Tumor promoting properties of a cigarette smoke prevalent polycyclic aromatic hydrocarbon as indicated by the inhibition of gap junctional intercellular communication via phosphatidylcholine-specific phospholipase C
Аутори
Upham, Brad L.Blaha, Ludek
Babica, Pavel
Park, Joon-Suk
Sovadinova, Iva
Pudrith, Charles
Rummel, Alisa M.
Weis, Liliane M.
Sai, Kimie
Tithof, Patti K.
Gužvić, Miodrag
Vondracek, Jan
Machala, Miroslav
Trosko, James E.
Чланак у часопису
Метаподаци
Приказ свих података о документуАпстракт
Inhibition of gap junctional intercellular communication (GJIC) and the activation of intracellular mitogenic pathways are common hallmarks of epithelial derived cancer cells. We previously determined that the 1-methyl and not the 2-methyl isomer of anthracene, which are prominent cigarette smoke components, activated extracellular receptor kinase, and inhibited GJIC in WB-F344 rat liver epithelial cells. Using these same cells, we show that an immediate upstream response to 1-methylanthracene was a rapid ( LT 1 min) release of arachidonic acid. Inhibition of phosphatidylcholine-specific phospholipase C prevented the inhibition of GJIC by 1-methylanthracene. In contrast, inhibition of phosphatidylinositol specific phospholipase C, phospholipase A(2), diacylglycerol lipase, phospholipase D, protein kinase C, and tyrosine protein kinases had no effect on 1-methylanthracene-induced inhibition of GJIC. Inhibition of protein kinase A also prevented inhibition of GJIC by 1-methylanthracene. ...Direct measurement of phosphatidylcholine-specific phospholipase C and sphingomyelinase indicated that only phosphatidylcholine-specific phospholipase C was activated in response to 1-methylanthracene, while 2-methylanthracene had no effect. 1-methylanthracene also activated p38-mitogen activated protein kinase; however, like extracellular kinase, its activation was not involved in 1-methylanthracene-induced regulation of GJIC, and this activation was independent of phosphatidylcholine-specific phospholipase C. Although mitogen activated protein kinases were activated, Western blot analyzes indicated no change in connexin43 phosphorylation status. Our results indicate that phosphatidylcholine-specific phospholipase C is an important enzyme in the induction of a tumorigenic phenotype, namely the inhibition of GJIC; whereas mitogen activated protein kinases triggered in response to 1-methylanthracene, were not involved in the deregulation of GJIC.
Извор:
Cancer Science, 2008, 99, 4, 696-705Финансирање / пројекти:
- NIEHS NIH HHS [R01 ES013268, R01 ES013268-01A2], FIC NIH HHS [5D43 TW00641-10, D43 TW000641]
DOI: 10.1111/j.1349-7006.2008.00752.x
ISSN: 1347-9032
PubMed: 18377422
WoS: 000254498800011
Scopus: 2-s2.0-41249096480
Колекције
Институција/група
VinčaTY - JOUR AU - Upham, Brad L. AU - Blaha, Ludek AU - Babica, Pavel AU - Park, Joon-Suk AU - Sovadinova, Iva AU - Pudrith, Charles AU - Rummel, Alisa M. AU - Weis, Liliane M. AU - Sai, Kimie AU - Tithof, Patti K. AU - Gužvić, Miodrag AU - Vondracek, Jan AU - Machala, Miroslav AU - Trosko, James E. PY - 2008 UR - https://vinar.vin.bg.ac.rs/handle/123456789/3396 AB - Inhibition of gap junctional intercellular communication (GJIC) and the activation of intracellular mitogenic pathways are common hallmarks of epithelial derived cancer cells. We previously determined that the 1-methyl and not the 2-methyl isomer of anthracene, which are prominent cigarette smoke components, activated extracellular receptor kinase, and inhibited GJIC in WB-F344 rat liver epithelial cells. Using these same cells, we show that an immediate upstream response to 1-methylanthracene was a rapid ( LT 1 min) release of arachidonic acid. Inhibition of phosphatidylcholine-specific phospholipase C prevented the inhibition of GJIC by 1-methylanthracene. In contrast, inhibition of phosphatidylinositol specific phospholipase C, phospholipase A(2), diacylglycerol lipase, phospholipase D, protein kinase C, and tyrosine protein kinases had no effect on 1-methylanthracene-induced inhibition of GJIC. Inhibition of protein kinase A also prevented inhibition of GJIC by 1-methylanthracene. Direct measurement of phosphatidylcholine-specific phospholipase C and sphingomyelinase indicated that only phosphatidylcholine-specific phospholipase C was activated in response to 1-methylanthracene, while 2-methylanthracene had no effect. 1-methylanthracene also activated p38-mitogen activated protein kinase; however, like extracellular kinase, its activation was not involved in 1-methylanthracene-induced regulation of GJIC, and this activation was independent of phosphatidylcholine-specific phospholipase C. Although mitogen activated protein kinases were activated, Western blot analyzes indicated no change in connexin43 phosphorylation status. Our results indicate that phosphatidylcholine-specific phospholipase C is an important enzyme in the induction of a tumorigenic phenotype, namely the inhibition of GJIC; whereas mitogen activated protein kinases triggered in response to 1-methylanthracene, were not involved in the deregulation of GJIC. T2 - Cancer Science T1 - Tumor promoting properties of a cigarette smoke prevalent polycyclic aromatic hydrocarbon as indicated by the inhibition of gap junctional intercellular communication via phosphatidylcholine-specific phospholipase C VL - 99 IS - 4 SP - 696 EP - 705 DO - 10.1111/j.1349-7006.2008.00752.x ER -
@article{ author = "Upham, Brad L. and Blaha, Ludek and Babica, Pavel and Park, Joon-Suk and Sovadinova, Iva and Pudrith, Charles and Rummel, Alisa M. and Weis, Liliane M. and Sai, Kimie and Tithof, Patti K. and Gužvić, Miodrag and Vondracek, Jan and Machala, Miroslav and Trosko, James E.", year = "2008", abstract = "Inhibition of gap junctional intercellular communication (GJIC) and the activation of intracellular mitogenic pathways are common hallmarks of epithelial derived cancer cells. We previously determined that the 1-methyl and not the 2-methyl isomer of anthracene, which are prominent cigarette smoke components, activated extracellular receptor kinase, and inhibited GJIC in WB-F344 rat liver epithelial cells. Using these same cells, we show that an immediate upstream response to 1-methylanthracene was a rapid ( LT 1 min) release of arachidonic acid. Inhibition of phosphatidylcholine-specific phospholipase C prevented the inhibition of GJIC by 1-methylanthracene. In contrast, inhibition of phosphatidylinositol specific phospholipase C, phospholipase A(2), diacylglycerol lipase, phospholipase D, protein kinase C, and tyrosine protein kinases had no effect on 1-methylanthracene-induced inhibition of GJIC. Inhibition of protein kinase A also prevented inhibition of GJIC by 1-methylanthracene. Direct measurement of phosphatidylcholine-specific phospholipase C and sphingomyelinase indicated that only phosphatidylcholine-specific phospholipase C was activated in response to 1-methylanthracene, while 2-methylanthracene had no effect. 1-methylanthracene also activated p38-mitogen activated protein kinase; however, like extracellular kinase, its activation was not involved in 1-methylanthracene-induced regulation of GJIC, and this activation was independent of phosphatidylcholine-specific phospholipase C. Although mitogen activated protein kinases were activated, Western blot analyzes indicated no change in connexin43 phosphorylation status. Our results indicate that phosphatidylcholine-specific phospholipase C is an important enzyme in the induction of a tumorigenic phenotype, namely the inhibition of GJIC; whereas mitogen activated protein kinases triggered in response to 1-methylanthracene, were not involved in the deregulation of GJIC.", journal = "Cancer Science", title = "Tumor promoting properties of a cigarette smoke prevalent polycyclic aromatic hydrocarbon as indicated by the inhibition of gap junctional intercellular communication via phosphatidylcholine-specific phospholipase C", volume = "99", number = "4", pages = "696-705", doi = "10.1111/j.1349-7006.2008.00752.x" }
Upham, B. L., Blaha, L., Babica, P., Park, J., Sovadinova, I., Pudrith, C., Rummel, A. M., Weis, L. M., Sai, K., Tithof, P. K., Gužvić, M., Vondracek, J., Machala, M.,& Trosko, J. E.. (2008). Tumor promoting properties of a cigarette smoke prevalent polycyclic aromatic hydrocarbon as indicated by the inhibition of gap junctional intercellular communication via phosphatidylcholine-specific phospholipase C. in Cancer Science, 99(4), 696-705. https://doi.org/10.1111/j.1349-7006.2008.00752.x
Upham BL, Blaha L, Babica P, Park J, Sovadinova I, Pudrith C, Rummel AM, Weis LM, Sai K, Tithof PK, Gužvić M, Vondracek J, Machala M, Trosko JE. Tumor promoting properties of a cigarette smoke prevalent polycyclic aromatic hydrocarbon as indicated by the inhibition of gap junctional intercellular communication via phosphatidylcholine-specific phospholipase C. in Cancer Science. 2008;99(4):696-705. doi:10.1111/j.1349-7006.2008.00752.x .
Upham, Brad L., Blaha, Ludek, Babica, Pavel, Park, Joon-Suk, Sovadinova, Iva, Pudrith, Charles, Rummel, Alisa M., Weis, Liliane M., Sai, Kimie, Tithof, Patti K., Gužvić, Miodrag, Vondracek, Jan, Machala, Miroslav, Trosko, James E., "Tumor promoting properties of a cigarette smoke prevalent polycyclic aromatic hydrocarbon as indicated by the inhibition of gap junctional intercellular communication via phosphatidylcholine-specific phospholipase C" in Cancer Science, 99, no. 4 (2008):696-705, https://doi.org/10.1111/j.1349-7006.2008.00752.x . .