The University of Southampton
University of Southampton Institutional Repository

Tyrosine kinases as therapeutic targets in BCR-ABL negative chronic myeloproliferative disorders

Reiter, Andreas, Walz, Christoph and Cross, Nicholas C.P. (2007) Tyrosine kinases as therapeutic targets in BCR-ABL negative chronic myeloproliferative disorders Current Drug Targets, 8, (2), pp. 205-216.

Record type: Article


Acquired constitutive activation of protein tyrosine kinases is a central feature in the pathogenesis of chronic myeloproliferative disorders (CMPDs). The most commonly involved genes are the receptor tyrosine kinases PDGFRA, PDGFRB, FGFR1 or c-KIT and the non-receptor tyrosine kinases JAK2 and ABL. Activation occurs as a consequence of specific point mutations or fusion genes generated by chromosomal translocations, insertions or deletions. Mutant kinases are constitutively active in the absence of the natural ligands resulting in deregulation of haemopoiesis in a manner analogous to BCR-ABL in chronic myeloid leukaemia. With the advent of targeted signal transduction therapy with tyrosine kinase inhibitors, an accurate diagnosis of CMPDs by morphology, karyotyping and molecular genetics has become increasingly important. Imatinib induces high response rates in patients associated with constitutive activation of ABL, PDGFRalpha, PDGFRbeta and some KIT mutants. Other inhibitors under development are promising candidates for effective treatment of patients with constitutive activation of JAK2, FGFR1 and imatinib-resistant KIT mutants.

Full text not available from this repository.

More information

Published date: 2007
Keywords: enzyme activation, mutation, review, genes, humans, treatment, patients, protein-tyrosine kinase, tyrosine, genetics, protein-tyrosine kinases, karyotyping, protein kinase inhibitors, diagnosis


Local EPrints ID: 60157
ISSN: 1389-4501
PURE UUID: cd7ab906-bb35-44c9-a335-bbf9b18f5b5b
ORCID for Nicholas C.P. Cross: ORCID iD

Catalogue record

Date deposited: 05 Sep 2008
Last modified: 17 Jul 2017 14:23

Export record

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton:

ePrints Soton supports OAI 2.0 with a base URL of

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.