Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint

Ugur Aytac, Kazuya Sato, Fernando Cabanillas, Nam H. Dang, Linus Ho, Francois Xavier Claret, Gordon Mills, Nam H. Dang, Kei Ohnuma, Chikao Morimoto

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

CD26, a Mr 110,000 surface-bound ectopeptidase with dipeptidyl peptidase IV (DPPIV) activity, has an array of diverse functional properties, with a role in T-cell physiology and the development of certain human cancers. In this study, we report that surface expression of CD26, through its associated DPPIV enzyme activity, enhanced sensitivity of Jurkat T-cell transfectants to G2-M arrest induced by the chemotherapeutic drug, doxorubicin. This was associated with disruption of cell cycle-related events, including hyperphosphorylation and inhibition of p34cdc2 kinase activity, phosphorylation of cdc25C, and alteration in cyclin B1 expression. In addition, we demonstrate that the addition of exogenous soluble DPPIV enhanced sensitivity of lymphoid tumor cell lines to doxorubicin, suggesting a potentially useful clinical role for CD26/DPPIV in the treatment of selected human hematological malignancies.

Original languageEnglish (US)
Pages (from-to)7204-7210
Number of pages7
JournalCancer Research
Volume61
Issue number19
StatePublished - Oct 1 2001
Externally publishedYes

Fingerprint

G2 Phase Cell Cycle Checkpoints
Dipeptidyl Peptidase 4
Doxorubicin
Enzymes
Cyclin B1
T-Lymphocytes
Cell Physiological Phenomena
Jurkat Cells
Human Development
Hematologic Neoplasms
Tumor Cell Line
Cell Cycle
Phosphotransferases
Phosphorylation
Lymphocytes
Pharmaceutical Preparations
Neoplasms

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

Aytac, U., Sato, K., Cabanillas, F., Dang, N. H., Ho, L., Claret, F. X., ... Morimoto, C. (2001). Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint. Cancer Research, 61(19), 7204-7210.

Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint. / Aytac, Ugur; Sato, Kazuya; Cabanillas, Fernando; Dang, Nam H.; Ho, Linus; Claret, Francois Xavier; Mills, Gordon; Dang, Nam H.; Ohnuma, Kei; Morimoto, Chikao.

In: Cancer Research, Vol. 61, No. 19, 01.10.2001, p. 7204-7210.

Research output: Contribution to journalArticle

Aytac, U, Sato, K, Cabanillas, F, Dang, NH, Ho, L, Claret, FX, Mills, G, Dang, NH, Ohnuma, K & Morimoto, C 2001, 'Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint', Cancer Research, vol. 61, no. 19, pp. 7204-7210.
Aytac, Ugur ; Sato, Kazuya ; Cabanillas, Fernando ; Dang, Nam H. ; Ho, Linus ; Claret, Francois Xavier ; Mills, Gordon ; Dang, Nam H. ; Ohnuma, Kei ; Morimoto, Chikao. / Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint. In: Cancer Research. 2001 ; Vol. 61, No. 19. pp. 7204-7210.
@article{675ed0ec6ac449bcb2a3efa5f5544677,
title = "Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint",
abstract = "CD26, a Mr 110,000 surface-bound ectopeptidase with dipeptidyl peptidase IV (DPPIV) activity, has an array of diverse functional properties, with a role in T-cell physiology and the development of certain human cancers. In this study, we report that surface expression of CD26, through its associated DPPIV enzyme activity, enhanced sensitivity of Jurkat T-cell transfectants to G2-M arrest induced by the chemotherapeutic drug, doxorubicin. This was associated with disruption of cell cycle-related events, including hyperphosphorylation and inhibition of p34cdc2 kinase activity, phosphorylation of cdc25C, and alteration in cyclin B1 expression. In addition, we demonstrate that the addition of exogenous soluble DPPIV enhanced sensitivity of lymphoid tumor cell lines to doxorubicin, suggesting a potentially useful clinical role for CD26/DPPIV in the treatment of selected human hematological malignancies.",
author = "Ugur Aytac and Kazuya Sato and Fernando Cabanillas and Dang, {Nam H.} and Linus Ho and Claret, {Francois Xavier} and Gordon Mills and Dang, {Nam H.} and Kei Ohnuma and Chikao Morimoto",
year = "2001",
month = "10",
day = "1",
language = "English (US)",
volume = "61",
pages = "7204--7210",
journal = "Journal of Cancer Research",
issn = "0099-7013",
publisher = "American Association for Cancer Research Inc.",
number = "19",

}

TY - JOUR

T1 - Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G2/M checkpoint

AU - Aytac, Ugur

AU - Sato, Kazuya

AU - Cabanillas, Fernando

AU - Dang, Nam H.

AU - Ho, Linus

AU - Claret, Francois Xavier

AU - Mills, Gordon

AU - Dang, Nam H.

AU - Ohnuma, Kei

AU - Morimoto, Chikao

PY - 2001/10/1

Y1 - 2001/10/1

N2 - CD26, a Mr 110,000 surface-bound ectopeptidase with dipeptidyl peptidase IV (DPPIV) activity, has an array of diverse functional properties, with a role in T-cell physiology and the development of certain human cancers. In this study, we report that surface expression of CD26, through its associated DPPIV enzyme activity, enhanced sensitivity of Jurkat T-cell transfectants to G2-M arrest induced by the chemotherapeutic drug, doxorubicin. This was associated with disruption of cell cycle-related events, including hyperphosphorylation and inhibition of p34cdc2 kinase activity, phosphorylation of cdc25C, and alteration in cyclin B1 expression. In addition, we demonstrate that the addition of exogenous soluble DPPIV enhanced sensitivity of lymphoid tumor cell lines to doxorubicin, suggesting a potentially useful clinical role for CD26/DPPIV in the treatment of selected human hematological malignancies.

AB - CD26, a Mr 110,000 surface-bound ectopeptidase with dipeptidyl peptidase IV (DPPIV) activity, has an array of diverse functional properties, with a role in T-cell physiology and the development of certain human cancers. In this study, we report that surface expression of CD26, through its associated DPPIV enzyme activity, enhanced sensitivity of Jurkat T-cell transfectants to G2-M arrest induced by the chemotherapeutic drug, doxorubicin. This was associated with disruption of cell cycle-related events, including hyperphosphorylation and inhibition of p34cdc2 kinase activity, phosphorylation of cdc25C, and alteration in cyclin B1 expression. In addition, we demonstrate that the addition of exogenous soluble DPPIV enhanced sensitivity of lymphoid tumor cell lines to doxorubicin, suggesting a potentially useful clinical role for CD26/DPPIV in the treatment of selected human hematological malignancies.

UR - http://www.scopus.com/inward/record.url?scp=0035477462&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035477462&partnerID=8YFLogxK

M3 - Article

C2 - 11585756

AN - SCOPUS:0035477462

VL - 61

SP - 7204

EP - 7210

JO - Journal of Cancer Research

JF - Journal of Cancer Research

SN - 0099-7013

IS - 19

ER -