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Effects of Calyculin a on the Motility and Protein Phosphorylation in Frozen-Thawed Bull Spermatozoa.

Zoological science

Ogata H, Tsukamoto M, Yamashita K, Iwamori T, Takahashi H, Kaneko T, Iwamori N, Inai T, Iida H.
PMID: 34854285
Zoolog Sci. 2021 Dec;38(6):531-543. doi: 10.2108/zs210046.

In this study, we examined the effects of calyculin A, a phosphatase inhibitor, on motility, protein phosphorylation, and the distribution of phospho-(Ser/Thr) PKA substrates in frozen-thawed bull spermatozoa that are actually used by most farmers for breeding. The data...

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Ogata H, Tsukamoto M, Yamashita K, et al. Effects of Calyculin a on the Motility and Protein Phosphorylation in Frozen-Thawed Bull Spermatozoa. Zoolog Sci. 2021;38(6):531-543doi: 10.2108/zs210046.
Ogata, H., Tsukamoto, M., Yamashita, K., Iwamori, T., Takahashi, H., Kaneko, T., Iwamori, N., Inai, T., & Iida, H. (2021). Effects of Calyculin a on the Motility and Protein Phosphorylation in Frozen-Thawed Bull Spermatozoa. Zoological science, 38(6), 531-543. https://doi.org/10.2108/zs210046
Ogata, Honami, et al. "Effects of Calyculin a on the Motility and Protein Phosphorylation in Frozen-Thawed Bull Spermatozoa." Zoological science vol. 38,6 (2021): 531-543. doi: https://doi.org/10.2108/zs210046
Ogata H, Tsukamoto M, Yamashita K, Iwamori T, Takahashi H, Kaneko T, Iwamori N, Inai T, Iida H. Effects of Calyculin a on the Motility and Protein Phosphorylation in Frozen-Thawed Bull Spermatozoa. Zoolog Sci. 2021 Dec;38(6):531-543. doi: 10.2108/zs210046. PMID: 34854285.
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Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells.

Proceedings of the National Academy of Sciences of the United States of America

Chandra S, Low PS.
PMID: 11607537
Proc Natl Acad Sci U S A. 1995 May 09;92(10):4120-3. doi: 10.1073/pnas.92.10.4120.

The oxidative burst is likely the most rapid defense response mounted by a plant under pathogen attack, and the generated oxidant species may be essential to several subsequent defense responses. In our effort to characterize the signal-transduction pathways leading...

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Chandra S, Low PS. Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells. Proc Natl Acad Sci U S A. 1995;92(10):4120-3doi: 10.1073/pnas.92.10.4120.
Chandra, S., & Low, P. S. (1995). Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells. Proceedings of the National Academy of Sciences of the United States of America, 92(10), 4120-3. https://doi.org/10.1073/pnas.92.10.4120
Chandra, S, and Low, P S. "Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells." Proceedings of the National Academy of Sciences of the United States of America vol. 92,10 (1995): 4120-3. doi: https://doi.org/10.1073/pnas.92.10.4120
Chandra S, Low PS. Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells. Proc Natl Acad Sci U S A. 1995 May 09;92(10):4120-3. doi: 10.1073/pnas.92.10.4120. PMID: 11607537; PMCID: PMC41896.
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Pharmacological approach to increase the retention of radiation induced gamma-H2AX foci using phosphatase inhibitors: significance in radiation biodosimetry.

Journal of radiological protection : official journal of the Society for Radiological Protection

Nayak AA, Mumbrekar KD, Rao S.
PMID: 29353813
J Radiol Prot. 2018 Jan 22; doi: 10.1088/1361-6498/aaa97a. Epub 2018 Jan 22.

In a scenario of accidental mass radiation exposure, transportation and analyzing samples may take its time resulting in loss of biomarker information over this period. The present study aims to use phosphatases inhibitors for longer retention of foci signals...

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Nayak AA, Mumbrekar KD, Rao S. Pharmacological approach to increase the retention of radiation induced gamma-H2AX foci using phosphatase inhibitors: significance in radiation biodosimetry. J Radiol Prot. 2018;doi: 10.1088/1361-6498/aaa97a.
Nayak, A. A., Mumbrekar, K. D., & Rao, S. (2018). Pharmacological approach to increase the retention of radiation induced gamma-H2AX foci using phosphatase inhibitors: significance in radiation biodosimetry. Journal of radiological protection : official journal of the Society for Radiological Protection, . https://doi.org/10.1088/1361-6498/aaa97a
Nayak, Akshaykumar A, et al. "Pharmacological approach to increase the retention of radiation induced gamma-H2AX foci using phosphatase inhibitors: significance in radiation biodosimetry." Journal of radiological protection : official journal of the Society for Radiological Protection vol. (2018). doi: https://doi.org/10.1088/1361-6498/aaa97a
Nayak AA, Mumbrekar KD, Rao S. Pharmacological approach to increase the retention of radiation induced gamma-H2AX foci using phosphatase inhibitors: significance in radiation biodosimetry. J Radiol Prot. 2018 Jan 22; doi: 10.1088/1361-6498/aaa97a. Epub 2018 Jan 22. PMID: 29353813.
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Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ.

World journal of biological chemistry

Samuels AL, Louw A, Zareie R, Ingley E.
PMID: 28924458
World J Biol Chem. 2017 Aug 26;8(3):163-174. doi: 10.4331/wjbc.v8.i3.163.

AIM: To identify and characterize the effect of phosphorylation on the subcellular localization of Ankrd54.METHODS: HEK293T cells were treated with calyculin A, staurosporin or phorbol 12-myristate 13-acetate (PMA). Cells were transfected with eGFP-tagged Ankrd54 with or without Lyn tyrosine...

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Samuels AL, Louw A, Zareie R, et al. Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ. World J Biol Chem. 2017;8(3):163-174doi: 10.4331/wjbc.v8.i3.163.
Samuels, A. L., Louw, A., Zareie, R., & Ingley, E. (2017). Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ. World journal of biological chemistry, 8(3), 163-174. https://doi.org/10.4331/wjbc.v8.i3.163
Samuels, Amy L, et al. "Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ." World journal of biological chemistry vol. 8,3 (2017): 163-174. doi: https://doi.org/10.4331/wjbc.v8.i3.163
Samuels AL, Louw A, Zareie R, Ingley E. Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ. World J Biol Chem. 2017 Aug 26;8(3):163-174. doi: 10.4331/wjbc.v8.i3.163. PMID: 28924458; PMCID: PMC5579962.
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Emetine regulates the alternative splicing of caspase 9 in tumor cells.

Oncology letters

Pan D, Boon-Unge K, Govitrapong P, Zhou J.
PMID: 22848307
Oncol Lett. 2011 Nov;2(6):1309-1312. doi: 10.3892/ol.2011.395. Epub 2011 Aug 29.

Exons 3 to 6 in the caspase 9 gene undergo alternative splicing in which the larger caspase 9 splice variant promotes apoptosis, in contrast to the dominant negative anti-apoptotic splice variant, the smaller caspase 9b. In this study, the...

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Pan D, Boon-Unge K, Govitrapong P, et al. Emetine regulates the alternative splicing of caspase 9 in tumor cells. Oncol Lett. 2011;2(6):1309-1312doi: 10.3892/ol.2011.395.
Pan, D., Boon-Unge, K., Govitrapong, P., & Zhou, J. (2011). Emetine regulates the alternative splicing of caspase 9 in tumor cells. Oncology letters, 2(6), 1309-1312. https://doi.org/10.3892/ol.2011.395
Pan, Danmin, et al. "Emetine regulates the alternative splicing of caspase 9 in tumor cells." Oncology letters vol. 2,6 (2011): 1309-1312. doi: https://doi.org/10.3892/ol.2011.395
Pan D, Boon-Unge K, Govitrapong P, Zhou J. Emetine regulates the alternative splicing of caspase 9 in tumor cells. Oncol Lett. 2011 Nov;2(6):1309-1312. doi: 10.3892/ol.2011.395. Epub 2011 Aug 29. PMID: 22848307; PMCID: PMC3406502.
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Comparative cytotoxic effects of two protein phosphatase inhibitors, okadaic acid and calyculin A, on thyroid cells.

Cell death and differentiation

Golstein J, Swillens S, Dumont JE.
PMID: 17180037
Cell Death Differ. 1995 Oct;2(4):321-9.

The cytotoxicity of two inhibitors of protein phosphatases PP1 and PP2A has been investigated on primary cultures of dog thyrocytes. Both compounds, okadaic acid and calyculin A elicited dose- and time- related effects, i.e. apoptosis and necrosis. In addition...

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Golstein J, Swillens S, Dumont JE. Comparative cytotoxic effects of two protein phosphatase inhibitors, okadaic acid and calyculin A, on thyroid cells. Cell Death Differ. 1995;2(4):321-9
Golstein, J., Swillens, S., & Dumont, J. E. (1995). Comparative cytotoxic effects of two protein phosphatase inhibitors, okadaic acid and calyculin A, on thyroid cells. Cell death and differentiation, 2(4), 321-9.
Golstein, J, et al. "Comparative cytotoxic effects of two protein phosphatase inhibitors, okadaic acid and calyculin A, on thyroid cells." Cell death and differentiation vol. 2,4 (1995): 321-9.
Golstein J, Swillens S, Dumont JE. Comparative cytotoxic effects of two protein phosphatase inhibitors, okadaic acid and calyculin A, on thyroid cells. Cell Death Differ. 1995 Oct;2(4):321-9. PMID: 17180037.
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Calyculin A, an enhancer of myosin, speeds up anaphase chromosome movement.

Cell & chromosome

Fabian L, Troscianczuk J, Forer A.
PMID: 17381845
Cell Chromosome. 2007 Mar 24;6:1. doi: 10.1186/1475-9268-6-1.

Actin and myosin inhibitors often blocked anaphase movements in insect spermatocytes in previous experiments. Here we treat cells with an enhancer of myosin, Calyculin A, which inhibits myosin-light-chain phosphatase from dephosphorylating myosin; myosin thus is hyperactivated. Calyculin A causes...

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Fabian L, Troscianczuk J, Forer A. Calyculin A, an enhancer of myosin, speeds up anaphase chromosome movement. Cell Chromosome. 2007;6:1doi: 10.1186/1475-9268-6-1.
Fabian, L., Troscianczuk, J., & Forer, A. (2007). Calyculin A, an enhancer of myosin, speeds up anaphase chromosome movement. Cell & chromosome, 61. https://doi.org/10.1186/1475-9268-6-1
Fabian, Lacramioara, et al. "Calyculin A, an enhancer of myosin, speeds up anaphase chromosome movement." Cell & chromosome vol. 6 (2007): 1. doi: https://doi.org/10.1186/1475-9268-6-1
Fabian L, Troscianczuk J, Forer A. Calyculin A, an enhancer of myosin, speeds up anaphase chromosome movement. Cell Chromosome. 2007 Mar 24;6:1. doi: 10.1186/1475-9268-6-1. PMID: 17381845; PMCID: PMC1847834.
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Alpha-mangostin dephosphorylates ERM to induce adhesion and decrease surface stiffness in KG-1 cells.

Human cell

Phan TKT, Do TL, Tachibana K, Kihara T.
PMID: 34817798
Hum Cell. 2021 Nov 24; doi: 10.1007/s13577-021-00651-8. Epub 2021 Nov 24.

Surface stiffness is a unique indicator of various cellular states and events and needs to be tightly controlled. α-Mangostin, a natural compound with numerous bioactivities, reduces the mechanical stiffness of various cells; however, the mechanism by which it affects...

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Phan TKT, Do TL, Tachibana K, et al. Alpha-mangostin dephosphorylates ERM to induce adhesion and decrease surface stiffness in KG-1 cells. Hum Cell. 2021;doi: 10.1007/s13577-021-00651-8.
Phan, T. K. T., Do, T. L., Tachibana, K., & Kihara, T. (2021). Alpha-mangostin dephosphorylates ERM to induce adhesion and decrease surface stiffness in KG-1 cells. Human cell, . https://doi.org/10.1007/s13577-021-00651-8
Phan, Thi Kieu Trang, et al. "Alpha-mangostin dephosphorylates ERM to induce adhesion and decrease surface stiffness in KG-1 cells." Human cell vol. (2021). doi: https://doi.org/10.1007/s13577-021-00651-8
Phan TKT, Do TL, Tachibana K, Kihara T. Alpha-mangostin dephosphorylates ERM to induce adhesion and decrease surface stiffness in KG-1 cells. Hum Cell. 2021 Nov 24; doi: 10.1007/s13577-021-00651-8. Epub 2021 Nov 24. PMID: 34817798.
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Denatonium and 6-n-Propyl-2-thiouracil, Agonists of Bitter Taste Receptor, Inhibit Contraction of Various Types of Smooth Muscles in the Rat and Mouse.

Biological & pharmaceutical bulletin

Sakai H, Sato K, Kai Y, Chiba Y, Narita M.
PMID: 27110632
Biol Pharm Bull. 2016;39(1):33-41.

Recently the global expression of taste 2 receptors (TAS2Rs) on smooth muscle cells in human airways was demonstrated. Here, the effects of agonists of taste receptor, type 2, denatonium and 6-n-propyl-2-thiouracil, on smooth-muscle contraction were examined in the rat...

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Sakai H, Sato K, Kai Y, et al. Denatonium and 6-n-Propyl-2-thiouracil, Agonists of Bitter Taste Receptor, Inhibit Contraction of Various Types of Smooth Muscles in the Rat and Mouse. Biol Pharm Bull. 2016;39(1):33-41
Sakai, H., Sato, K., Kai, Y., Chiba, Y., & Narita, M. (2016). Denatonium and 6-n-Propyl-2-thiouracil, Agonists of Bitter Taste Receptor, Inhibit Contraction of Various Types of Smooth Muscles in the Rat and Mouse. Biological & pharmaceutical bulletin, 39(1), 33-41.
Sakai, Hiroyasu, et al. "Denatonium and 6-n-Propyl-2-thiouracil, Agonists of Bitter Taste Receptor, Inhibit Contraction of Various Types of Smooth Muscles in the Rat and Mouse." Biological & pharmaceutical bulletin vol. 39,1 (2016): 33-41.
Sakai H, Sato K, Kai Y, Chiba Y, Narita M. Denatonium and 6-n-Propyl-2-thiouracil, Agonists of Bitter Taste Receptor, Inhibit Contraction of Various Types of Smooth Muscles in the Rat and Mouse. Biol Pharm Bull. 2016;39(1):33-41. PMID: 27110632.
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Blocking Protein Phosphatase 1 [PP1] Prevents Loss of Tether Elasticity in Anaphase Crane-Fly Spermatocytes.

Frontiers in molecular biosciences

Forer A, Adil A, Berns MW.
PMID: 34169091
Front Mol Biosci. 2021 Jun 08;8:636746. doi: 10.3389/fmolb.2021.636746. eCollection 2021.

In normal anaphase cells, telomeres of each separating chromosome pair are connected to each other by tethers. Tethers are elastic at the start of anaphase: arm fragments cut from anaphase chromosomes in early anaphase move across the equator to...

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Forer A, Adil A, Berns MW. Blocking Protein Phosphatase 1 [PP1] Prevents Loss of Tether Elasticity in Anaphase Crane-Fly Spermatocytes. Front Mol Biosci. 2021;8:636746doi: 10.3389/fmolb.2021.636746.
Forer, A., Adil, A., & Berns, M. W. (2021). Blocking Protein Phosphatase 1 [PP1] Prevents Loss of Tether Elasticity in Anaphase Crane-Fly Spermatocytes. Frontiers in molecular biosciences, 8636746. https://doi.org/10.3389/fmolb.2021.636746
Forer, Arthur, et al. "Blocking Protein Phosphatase 1 [PP1] Prevents Loss of Tether Elasticity in Anaphase Crane-Fly Spermatocytes." Frontiers in molecular biosciences vol. 8 (2021): 636746. doi: https://doi.org/10.3389/fmolb.2021.636746
Forer A, Adil A, Berns MW. Blocking Protein Phosphatase 1 [PP1] Prevents Loss of Tether Elasticity in Anaphase Crane-Fly Spermatocytes. Front Mol Biosci. 2021 Jun 08;8:636746. doi: 10.3389/fmolb.2021.636746. eCollection 2021. PMID: 34169091; PMCID: PMC8218814.
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Transient Activation and Tyrosine Phosphorylation of a Protein Kinase in Tobacco Cells Treated with a Fungal Elicitor.

The Plant cell

Suzuki K, Shinshi H.
PMID: 12242379
Plant Cell. 1995 May;7(5):639-647. doi: 10.1105/tpc.7.5.639.

Suspension-cultured tobacco cells respond to fungal elicitor by activating the transcription of so-called defense genes. This response has been shown to be blocked by staurosporine, an inhibitor of protein kinases, and by Gd3+, which blocks Ca2+ channels. We report...

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Suzuki K, Shinshi H. Transient Activation and Tyrosine Phosphorylation of a Protein Kinase in Tobacco Cells Treated with a Fungal Elicitor. Plant Cell. 1995;7(5):639-647doi: 10.1105/tpc.7.5.639.
Suzuki, K., & Shinshi, H. (1995). Transient Activation and Tyrosine Phosphorylation of a Protein Kinase in Tobacco Cells Treated with a Fungal Elicitor. The Plant cell, 7(5), 639-647. https://doi.org/10.1105/tpc.7.5.639
Suzuki, K., and Shinshi, H.. "Transient Activation and Tyrosine Phosphorylation of a Protein Kinase in Tobacco Cells Treated with a Fungal Elicitor." The Plant cell vol. 7,5 (1995): 639-647. doi: https://doi.org/10.1105/tpc.7.5.639
Suzuki K, Shinshi H. Transient Activation and Tyrosine Phosphorylation of a Protein Kinase in Tobacco Cells Treated with a Fungal Elicitor. Plant Cell. 1995 May;7(5):639-647. doi: 10.1105/tpc.7.5.639. PMID: 12242379; PMCID: PMC160810.
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The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate.

Proceedings of the National Academy of Sciences of the United States of America

Felix G, Regenass M, Spanu P, Boller T.
PMID: 11607454
Proc Natl Acad Sci U S A. 1994 Feb 01;91(3):952-6. doi: 10.1073/pnas.91.3.952.

Suspension-cultured tomato cells react to microbial signals, so-called elicitors, with rapid alkalinization of the growth medium and increased biosynthesis of the stress hormone ethylene. These responses to elicitors can be blocked by staurosporine and K-252a, two specific inhibitors of...

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Felix G, Regenass M, Spanu P, et al. The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate. Proc Natl Acad Sci U S A. 1994;91(3):952-6doi: 10.1073/pnas.91.3.952.
Felix, G., Regenass, M., Spanu, P., & Boller, T. (1994). The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate. Proceedings of the National Academy of Sciences of the United States of America, 91(3), 952-6. https://doi.org/10.1073/pnas.91.3.952
Felix, G, et al. "The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate." Proceedings of the National Academy of Sciences of the United States of America vol. 91,3 (1994): 952-6. doi: https://doi.org/10.1073/pnas.91.3.952
Felix G, Regenass M, Spanu P, Boller T. The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate. Proc Natl Acad Sci U S A. 1994 Feb 01;91(3):952-6. doi: 10.1073/pnas.91.3.952. PMID: 11607454; PMCID: PMC521431.
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Showing 1 to 12 of 32 entries