . 24040963 . 10.1021/cr4004665 .
  4. Cowan RL, Wilson CJ, Emson PC, Heizmann CW . Parvalbumin-containing GABAergic interneurons in the rat neostriatum . The Journal of Comparative Neurology . 302 . 2 . 197–205 . December 1990 . 2289971 . 10.1002/cne.903020202 . 38540563 .
  5. Schwaller B, Meyer M, Schiffmann S . 'New' functions for 'old' proteins: the role of the calcium-binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice . Cerebellum . 1 . 4 . 241–58 . December 2002 . 12879963 . 10.1080/147342202320883551 . 25917565 .
  6. Klausberger T, Marton LF, O'Neill J, Huck JH, Dalezios Y, Fuentealba P, Suen WY, Papp E, Kaneko T, Watanabe M, Csicsvari J, Somogyi P . Complementary roles of cholecystokinin- and parvalbumin-expressing GABAergic neurons in hippocampal network oscillations . The Journal of Neuroscience . 25 . 42 . 9782–93 . October 2005 . 16237182 . 6725722 . 10.1523/JNEUROSCI.3269-05.2005 . free full text
  7. Condé F, Lund JS, Jacobowitz DM, Baimbridge KG, Lewis DA . Local circuit neurons immunoreactive for calretinin, calbindin D-28k or parvalbumin in monkey prefrontal cortex: distribution and morphology . The Journal of Comparative Neurology . 341 . 1 . 95–116 . March 1994 . 8006226 . 10.1002/cne.903410109 . 2583429 .
  8. Gabbott PL, Bacon SJ . Local circuit neurons in the medial prefrontal cortex (areas 24a, b, c, 25 and 32) in the monkey: II. Quantitative areal and laminar distributions . The Journal of Comparative Neurology . 364 . 4 . 609–36 . January 1996 . 8821450 . 10.1002/(SICI)1096-9861(19960122)364:4<609::AID-CNE2>3.0.CO;2-7 . 27397665 .
  9. Celio MR, Heizmann CW . Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres . Nature . 297 . 5866 . 504–6 . June 1982 . 6211622 . 10.1038/297504a0 . 1982Natur.297..504C . 4360112 .
  10. Heizmann CW, Berchtold MW, Rowlerson AM . Correlation of parvalbumin concentration with relaxation speed in mammalian muscles . Proceedings of the National Academy of Sciences of the United States of America . 79 . 23 . 7243–7 . December 1982 . 6961404 . 10.1073/pnas.79.23.7243 . 347315 . 1982PNAS...79.7243H . free .
  11. Book: https://www.ncbi.nlm.nih.gov/books/NBK21054/ . Molecular Biology of the Cell . Alberts . Bruce . Johnson . Lewis . Raff . Roberts . Walter . vanc . Garland Science . 2002 . 0-8153-3218-1 . 4th . New York . Molecular Motors .
  12. Arif SH . A Ca(2+)-binding protein with numerous roles and uses: parvalbumin in molecular biology and physiology . BioEssays . 31 . 4 . 410–21 . April 2009 . 19274659 . 10.1002/bies.200800170 . 42448973 .
  13. Hashimoto T, Volk DW, Eggan SM, Mirnics K, Pierri JN, Sun Z, Sampson AR, Lewis DA . Gene expression deficits in a subclass of GABA neurons in the prefrontal cortex of subjects with schizophrenia . The Journal of Neuroscience . 23 . 15 . 6315–26 . July 2003 . 12867516 . 6740534 . 10.1523/JNEUROSCI.23-15-06315.2003 .
  14. Nakazawa K, Zsiros V, Jiang Z, Nakao K, Kolata S, Zhang S, Belforte JE . GABAergic interneuron origin of schizophrenia pathophysiology . Neuropharmacology . 62 . 3 . 1574–83 . March 2012 . 21277876 . 3090452 . 10.1016/j.neuropharm.2011.01.022 .
  15. Leung NY, Wai CY, Shu S, Wang J, Kenny TP, Chu KH, Leung PS . Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review . Clin Rev Allergy Immunol . 46 . 3 . 180–97 . June 2014 . 23242979 . 10.1007/s12016-012-8336-9 . 29615377 .
  16. Stephen JN, Sharp MF, Ruethers T, Taki A, Campbell DE, Lopata AL . Allergenicity of bony and cartilaginous fish - molecular and immunological properties . Clin. Exp. Allergy . 47 . 3 . 300–12 . March 2017 . 28117510 . 10.1111/cea.12892 . 11343/292433 . 22539836 . free .
  17. Sharp MF, Stephen JN, Kraft L, Weiss T, Kamath SD, Lopata AL . Immunological cross-reactivity between four distant parvalbumins-Impact on allergen detection and diagnostics . Mol. Immunol. . 63 . 2 . 437–48 . February 2015 . 25451973 . 10.1016/j.molimm.2014.09.019 .
  18. Fernandes TJ, Costa J, Carrapatoso I, Oliveira MB, Mafra I . Advances on the molecular characterization, clinical relevance, and detection methods of Gadiform parvalbumin allergens . Crit Rev Food Sci Nutr . 57 . 15 . 3281–296 . October 2017 . 26714098 . 10.1080/10408398.2015.1113157 . 22118352 .
  19. Hamoir . G . Konosu . S . Carp Myogens of White and Red Muscles. General Composition and Isolation of Low-Molecular-Weight Components of Abnormal Amino Acid Composition . Biochemical Journal . 1 July 1965 . 96 . 1 . 85–97 . 10.1042/bj0960085 . 14343157 . 1206910.
  20. Pechère . JF . Muscular parvalbumins as homologous proteins. . Comparative Biochemistry and Physiology . January 1968 . 24 . 1 . 289–95 . 10.1016/0010-406x(68)90978-x . 5645516.

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