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Showing 1 to 6 of 6 entries
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Expression of Ca(2+) Transport Genes in Platelets and Endothelial Cells in Hypertension.

Hypertension (Dallas, Tex. : 1979)

Mountian, Baba-Aïssa F, Jonas JC, Humbert De Smedt, Wuytack F, Parys JB.
PMID: 11208768
Hypertension. 2001 Jan;37(1):135-141. doi: 10.1161/01.hyp.37.1.135.

-Altered Ca(2+) handling is observed in different cells in essential hypertension. We investigated the expression of sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) and inositol 1,4,5-trisphosphate receptor (IP(3)R) isoforms in platelets and aortic endothelial cells (EC) isolated from spontaneously hypertensive (SHR) and...

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Mountian, Baba-Aïssa F, Jonas JC, et al. Expression of Ca(2+) Transport Genes in Platelets and Endothelial Cells in Hypertension. Hypertension. 2001;37(1):135-141doi: 10.1161/01.hyp.37.1.135.
Mountian, Baba-Aïssa, F., Jonas, J. C., Humbert De Smedt, Wuytack, F., & Parys, J. B. (2001). Expression of Ca(2+) Transport Genes in Platelets and Endothelial Cells in Hypertension. Hypertension (Dallas, Tex. : 1979), 37(1), 135-141. https://doi.org/10.1161/01.hyp.37.1.135
Mountian, Irina, et al. "Expression of Ca(2+) Transport Genes in Platelets and Endothelial Cells in Hypertension." Hypertension (Dallas, Tex. : 1979) vol. 37,1 (2001): 135-141. doi: https://doi.org/10.1161/01.hyp.37.1.135
Mountian, Baba-Aïssa F, Jonas JC, Humbert De Smedt, Wuytack F, Parys JB. Expression of Ca(2+) Transport Genes in Platelets and Endothelial Cells in Hypertension. Hypertension. 2001 Jan;37(1):135-141. doi: 10.1161/01.hyp.37.1.135. PMID: 11208768.
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STIM1 as a key regulator for Ca2+ homeostasis in skeletal-muscle development and function.

Skeletal muscle

Kiviluoto S, Decuypere JP, De Smedt H, Missiaen L, Parys JB, Bultynck G.
PMID: 21798093
Skelet Muscle. 2011 Apr 04;1(1):16. doi: 10.1186/2044-5040-1-16.

Stromal interaction molecules (STIM) were identified as the endoplasmic-reticulum (ER) Ca2+ sensor controlling store-operated Ca2+ entry (SOCE) and Ca2+-release-activated Ca2+ (CRAC) channels in non-excitable cells. STIM proteins target Orai1-3, tetrameric Ca2+-permeable channels in the plasma membrane. Structure-function analysis revealed...

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Kiviluoto S, Decuypere JP, De Smedt H, et al. STIM1 as a key regulator for Ca2+ homeostasis in skeletal-muscle development and function. Skelet Muscle. 2011;1(1):16doi: 10.1186/2044-5040-1-16.
Kiviluoto, S., Decuypere, J. P., De Smedt, H., Missiaen, L., Parys, J. B., & Bultynck, G. (2011). STIM1 as a key regulator for Ca2+ homeostasis in skeletal-muscle development and function. Skeletal muscle, 1(1), 16. https://doi.org/10.1186/2044-5040-1-16
Kiviluoto, Santeri, et al. "STIM1 as a key regulator for Ca2+ homeostasis in skeletal-muscle development and function." Skeletal muscle vol. 1,1 (2011): 16. doi: https://doi.org/10.1186/2044-5040-1-16
Kiviluoto S, Decuypere JP, De Smedt H, Missiaen L, Parys JB, Bultynck G. STIM1 as a key regulator for Ca2+ homeostasis in skeletal-muscle development and function. Skelet Muscle. 2011 Apr 04;1(1):16. doi: 10.1186/2044-5040-1-16. PMID: 21798093; PMCID: PMC3156639.
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Unraveling the role of polycystin-2/inositol 1,4,5-trisphosphate receptor interaction in Ca signaling.

Communicative & integrative biology

Sammels E, Devogelaere B, Mekahli D, Bultynck G, Missiaen L, Parys JB, De Smedt H.
PMID: 21331231
Commun Integr Biol. 2010 Nov;3(6):530-2. doi: 10.4161/cib.3.6.12751. Epub 2010 Nov 01.

Autosomal dominant polycystic kidney disease (ADPKD) arises as a consequence of mutations of the genes PKD1 and PKD2, encoding respectively the integral membrane proteins polycystin-1 and polycystin-2 (TRPP2), resulting in a disturbance in intracellular Ca(2+) signaling. Previously we investigated...

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Sammels E, Devogelaere B, Mekahli D, et al. Unraveling the role of polycystin-2/inositol 1,4,5-trisphosphate receptor interaction in Ca signaling. Commun Integr Biol. 2010;3(6):530-2doi: 10.4161/cib.3.6.12751.
Sammels, E., Devogelaere, B., Mekahli, D., Bultynck, G., Missiaen, L., Parys, J. B., & De Smedt, H. (2010). Unraveling the role of polycystin-2/inositol 1,4,5-trisphosphate receptor interaction in Ca signaling. Communicative & integrative biology, 3(6), 530-2. https://doi.org/10.4161/cib.3.6.12751
Sammels, Eva, et al. "Unraveling the role of polycystin-2/inositol 1,4,5-trisphosphate receptor interaction in Ca signaling." Communicative & integrative biology vol. 3,6 (2010): 530-2. doi: https://doi.org/10.4161/cib.3.6.12751
Sammels E, Devogelaere B, Mekahli D, Bultynck G, Missiaen L, Parys JB, De Smedt H. Unraveling the role of polycystin-2/inositol 1,4,5-trisphosphate receptor interaction in Ca signaling. Commun Integr Biol. 2010 Nov;3(6):530-2. doi: 10.4161/cib.3.6.12751. Epub 2010 Nov 01. PMID: 21331231; PMCID: PMC3038055.
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IP(3) Receptors, Mitochondria, and Ca Signaling: Implications for Aging.

Journal of aging research

Decuypere JP, Monaco G, Missiaen L, De Smedt H, Parys JB, Bultynck G.
PMID: 21423550
J Aging Res. 2011 Mar 08;2011:920178. doi: 10.4061/2011/920178.

The tight interplay between endoplasmic-reticulum-(ER-) and mitochondria-mediated Ca(2+) signaling is a key determinant of cellular health and cellular fate through the control of apoptosis and autophagy. Proteins that prevent or promote apoptosis and autophagy can affect intracellular Ca(2+) dynamics...

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Decuypere JP, Monaco G, Missiaen L, et al. IP(3) Receptors, Mitochondria, and Ca Signaling: Implications for Aging. J Aging Res. 2011;2011:920178doi: 10.4061/2011/920178.
Decuypere, J. P., Monaco, G., Missiaen, L., De Smedt, H., Parys, J. B., & Bultynck, G. (2011). IP(3) Receptors, Mitochondria, and Ca Signaling: Implications for Aging. Journal of aging research, 2011920178. https://doi.org/10.4061/2011/920178
Decuypere, Jean-Paul, et al. "IP(3) Receptors, Mitochondria, and Ca Signaling: Implications for Aging." Journal of aging research vol. 2011 (2011): 920178. doi: https://doi.org/10.4061/2011/920178
Decuypere JP, Monaco G, Missiaen L, De Smedt H, Parys JB, Bultynck G. IP(3) Receptors, Mitochondria, and Ca Signaling: Implications for Aging. J Aging Res. 2011 Mar 08;2011:920178. doi: 10.4061/2011/920178. PMID: 21423550; PMCID: PMC3056293.
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Reciprocal sensitivity of diffuse large B-cell lymphoma cells to Bcl-2 inhibitors BIRD-2 versus venetoclax.

Oncotarget

Vervloessem T, Akl H, Tousseyn T, De Smedt H, Parys JB, Bultynck G.
PMID: 29340082
Oncotarget. 2017 Dec 04;8(67):111656-111671. doi: 10.18632/oncotarget.22898. eCollection 2017 Dec 19.

Bcl-2 is often upregulated in cancers to neutralize the BH3-only protein Bim at the mitochondria. BH3 mimetics (e.g. ABT-199 (venetoclax)) kill cancer cells by targeting Bcl-2's hydrophobic cleft and disrupting Bcl-2/Bim complexes. Some cancers with elevated Bcl-2 display poor...

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Vervloessem T, Akl H, Tousseyn T, et al. Reciprocal sensitivity of diffuse large B-cell lymphoma cells to Bcl-2 inhibitors BIRD-2 versus venetoclax. Oncotarget. 2017;8(67):111656-111671doi: 10.18632/oncotarget.22898.
Vervloessem, T., Akl, H., Tousseyn, T., De Smedt, H., Parys, J. B., & Bultynck, G. (2017). Reciprocal sensitivity of diffuse large B-cell lymphoma cells to Bcl-2 inhibitors BIRD-2 versus venetoclax. Oncotarget, 8(67), 111656-111671. https://doi.org/10.18632/oncotarget.22898
Vervloessem, Tamara, et al. "Reciprocal sensitivity of diffuse large B-cell lymphoma cells to Bcl-2 inhibitors BIRD-2 versus venetoclax." Oncotarget vol. 8,67 (2017): 111656-111671. doi: https://doi.org/10.18632/oncotarget.22898
Vervloessem T, Akl H, Tousseyn T, De Smedt H, Parys JB, Bultynck G. Reciprocal sensitivity of diffuse large B-cell lymphoma cells to Bcl-2 inhibitors BIRD-2 versus venetoclax. Oncotarget. 2017 Dec 04;8(67):111656-111671. doi: 10.18632/oncotarget.22898. eCollection 2017 Dec 19. PMID: 29340082; PMCID: PMC5762350.
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PKD2/polycystin-2 induces autophagy by forming a complex with BECN1.

Autophagy

Peña-Oyarzun D, Rodriguez-Peña M, Burgos-Bravo F, Vergara A, Kretschmar C, Sotomayor-Flores C, Ramirez-Sarmiento CA, De Smedt H, Reyes M, Perez W, Torres VA, Morselli E, Altamirano F, Wilson CAM, Hill JA, Lavandero S, Criollo A.
PMID: 32543276
Autophagy. 2021 Jul;17(7):1714-1728. doi: 10.1080/15548627.2020.1782035. Epub 2020 Jun 30.

Macroautophagy/autophagy is an intracellular process involved in the breakdown of macromolecules and organelles. Recent studies have shown that PKD2/PC2/TRPP2 (polycystin 2, transient receptor potential cation channel), a nonselective cation channel permeable to Ca

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Peña-Oyarzun D, Rodriguez-Peña M, Burgos-Bravo F, et al. PKD2/polycystin-2 induces autophagy by forming a complex with BECN1. Autophagy. 2020;17(7):1714-1728doi: 10.1080/15548627.2020.1782035.
Peña-Oyarzun, D., Rodriguez-Peña, M., Burgos-Bravo, F., Vergara, A., Kretschmar, C., Sotomayor-Flores, C., Ramirez-Sarmiento, C. A., De Smedt, H., Reyes, M., Perez, W., Torres, V. A., Morselli, E., Altamirano, F., Wilson, C. A. M., Hill, J. A., Lavandero, S., & Criollo, A. (2021). PKD2/polycystin-2 induces autophagy by forming a complex with BECN1. Autophagy, 17(7), 1714-1728. https://doi.org/10.1080/15548627.2020.1782035
Peña-Oyarzun, Daniel, et al. "PKD2/polycystin-2 induces autophagy by forming a complex with BECN1." Autophagy vol. 17,7 (2021): 1714-1728. doi: https://doi.org/10.1080/15548627.2020.1782035
Peña-Oyarzun D, Rodriguez-Peña M, Burgos-Bravo F, Vergara A, Kretschmar C, Sotomayor-Flores C, Ramirez-Sarmiento CA, De Smedt H, Reyes M, Perez W, Torres VA, Morselli E, Altamirano F, Wilson CAM, Hill JA, Lavandero S, Criollo A. PKD2/polycystin-2 induces autophagy by forming a complex with BECN1. Autophagy. 2021 Jul;17(7):1714-1728. doi: 10.1080/15548627.2020.1782035. Epub 2020 Jun 30. PMID: 32543276; PMCID: PMC8354594.
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Showing 1 to 6 of 6 entries