Abstract
Bcr-Abl, a constitutively active tyrosine kinase, is the cause of chronic myeloid leukemia (CML) and a subset of acute lymphoblastic leukemias (ALL). Bruton's tyrosine kinase (BTK), a member of the Tec family of tyrosine kinases with a crucial role in B-cell development, is consistently tyrosine phosphorylated in Bcr-Abl expressing murine pre B cells. BTK has been implicated in Bcr-Abl-mediated B-cell transformation and resistance to imatinib, implying that inhibiting BTK may be therapeutically beneficial. We decided to test whether BTK is a critical node in Bcr-Abl transformation and potential drug target in imatinib-resistant Bcr-Abl-positive cells. We depleted BTK in Ba/F3 and 32D cells expressing native and kinase domain (KD) mutant (E255K and T315I) Bcr-Abl, using shRNA. BTK levels were reduced to
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1354-1360 |
| Number of pages | 7 |
| Journal | Leukemia |
| Volume | 22 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jul 2008 |
Fingerprint
ASJC Scopus subject areas
- Hematology
- Cancer Research
Cite this
Bruton's tyrosine kinase is not essential for Bcr-Abl-mediated transformation of lymphoid or myeloid cells. / MacPartlin, M.; Smith, A. M.; Druker, Brian; Honigberg, L. A.; Deininger, M. W.
In: Leukemia, Vol. 22, No. 7, 07.2008, p. 1354-1360.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Bruton's tyrosine kinase is not essential for Bcr-Abl-mediated transformation of lymphoid or myeloid cells
AU - MacPartlin, M.
AU - Smith, A. M.
AU - Druker, Brian
AU - Honigberg, L. A.
AU - Deininger, M. W.
PY - 2008/7
Y1 - 2008/7
N2 - Bcr-Abl, a constitutively active tyrosine kinase, is the cause of chronic myeloid leukemia (CML) and a subset of acute lymphoblastic leukemias (ALL). Bruton's tyrosine kinase (BTK), a member of the Tec family of tyrosine kinases with a crucial role in B-cell development, is consistently tyrosine phosphorylated in Bcr-Abl expressing murine pre B cells. BTK has been implicated in Bcr-Abl-mediated B-cell transformation and resistance to imatinib, implying that inhibiting BTK may be therapeutically beneficial. We decided to test whether BTK is a critical node in Bcr-Abl transformation and potential drug target in imatinib-resistant Bcr-Abl-positive cells. We depleted BTK in Ba/F3 and 32D cells expressing native and kinase domain (KD) mutant (E255K and T315I) Bcr-Abl, using shRNA. BTK levels were reduced to
AB - Bcr-Abl, a constitutively active tyrosine kinase, is the cause of chronic myeloid leukemia (CML) and a subset of acute lymphoblastic leukemias (ALL). Bruton's tyrosine kinase (BTK), a member of the Tec family of tyrosine kinases with a crucial role in B-cell development, is consistently tyrosine phosphorylated in Bcr-Abl expressing murine pre B cells. BTK has been implicated in Bcr-Abl-mediated B-cell transformation and resistance to imatinib, implying that inhibiting BTK may be therapeutically beneficial. We decided to test whether BTK is a critical node in Bcr-Abl transformation and potential drug target in imatinib-resistant Bcr-Abl-positive cells. We depleted BTK in Ba/F3 and 32D cells expressing native and kinase domain (KD) mutant (E255K and T315I) Bcr-Abl, using shRNA. BTK levels were reduced to
UR - http://www.scopus.com/inward/record.url?scp=47549101393&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=47549101393&partnerID=8YFLogxK
U2 - 10.1038/leu.2008.126
DO - 10.1038/leu.2008.126
M3 - Article
VL - 22
SP - 1354
EP - 1360
JO - Leukemia
JF - Leukemia
SN - 0887-6924
IS - 7
ER -