Parvalbumin

Last updated

PVALB
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PVALB , D22S749, parvalbumin
External IDs OMIM: 168890; MGI: 97821; HomoloGene: 2137; GeneCards: PVALB; OMA:PVALB - orthologs
Orthologs
SpeciesHumanMouse
Entrez

5816

19293

Ensembl

ENSG00000274665
ENSG00000100362

ENSMUSG00000005716

UniProt

P20472

P32848

RefSeq (mRNA)

NM_002854
NM_001315532

NM_013645
NM_001330686

RefSeq (protein)

NP_001302461
NP_002845
NP_001302461.1
NP_002845.1

NP_001317615
NP_038673

Location (UCSC) Chr 22: 36.8 – 36.82 Mb Chr 15: 78.08 – 78.09 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Parvalbumin
Identifiers
Symbol?
InterPro IPR008080

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 parvus which means "small") and its ability to coagulate.

Contents

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. [5] 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. [5]

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. [6] 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. [6] [7]

Location and function

Pvalb is expressed in the reticular nucleus of the thalamus in the postnatal day 56 mouse. Allen Brain Atlases Pvalb, mouse, ret thalamus, ISH.jpg
Pvalb is expressed in the reticular nucleus of the thalamus in the postnatal day 56 mouse. Allen Brain Atlases
In the cerebellum of adult mice Pvalb is expressed in Purkinje cells and molecular layer interneurons. Allen Brain Atlases Pvalb, cerebellum, ISH.jpg
In the cerebellum of adult mice Pvalb is expressed in Purkinje cells and molecular layer interneurons. Allen Brain Atlases

In neural tissue

Parvalbumin is present in some GABAergic interneurons in the nervous system, especially the reticular thalamus, [8] and expressed predominantly by chandelier and basket cells in the cortex. In the cerebellum, PV is expressed in Purkinje cells and molecular layer interneurons. [9] In the hippocampus, PV+ interneurons are subdivided into basket, axo-axonic, and bistratified cells, each subtype targeting distinct compartments of pyramidal cells. [10]

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. [11] [12] 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. [13] [14] This function is associated with the PV role in calcium sequestration.

During muscle contraction, the action potential stimulates voltage-sensitive proteins in the T-tubule 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. [15] 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. [16]

Clinical significance

Decreased PV and GAD67 expression was found in PV+ GABAergic interneurons in schizophrenia. [17] [18]

Parvalbumin has been identified as the major allergen causing fish meat allergy (but not shellfish allergy). [19] [20] [21] [22] Most bony fishes manifest β-parvalbumins as major allergens and cartilaginous fishes such as sharks and rays manifest α-parvalbumins as major allergens; allergenicity to bony fishes has a low cross-reactivity to cartilaginous fishes [20] and also chicken meat. [23]

Parvalbumins, an ancient family of proteins

Parvalbumins and their genes have only been found in jawed vertebrate species so far. From the evolutionary level of sharks, already three major lineages of parvalbumins can be distinguished [24] : (1) α-parvalbumins, which include the above discussed human "parvalbumin"; (2) oncomodulins (sometimes called "β-1 parvalbumins"), which are also found in human and mouse; and (3) β-2 parvalbumins, which are the major allergens in most bony fish and were lost in human and mouse but conserved in some primitive mammals.

All parvalbumins share a highly conserved structure (see the figure) [24] , which explains their high level of sequence conservation, resulting in the above-mentioned cross-reactivity in allergenic reactions against different bony fish species and even species from other animal clades such as chicken. [25]

Conserved Parvalbumin Structures.png

Bony fishes have, depending on the species, combined for all three parvalbumin lineages between 7 and 22 genes. [26] [24] Although in most bony fishes the β-2 parvalbumins are the major allergens, in some bony fishes the α-parvalbumins are the highest expressed in muscle and were identified as the allergens. [25] The allergen nomenclature is partly based on the order of allergen detection per species, and therefore identical allergen numbers in different fish species do not always refer to the same gene (see the table). [25]

Nomenclature of fish parvalbumin allergens.png

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". [27] It is unknown who coined the term parvalbumin, but the word is already in use by 1967. [28]

Related Research Articles

<span class="mw-page-title-main">Calmodulin</span> Messenger protein

Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases.

<span class="mw-page-title-main">Interneuron</span> Neurons that are not motor or sensory

Interneurons are neurons that connect to brain regions, i.e. not direct motor neurons or sensory neurons. Interneurons are the central nodes of neural circuits, enabling communication between sensory or motor neurons and the central nervous system (CNS). They play vital roles in reflexes, neuronal oscillations, and neurogenesis in the adult mammalian brain.

<span class="mw-page-title-main">Sarcoplasm</span> Cytoplasm of a muscle cell, including the sarcoplasmic reticulum

Sarcoplasm is the cytoplasm of a muscle cell. It is comparable to the cytoplasm of other cells, but it contains unusually large amounts of glycogen (a polymer of glucose), myoglobin, a red-colored protein necessary for binding oxygen molecules that diffuse into muscle fibers, and mitochondria. The calcium ion concentration in sarcoplasma is also a special element of the muscle fiber; it is the means by which muscle contractions take place and are regulated. The sarcoplasm plays a critical role in muscle contraction as an increase in Ca2+ concentration in the sarcoplasm begins the process of filament sliding. The decrease in Ca2+ in the sarcoplasm subsequently ceases filament sliding. The sarcoplasm also aids in pH and ion balance within muscle cells.

Voltage-gated calcium channels (VGCCs), also known as voltage-dependent calcium channels (VDCCs), are a group of voltage-gated ion channels found in the membrane of excitable cells (e.g. muscle, glial cells, neurons) with a permeability to the calcium ion Ca2+. These channels are slightly permeable to sodium ions, so they are also called Ca2+–Na+ channels, but their permeability to calcium is about 1000-fold greater than to sodium under normal physiological conditions.

<span class="mw-page-title-main">Tropomyosin</span> Protein

Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in many animal and fungal cells. In animals, it is an important component of the muscular system which works in conjunction with troponin to regulate muscle contraction. It is present in smooth and striated muscle tissues, which can be found in various organs and body systems, including the heart, blood vessels, respiratory system, and digestive system. In fungi, tropomyosin is found in cell walls and helps maintain the structural integrity of cells.

Molecular neuroscience is a branch of neuroscience that observes concepts in molecular biology applied to the nervous systems of animals. The scope of this subject covers topics such as molecular neuroanatomy, mechanisms of molecular signaling in the nervous system, the effects of genetics and epigenetics on neuronal development, and the molecular basis for neuroplasticity and neurodegenerative diseases. As with molecular biology, molecular neuroscience is a relatively new field that is considerably dynamic.

Ryanodine receptors form a class of intracellular calcium channels in various forms of excitable animal tissue like muscles and neurons. There are three major isoforms of the ryanodine receptor, which are found in different tissues and participate in different signaling pathways involving calcium release from intracellular organelles. The RYR2 ryanodine receptor isoform is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells.

<span class="mw-page-title-main">Calcium signaling</span> Intracellular communication process

Calcium signaling is the use of calcium ions (Ca2+) to communicate and drive intracellular processes often as a step in signal transduction. Ca2+ is important for cellular signalling, for once it enters the cytosol of the cytoplasm it exerts allosteric regulatory effects on many enzymes and proteins. Ca2+ can act in signal transduction resulting from activation of ion channels or as a second messenger caused by indirect signal transduction pathways such as G protein-coupled receptors.

<span class="mw-page-title-main">Glutamate receptor</span> Cell-surface proteins that bind glutamate and trigger changes which influence the behavior of cells

Glutamate receptors are synaptic and non synaptic receptors located primarily on the membranes of neuronal and glial cells. Glutamate is abundant in the human body, but particularly in the nervous system and especially prominent in the human brain where it is the body's most prominent neurotransmitter, the brain's main excitatory neurotransmitter, and also the precursor for GABA, the brain's main inhibitory neurotransmitter. Glutamate receptors are responsible for the glutamate-mediated postsynaptic excitation of neural cells, and are important for neural communication, memory formation, learning, and regulation.

<span class="mw-page-title-main">Calbindin</span> Protein

Calbindins are three different calcium-binding proteins: calbindin, calretinin and S100G. They were originally described as vitamin D-dependent calcium-binding proteins in the intestine and kidney of chicks and mammals. They are now classified in different subfamilies as they differ in the number of Ca2+ binding EF hands.

Oncomodulin is a parvalbumin-family calcium-binding protein expressed and secreted by macrophages.

Calcium-binding proteins are proteins that participate in calcium cell signaling pathways by binding to Ca2+, the calcium ion that plays an important role in many cellular processes. Calcium-binding proteins have specific domains that bind to calcium and are known to be heterogeneous.

<span class="mw-page-title-main">Calretinin</span> Protein found in humans

Calretinin, also known as calbindin 2, is a calcium-binding protein involved in calcium signaling. In humans, the calretinin protein is encoded by the CALB2 gene.

<span class="mw-page-title-main">Cannabinoid receptor 1</span> Mammalian protein found in humans

Cannabinoid receptor 1 (CB1), is a G protein-coupled cannabinoid receptor that in humans is encoded by the CNR1 gene. The human CB1 receptor is expressed in the peripheral nervous system and central nervous system. It is activated by endogenous cannabinoids called endocannabinoids, a group of retrograde neurotransmitters that include lipids, such as anandamide and 2-arachidonoylglycerol (2-AG); plant phytocannabinoids, such as docosatetraenoylethanolamide found in wild daga, the compound THC which is an active constituent of the psychoactive drug cannabis; and synthetic analogs of THC. CB1 is antagonized by the phytocannabinoid tetrahydrocannabivarin (THCV).

<span class="mw-page-title-main">S100A1</span> Protein-coding gene in the species Homo sapiens

Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Z-discs and sarcoplasmic reticulum. S100A1 has shown promise as an effective candidate for gene therapy to treat post-myocardially infarcted cardiac tissue.

<span class="mw-page-title-main">S100P</span> Protein-coding gene in the species Homo sapiens

S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene.

<span class="mw-page-title-main">STIM2</span> Protein-coding gene in the species Homo sapiens

Stromal interaction molecule 2 (STIM2) is a protein that in humans is encoded by the STIM2 gene.

ParvE101Q is an experimental modification of parvalbumin, designed to delay calcium sequestration in heart muscles to enhance contraction. The protein parvalbumin has EF hand motifs used for calcium binding. EF hands are structural helix-loop-helix protein subunits that have a high affinity for calcium ions, and a moderate affinity for magnesium ions. In muscle, the binding of Ca2+ by parvalbumin efficiently sequesters it following contraction. This increases the speed of muscle relaxation, allowing the muscle to contract again sooner. Although parvalbumin is classified as a delayed calcium buffer, it quickly sequesters Ca2+, usually before the muscle is done fully contracting. Large amounts of parvalbumin allow rapid contractions of muscles at a high contractile speed with the trade-off of having relatively lower contraction force. This decreased force of contraction is due to the rapid sequestration of Ca2+, preventing prolonged contraction which is required for greater force.

Calcium imaging is a microscopy technique to optically measure the calcium (Ca2+) status of an isolated cell, tissue or medium. Calcium imaging takes advantage of calcium indicators, fluorescent molecules that respond to the binding of Ca2+ ions by fluorescence properties. Two main classes of calcium indicators exist: chemical indicators and genetically encoded calcium indicators (GECI). This technique has allowed studies of calcium signalling in a wide variety of cell types. In neurons, action potential generation is always accompanied by rapid influx of Ca2+ ions. Thus, calcium imaging can be used to monitor the electrical activity in hundreds of neurons in cell culture or in living animals, which has made it possible to observe the activity of neuronal circuits during ongoing behavior.

<span class="mw-page-title-main">Fish allergy</span> Type of food allergy caused by fish

Fish allergy is an immune hypersensitivity to proteins found in fish. Symptoms can be either rapid or gradual in onset. The latter can take hours to days to appear. The former may include anaphylaxis, a potentially life-threatening condition which requires treatment with epinephrine. Other presentations may include atopic dermatitis or inflammation of the esophagus. Fish is one of the eight common food allergens which are responsible for 90% of allergic reactions to foods: cow's milk, eggs, wheat, shellfish, peanuts, tree nuts, fish, and soy beans.

References

  1. 1 2 3 ENSG00000100362 GRCh38: Ensembl release 89: ENSG00000274665, ENSG00000100362 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005716 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Cates MS, Teodoro ML, Phillips GN (March 2002). "Molecular mechanisms of calcium and magnesium binding to parvalbumin". Biophysical Journal. 82 (3): 1133–1146. Bibcode:2002BpJ....82.1133C. doi:10.1016/S0006-3495(02)75472-6. PMC   1301919 . PMID   11867433.
  6. 1 2 Cates MS, Berry MB, Ho EL, Li Q, Potter JD, Phillips GN (October 1999). "Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin". Structure. 7 (10): 1269–1278. doi: 10.1016/S0969-2126(00)80060-X . PMID   10545326.
  7. ↑ Dudev T, Lim C (January 2014). "Competition among metal ions for protein binding sites: determinants of metal ion selectivity in proteins". Chemical Reviews. 114 (1): 538–556. doi:10.1021/cr4004665. PMID   24040963.
  8. ↑ Cowan RL, Wilson CJ, Emson PC, Heizmann CW (December 1990). "Parvalbumin-containing GABAergic interneurons in the rat neostriatum". The Journal of Comparative Neurology. 302 (2): 197–205. doi:10.1002/cne.903020202. PMID   2289971. S2CID   38540563.
  9. ↑ Schwaller B, Meyer M, Schiffmann S (December 2002). "'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): 241–258. doi:10.1080/147342202320883551. PMID   12879963. S2CID   25917565.
  10. ↑ Klausberger T, Marton LF, O'Neill J, Huck JH, Dalezios Y, Fuentealba P, et al. (October 2005). "Complementary roles of cholecystokinin- and parvalbumin-expressing GABAergic neurons in hippocampal network oscillations". The Journal of Neuroscience. 25 (42): 9782–9793. doi:10.1523/JNEUROSCI.3269-05.2005. PMC   6725722 . PMID   16237182. free full text
  11. ↑ Condé F, Lund JS, Jacobowitz DM, Baimbridge KG, Lewis DA (March 1994). "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. doi:10.1002/cne.903410109. PMID   8006226. S2CID   2583429.
  12. ↑ Gabbott PL, Bacon SJ (January 1996). "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): 609–636. doi:10.1002/(SICI)1096-9861(19960122)364:4<609::AID-CNE2>3.0.CO;2-7. PMID   8821450. S2CID   27397665.
  13. ↑ Celio MR, Heizmann CW (June 1982). "Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres". Nature. 297 (5866): 504–506. Bibcode:1982Natur.297..504C. doi:10.1038/297504a0. PMID   6211622. S2CID   4360112.
  14. ↑ Heizmann CW, Berchtold MW, Rowlerson AM (December 1982). "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): 7243–7247. Bibcode:1982PNAS...79.7243H. doi: 10.1073/pnas.79.23.7243 . PMC   347315 . PMID   6961404.
  15. ↑ Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002). "Molecular Motors". Molecular Biology of the Cell (4th ed.). New York: Garland Science. ISBN   0-8153-3218-1.
  16. ↑ Arif SH (April 2009). "A Ca(2+)-binding protein with numerous roles and uses: parvalbumin in molecular biology and physiology". BioEssays. 31 (4): 410–421. doi:10.1002/bies.200800170. PMID   19274659. S2CID   42448973.
  17. ↑ Hashimoto T, Volk DW, Eggan SM, Mirnics K, Pierri JN, Sun Z, et al. (July 2003). "Gene expression deficits in a subclass of GABA neurons in the prefrontal cortex of subjects with schizophrenia". The Journal of Neuroscience. 23 (15): 6315–6326. doi:10.1523/JNEUROSCI.23-15-06315.2003. PMC   6740534 . PMID   12867516.
  18. ↑ Nakazawa K, Zsiros V, Jiang Z, Nakao K, Kolata S, Zhang S, et al. (March 2012). "GABAergic interneuron origin of schizophrenia pathophysiology". Neuropharmacology. 62 (3): 1574–1583. doi:10.1016/j.neuropharm.2011.01.022. PMC   3090452 . PMID   21277876.
  19. ↑ Leung NY, Wai CY, Shu S, Wang J, Kenny TP, Chu KH, et al. (June 2014). "Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review". Clinical Reviews in Allergy & Immunology. 46 (3): 180–197. doi:10.1007/s12016-012-8336-9. PMID   23242979. S2CID   29615377.
  20. 1 2 Stephen JN, Sharp MF, Ruethers T, Taki A, Campbell DE, Lopata AL (March 2017). "Allergenicity of bony and cartilaginous fish - molecular and immunological properties". Clinical and Experimental Allergy. 47 (3): 300–312. doi:10.1111/cea.12892. hdl: 11343/292433 . PMID   28117510. S2CID   22539836.
  21. ↑ Sharp MF, Stephen JN, Kraft L, Weiss T, Kamath SD, Lopata AL (February 2015). "Immunological cross-reactivity between four distant parvalbumins-Impact on allergen detection and diagnostics". Molecular Immunology. 63 (2): 437–448. doi:10.1016/j.molimm.2014.09.019. PMID   25451973.
  22. ↑ Fernandes TJ, Costa J, Carrapatoso I, Oliveira MB, Mafra I (October 2017). "Advances on the molecular characterization, clinical relevance, and detection methods of Gadiform parvalbumin allergens". Critical Reviews in Food Science and Nutrition. 57 (15): 3281–3296. doi:10.1080/10408398.2015.1113157. PMID   26714098. S2CID   22118352.
  23. ↑ Kuehn A, Codreanu-Morel F, Lehners-Weber C, Doyen V, Gomez-André SA, Bienvenu F, et al. (December 2016). "Cross-reactivity to fish and chicken meat - a new clinical syndrome". Allergy. 71 (12): 1772–1781. doi:10.1111/all.12968. PMID   27344988.
  24. 1 2 3 Dijkstra JM, Kondo Y (November 2022). "Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species". Biology. 11 (12): 1713. doi: 10.3390/biology11121713 . PMC   9774829 . PMID   36552222.
  25. 1 2 3 Dijkstra JM, Kuehn A, Sugihara E, Kondo Y (October 2024). "Exploring Fish Parvalbumins through Allergen Names and Gene Identities". Genes. 15 (10): 1337. doi: 10.3390/genes15101337 . PMC   11507022 . PMID   39457461.{{cite journal}}: Check |pmc= value (help)
  26. ↑ Mukherjee S, Bartoš O, Zdeňková K, Hanák P, Horká P, Musilova Z (December 2021). "Evolution of the Parvalbumin Genes in Teleost Fishes after the Whole-Genome Duplication". Fishes. 6 (4): 70. doi: 10.3390/fishes6040070 . ISSN   2410-3888.
  27. ↑ Hamoir G, Konosu S (July 1965). "Carp Myogens of White and Red Muscles. General Composition and Isolation of Low-Molecular-Weight Components of Abnormal Amino Acid Composition". The Biochemical Journal. 96 (1): 85–97. doi:10.1042/bj0960085. PMC   1206910 . PMID   14343157.
  28. ↑ Pechère JF (January 1968). "Muscular parvalbumins as homologous proteins". Comparative Biochemistry and Physiology. 24 (1): 289–295. doi:10.1016/0010-406x(68)90978-x. PMID   5645516.
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