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Year 2018, Volume: 46 Issue: 3, 329 - 336, 01.09.2018

Abstract

References

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  • J. Adams, The proteasome: structure, function and role in the cell, Cancer Treat. Rev., 1 (2003) 3-9.
  • J.D. Etlinger, A.L. Goldberg, A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes, PNAS, 74 (1977) 54–58.
  • N. Benaroudj, P. Zwickl, E. Seemuller, W. Baumeister, A.L. Goldberg, ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation, Molecul. Cell, 11 (2003) 69–78.
  • J.E. Nelson, A. Loukissa, C. Altschuller-Felberg, J.J. Monaco, J.T. Fallon, C. Cardozo, Up-regulation of the proteasome subunit LMP7 in tissues of endotoxemic rats. J. Laborat. Clin. Med., 135 (2000) 324–331.
  • S. Türkoğlu, F. Köçkar, SP1 and USF differentially regulate ADAMTS1 gene expression under normoxic and hypoxic conditions in hepatoma cells, Gene, 575 1 (2016) 48-57.
  • M. Alper and F. Köçkar, Induction of Human ADAMTS-2 Gene Expression by IL-1α is Mediated by a Multiple Crosstalk of MEK/JNK and PI3K Pathways in Osteoblast like Cells, Gene, 573 (2015) 321-327.
  • E.Tokay and F. Köçkar, ‘In Silico and Expression analysis of URG-4/URGCP Gene in Different Cancer Cells, J.Appl. Biol. Sci., 2 (2015) 13-18.
  • J. Wang, M.A. Maldonado, The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases, Cell. Mol. Immunol., 34 (2006) 255–261.
  • Y. Uyanıkgil, C. Sümer Turanlıgil, Ubikitin-proteozom yolağının karsinojenezdeki rolü. ARŞİV, 19 (2010) 36.
  • G.P. Tuszynski, V.L. Rothman, M. Papale, B.K. Hamilton, J. Eyal, Identification and characterization of a tumor cell receptor for CSVTCG. a thrombospondin adhesive domain, J. Cell. Biol., 120 (1993) 513–521.
  • C. Wang, H. Fan, J. Zhou, M. Lu, J. Sun, Y. Song, H. Le, L. Jiang, B. Wang, Jiao, S5a binds to death receptor-6 to induce THP-1 monocytes to differentiate through the activation of the NF-kB pathway, J. Cell Sci., 127 (2014) 3257–3268.
  • A. Sparks, S. Dayal, J. Das, P. Robertson, S. Menendez, MK. Saville, The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a. Oncogene, (2013) 1–12.
  • R.K. Singh, S. Zerath, O. Kleifeld, M. Scheffner, M.H. Glickman, D. Fushman, Recognition and Cleavage of Related to Ubiquitin 1 (Rub1) and Rub1-Ubiquitin Chains by Components of the Ubiquitin-Proteasome System, Mol. Cell. Proteomics, 11 (2012) 1595–1611.
  • M. Elangovan, C. Oh, L. Sukumaran, C. Wójcik, Y.J. Yoo, Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13, Biochem. Biophy. Res. Comm., 396 (2010) 425–428.
  • A. Arlt, I. Bauer, C. Schafmayer, J. Tepel, S.S. Müerköster, M. Brosch, C. Röder, H. Kalthoff, J. Hampe, M.P. Moyer, U.R. Fölsch, H. Schafer, Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2), Oncogene, 28 (2009) 3983–3996.
  • S.M. Pulukuri, C.S. Gondi, S.S. Lakka, A. Jutla, N. Estes, M. Gujrati, J.S. Rao, RNA interference -directed knockdown of urokinase plasminogen activator and urokinase plasminogen activator receptor inhibits prostate cancer cell invasion, survival, and tumorigenicity in vivo, J. Biol. Chem., 280 (2005) 36529-36540.

The Bioinformatic and Expression Analysis of PSMD4 Gene

Year 2018, Volume: 46 Issue: 3, 329 - 336, 01.09.2018

Abstract

26S proteasome non-ATPase subunit 4 (PSMD4) that has a molecular weight of 41 kDa is included on
chromosome 1 (1q21.3). PSMD4 protein is a subunit of the 19S regulatory region in the 26S proteasome.
The proteasome breaks down proteins that are not needed or non-functional in the cell. We have limited data
about the regulation of this gene in the literature. In our research, changes in the mRNA and protein levels
of the PSMD4 gene were investigated in different cancer cell lines (prostate, breast, colon, cervix, hepatoma,
osteosarcoma and pancreas) and a normal cell (human vein endothelial cell). The highest expression of PSMD4
gene was seen in HUVEC and PC-3 cells. Bioinformatic analysis was also performed on PSMD4 protein for
different species namely human, mouse and rat. Our Bioinformatic analyses showed that first 250 nucleotides
are much conserved in all three species.

References

  • H. Lodish, A. Berk, P. Matsudaira, C.A. Kaiser, M. Krieger, M.P. Scott, S.L. Zipursky, J. Darnell, Molecular cell biology, (2004) 66–72.
  • J. Adams, The proteasome: structure, function and role in the cell, Cancer Treat. Rev., 1 (2003) 3-9.
  • J.D. Etlinger, A.L. Goldberg, A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes, PNAS, 74 (1977) 54–58.
  • N. Benaroudj, P. Zwickl, E. Seemuller, W. Baumeister, A.L. Goldberg, ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation, Molecul. Cell, 11 (2003) 69–78.
  • J.E. Nelson, A. Loukissa, C. Altschuller-Felberg, J.J. Monaco, J.T. Fallon, C. Cardozo, Up-regulation of the proteasome subunit LMP7 in tissues of endotoxemic rats. J. Laborat. Clin. Med., 135 (2000) 324–331.
  • S. Türkoğlu, F. Köçkar, SP1 and USF differentially regulate ADAMTS1 gene expression under normoxic and hypoxic conditions in hepatoma cells, Gene, 575 1 (2016) 48-57.
  • M. Alper and F. Köçkar, Induction of Human ADAMTS-2 Gene Expression by IL-1α is Mediated by a Multiple Crosstalk of MEK/JNK and PI3K Pathways in Osteoblast like Cells, Gene, 573 (2015) 321-327.
  • E.Tokay and F. Köçkar, ‘In Silico and Expression analysis of URG-4/URGCP Gene in Different Cancer Cells, J.Appl. Biol. Sci., 2 (2015) 13-18.
  • J. Wang, M.A. Maldonado, The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases, Cell. Mol. Immunol., 34 (2006) 255–261.
  • Y. Uyanıkgil, C. Sümer Turanlıgil, Ubikitin-proteozom yolağının karsinojenezdeki rolü. ARŞİV, 19 (2010) 36.
  • G.P. Tuszynski, V.L. Rothman, M. Papale, B.K. Hamilton, J. Eyal, Identification and characterization of a tumor cell receptor for CSVTCG. a thrombospondin adhesive domain, J. Cell. Biol., 120 (1993) 513–521.
  • C. Wang, H. Fan, J. Zhou, M. Lu, J. Sun, Y. Song, H. Le, L. Jiang, B. Wang, Jiao, S5a binds to death receptor-6 to induce THP-1 monocytes to differentiate through the activation of the NF-kB pathway, J. Cell Sci., 127 (2014) 3257–3268.
  • A. Sparks, S. Dayal, J. Das, P. Robertson, S. Menendez, MK. Saville, The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a. Oncogene, (2013) 1–12.
  • R.K. Singh, S. Zerath, O. Kleifeld, M. Scheffner, M.H. Glickman, D. Fushman, Recognition and Cleavage of Related to Ubiquitin 1 (Rub1) and Rub1-Ubiquitin Chains by Components of the Ubiquitin-Proteasome System, Mol. Cell. Proteomics, 11 (2012) 1595–1611.
  • M. Elangovan, C. Oh, L. Sukumaran, C. Wójcik, Y.J. Yoo, Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13, Biochem. Biophy. Res. Comm., 396 (2010) 425–428.
  • A. Arlt, I. Bauer, C. Schafmayer, J. Tepel, S.S. Müerköster, M. Brosch, C. Röder, H. Kalthoff, J. Hampe, M.P. Moyer, U.R. Fölsch, H. Schafer, Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2), Oncogene, 28 (2009) 3983–3996.
  • S.M. Pulukuri, C.S. Gondi, S.S. Lakka, A. Jutla, N. Estes, M. Gujrati, J.S. Rao, RNA interference -directed knockdown of urokinase plasminogen activator and urokinase plasminogen activator receptor inhibits prostate cancer cell invasion, survival, and tumorigenicity in vivo, J. Biol. Chem., 280 (2005) 36529-36540.
There are 17 citations in total.

Details

Primary Language English
Journal Section Articles
Authors

Sümeyye Aydoğan Türkoğlu This is me

Gizem Güler This is me

Feray Köçkar This is me

Publication Date September 1, 2018
Acceptance Date July 31, 2018
Published in Issue Year 2018 Volume: 46 Issue: 3

Cite

APA Aydoğan Türkoğlu, S., Güler, G., & Köçkar, F. (2018). The Bioinformatic and Expression Analysis of PSMD4 Gene. Hacettepe Journal of Biology and Chemistry, 46(3), 329-336.
AMA Aydoğan Türkoğlu S, Güler G, Köçkar F. The Bioinformatic and Expression Analysis of PSMD4 Gene. HJBC. September 2018;46(3):329-336.
Chicago Aydoğan Türkoğlu, Sümeyye, Gizem Güler, and Feray Köçkar. “The Bioinformatic and Expression Analysis of PSMD4 Gene”. Hacettepe Journal of Biology and Chemistry 46, no. 3 (September 2018): 329-36.
EndNote Aydoğan Türkoğlu S, Güler G, Köçkar F (September 1, 2018) The Bioinformatic and Expression Analysis of PSMD4 Gene. Hacettepe Journal of Biology and Chemistry 46 3 329–336.
IEEE S. Aydoğan Türkoğlu, G. Güler, and F. Köçkar, “The Bioinformatic and Expression Analysis of PSMD4 Gene”, HJBC, vol. 46, no. 3, pp. 329–336, 2018.
ISNAD Aydoğan Türkoğlu, Sümeyye et al. “The Bioinformatic and Expression Analysis of PSMD4 Gene”. Hacettepe Journal of Biology and Chemistry 46/3 (September 2018), 329-336.
JAMA Aydoğan Türkoğlu S, Güler G, Köçkar F. The Bioinformatic and Expression Analysis of PSMD4 Gene. HJBC. 2018;46:329–336.
MLA Aydoğan Türkoğlu, Sümeyye et al. “The Bioinformatic and Expression Analysis of PSMD4 Gene”. Hacettepe Journal of Biology and Chemistry, vol. 46, no. 3, 2018, pp. 329-36.
Vancouver Aydoğan Türkoğlu S, Güler G, Köçkar F. The Bioinformatic and Expression Analysis of PSMD4 Gene. HJBC. 2018;46(3):329-36.

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