Immunohistochemical localization of parvalbumin calcium-binding protein in the heart tissues of various species

Vongvatcharanon, Surapong; Vongvatcharanon, Uraporn; Boonyoung, Piyakorn

doi:10.1016/j.acthis.2007.05.005

Cited by 6 publications

(2 citation statements)

References 20 publications

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“…PGC-1α is abundantly expressed in heart and skeletal muscle (Puigserver et al, 1998), and these tissues express PV as well (Heizmann et al, 1982; Vongvatcharanon et al, 2008). We also wanted to investigate the expression of PV in the retina; although the expression of PGC-1α has not yet been examined in the retina, PV is found in AII amacrine cells (Wassle et al, 1993).…”

Section: Resultsmentioning

confidence: 99%

Parvalbumin Deficiency and GABAergic Dysfunction in Mice Lacking PGC-1α

Lucas¹,

Markwardt²,

et al. 2010

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The transcriptional coactivator peroxisome proliferator-activated receptor ␥ coactivator 1␣ (PGC-1␣) is a master regulator of metabolism in peripheral tissues, and it has been proposed that PGC-1␣ plays a similar role in the brain. Recent evidence suggests that PGC-1␣ is concentrated in GABAergic interneurons, so we investigated whether male and female PGC-1␣ Ϫ/Ϫ mice exhibit abnormalities in interneuron gene expression and/or function. We found a striking reduction in the expression of the Ca 2ϩ -binding protein parvalbumin (PV), but not other GABAergic markers, throughout the cerebrum in PGC-1␣ ϩ/Ϫ and Ϫ/Ϫ mice. Furthermore, PGC-1␣ overexpression in cell culture was sufficient to robustly induce PV expression. Consistent with a reduction in PV rather than a loss of PV-expressing interneurons, spontaneous synaptic inhibition was not altered in PGC-1␣ Ϫ/Ϫ mice. However, evoked synaptic responses displayed less paired-pulse depression and dramatic facilitation in response to repetitive stimulation at the gamma frequency. PV transcript expression was also significantly reduced in retina and heart of PGC-1␣ Ϫ/Ϫ animals, suggesting that PGC-1␣ is required for proper expression of PV in multiple tissues. Together these findings indicate that PGC-1␣ is a novel regulator of interneuron gene expression and function and a potential therapeutic target for neurological disorders associated with interneuron dysfunction.

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Section: Resultsmentioning

confidence: 99%

Parvalbumin Deficiency and GABAergic Dysfunction in Mice Lacking PGC-1α

Lucas¹,

Markwardt²,

et al. 2010

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“…In addition to fast skeletal muscles, PA has also been found in cardiac muscle tissue of rat, mouse, chicken, rabbit, and pig [56,57], and it was revealed that PA takes part in the relaxation of cardiac myocytes [58][59][60][61][62][63]. It has been suggested [60] that at the end of systole, Ca 2+ dissociates from troponin C and binds to PA, which causes cardiac myocyte relaxation.…”

Section: Parvalbumin In Muscle Cellsmentioning

confidence: 99%

What Is Parvalbumin for?

Permyakov

Uversky

2022

Biomolecules

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Parvalbumin (PA) is a small, acidic, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily. Structural and physical properties of PA are well studied but recently two highly conserved structural motifs consisting of three amino acids each (clusters I and II), which contribute to the hydrophobic core of the EF-hand domains, have been revealed. Despite several decades of studies, physiological functions of PA are still poorly known. Since no target proteins have been revealed for PA so far, it is believed that PA acts as a slow calcium buffer. Numerous experiments on various muscle systems have shown that PA accelerates the relaxation of fast skeletal muscles. It has been found that oxidation of PA by reactive oxygen species (ROS) is conformation-dependent and one more physiological function of PA in fast muscles could be a protection of these cells from ROS. PA is thought to regulate calcium-dependent metabolic and electric processes within the population of gamma-aminobutyric acid (GABA) neurons. Genetic elimination of PA results in changes in GABAergic synaptic transmission. Mammalian oncomodulin (OM), the β isoform of PA, is expressed mostly in cochlear outer hair cells and in vestibular hair cells. OM knockout mice lose their hearing after 3–4 months. It was suggested that, in sensory cells, OM maintains auditory function, most likely affecting outer hair cells’ motility mechanisms.

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2010

Calcium Binding Proteins

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Immunohistochemical localization of parvalbumin calcium-binding protein in the heart tissues of various species

Cited by 6 publications

References 20 publications

Parvalbumin Deficiency and GABAergic Dysfunction in Mice Lacking PGC-1α

Parvalbumin Deficiency and GABAergic Dysfunction in Mice Lacking PGC-1α

What Is Parvalbumin for?

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