Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells.
Dipeptidyl peptidase IV (DPPIV/CD26) is a transmembrane glycoprotein that inactivates or degrades some bioactive peptides and chemokines. For this reason, it regulates cell proliferation, migration and adhesion, showing its role in cancer processes. This enzyme is found mainly anchored onto the cell...
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Public Library of Science (PLoS)
2015-01-01
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Online Access: | http://europepmc.org/articles/PMC4519168?pdf=render |
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author | Aline Beckenkamp Júlia Biz Willig Danielle Bertodo Santana Jéssica Nascimento Juliano Domiraci Paccez Luiz Fernando Zerbini Alessandra Nejar Bruno Diogo André Pilger Márcia Rosângela Wink Andréia Buffon |
author_facet | Aline Beckenkamp Júlia Biz Willig Danielle Bertodo Santana Jéssica Nascimento Juliano Domiraci Paccez Luiz Fernando Zerbini Alessandra Nejar Bruno Diogo André Pilger Márcia Rosângela Wink Andréia Buffon |
author_sort | Aline Beckenkamp |
collection | DOAJ |
description | Dipeptidyl peptidase IV (DPPIV/CD26) is a transmembrane glycoprotein that inactivates or degrades some bioactive peptides and chemokines. For this reason, it regulates cell proliferation, migration and adhesion, showing its role in cancer processes. This enzyme is found mainly anchored onto the cell membrane, although it also has a soluble form, an enzymatically active isoform. In the present study, we investigated DPPIV/CD26 activity and expression in cervical cancer cell lines (SiHa, HeLa and C33A) and non-tumorigenic HaCaT cells. The effect of the DPPIV/CD26 inhibitor (sitagliptin phosphate) on cell migration and adhesion was also evaluated. Cervical cancer cells and keratinocytes exhibited DPPIV/CD26 enzymatic activity both membrane-bound and in soluble form. DPPIV/CD26 expression was observed in HaCaT, SiHa and C33A, while in HeLa cells it was almost undetectable. We observed higher migratory capacity of HeLa, when compared to SiHa. But in the presence of sitagliptin SiHa showed an increase in migration, indicating that, at least in part, cell migration is regulated by DPPIV/CD26 activity. Furthermore, in the presence of sitagliptin phosphate, SiHa and HeLa cells exhibited a significant reduction in adhesion. However this mechanism seems to be mediated independent of DPPIV/CD26. This study demonstrates, for the first time, the activity and expression of DPPIV/CD26 in cervical cancer cells and the effect of sitagliptin phosphate on cell migration and adhesion. |
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issn | 1932-6203 |
language | English |
last_indexed | 2024-12-14T16:16:08Z |
publishDate | 2015-01-01 |
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spelling | doaj.art-8d9a596b454449338f7f46ca44becd3c2022-12-21T22:54:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01107e013430510.1371/journal.pone.0134305Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells.Aline BeckenkampJúlia Biz WilligDanielle Bertodo SantanaJéssica NascimentoJuliano Domiraci PaccezLuiz Fernando ZerbiniAlessandra Nejar BrunoDiogo André PilgerMárcia Rosângela WinkAndréia BuffonDipeptidyl peptidase IV (DPPIV/CD26) is a transmembrane glycoprotein that inactivates or degrades some bioactive peptides and chemokines. For this reason, it regulates cell proliferation, migration and adhesion, showing its role in cancer processes. This enzyme is found mainly anchored onto the cell membrane, although it also has a soluble form, an enzymatically active isoform. In the present study, we investigated DPPIV/CD26 activity and expression in cervical cancer cell lines (SiHa, HeLa and C33A) and non-tumorigenic HaCaT cells. The effect of the DPPIV/CD26 inhibitor (sitagliptin phosphate) on cell migration and adhesion was also evaluated. Cervical cancer cells and keratinocytes exhibited DPPIV/CD26 enzymatic activity both membrane-bound and in soluble form. DPPIV/CD26 expression was observed in HaCaT, SiHa and C33A, while in HeLa cells it was almost undetectable. We observed higher migratory capacity of HeLa, when compared to SiHa. But in the presence of sitagliptin SiHa showed an increase in migration, indicating that, at least in part, cell migration is regulated by DPPIV/CD26 activity. Furthermore, in the presence of sitagliptin phosphate, SiHa and HeLa cells exhibited a significant reduction in adhesion. However this mechanism seems to be mediated independent of DPPIV/CD26. This study demonstrates, for the first time, the activity and expression of DPPIV/CD26 in cervical cancer cells and the effect of sitagliptin phosphate on cell migration and adhesion.http://europepmc.org/articles/PMC4519168?pdf=render |
spellingShingle | Aline Beckenkamp Júlia Biz Willig Danielle Bertodo Santana Jéssica Nascimento Juliano Domiraci Paccez Luiz Fernando Zerbini Alessandra Nejar Bruno Diogo André Pilger Márcia Rosângela Wink Andréia Buffon Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells. PLoS ONE |
title | Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells. |
title_full | Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells. |
title_fullStr | Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells. |
title_full_unstemmed | Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells. |
title_short | Differential Expression and Enzymatic Activity of DPPIV/CD26 Affects Migration Ability of Cervical Carcinoma Cells. |
title_sort | differential expression and enzymatic activity of dppiv cd26 affects migration ability of cervical carcinoma cells |
url | http://europepmc.org/articles/PMC4519168?pdf=render |
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