2006Cancer ResearchRequires access

SNS-032 is a potent and selective inhibitor of CDK2, 7 and 9 and induces cell death by inhibiting cell cycle progression and the expression of antiapoptotic proteins

Samer J. Nuwayhid, Jennifer Hyde, Alexey Aleshin, Duncan Walker, Michelle R. Arkin

Open publisher page 10 citations

Abstract

2079 The cell cycle-regulated CDKs, CDK1, 2, and 4 have been extensively studied as potential therapeutic targets in cancer. Recent research has additionally underscored the potential role of several constitutively active CDKs including CDK7 and 9 as cancer targets. Phosphorylation of the c-terminal domain (CTD) of RNA Polymerase II by CDK7 and 9 are critical steps in transcriptional regulation. Inhibition of these kinases is predicted to have the greatest effect on the expression of proteins with short T \(\frac{1}{2}\) and short-lived mRNA, including proteins involved in apoptotic regulation. CDK7 also activates cell-cycle CDKs 1, 2, 4 and 6. SNS-032 (formerly BMS-387032) has previously been described as a selective inhibitor of CDK2 with potent antitumor activity in animal models. Here we show that in addition to inhibition of CDK2, SNS-032 also inhibits CDK7/cyclinH and CDK9/cyclinT at low nanomolar concentrations in biochemical assays. The compound is highly selective for CDK inhibition; in a panel of 208 kinases, only four non-CDK proteins were inhibited by >50% at 1 μM SNS-032. The cellular pharmacology of SNS-032 mirrors the biochemical data. Cells treated with SNS-032 show a rapid cell cycle arrest and onset of cell death that corresponds with inhibition of multiple substrates of CDK2, 7, and 9. For instance, inhibition of pRb phosphorylation, accumulation of cyclin E protein, and cell-cycle arrest at G1 and G2 are observed in multiple cell lines in a time- and dose-dependent manner, consistent with inhibition of CDK2 and CAK. Furthermore, SNS-032 inhibits CDK9-mediated phosphorylation of Ser2 in the CTD with an IC50= 20 nM. Corresponding with inhibition of RNA polymerase II, the short half-life, anti-apoptotic protein Mcl-1 is rapidly depleted from cells, coincident with the phosphorylation of p53. Expression of Mcl-1 is a candidate predictor of aggressive disease and resistance to chemotherapy in CLL and is essential for survival of B-cell lymphoma and multiple myelomas, supporting the use of SNS-032 as a treatment for these diseases. SNS-032, a selective inhibitor of multiple CDKs involved in apoptosis and cell cycle regulation, has potential for antitumor activity in both solid and hematological cancers. SNS-032 is currently in phase 1 clinical studies.

About this research paper

What this paper is about

2079 The cell cycle-regulated CDKs, CDK1, 2, and 4 have been extensively studied as potential therapeutic targets in cancer. Recent research has additionally underscored the potential role of several constitutively active CDKs including CDK7 and 9 as cancer targets. Phosphorylation of the c-terminal domain (CTD) of RNA Polymerase II by CDK7 and 9 are critical steps in transcriptional regulation. Inhibition of these kinases is predicted to have the greatest effect on the expression of proteins with short T \(\frac{1}{2}\) and short-lived mRNA, including proteins involved in apoptotic regulation. CDK7 also activates cell-cycle CDKs 1, 2, 4 and 6. SNS-032 (formerly BMS-387032) has previously been described as a selective inhibitor of CDK2 with potent antitumor activity in animal models. Here we show that in addition to inhibition of CDK2, SNS-032 also inhibits CDK7/cyclinH and CDK9/cyclinT at low nanomolar concentrations in biochemical assays. The compound is highly selective for CDK inhibition; in a panel of 208 kinases, only four non-CDK proteins were inhibited by >50% at 1 μM SNS-032. The cellular pharmacology of SNS-032 mirrors the biochemical data. Cells treated with SNS-032 show a rapid cell cycle arrest and onset of cell death that corresponds with inhibition of multiple substrates of CDK2, 7, and 9. For instance, inhibition of pRb phosphorylation, accumulation of cyclin E protein, and cell-cycle arrest at G1 and G2 are observed in multiple cell lines in a time- and dose-dependent manner, consistent with inhibition of CDK2 and CAK. Furthermore, SNS-032 inhibits CDK9-mediated phosphorylation of Ser2 in the CTD with an IC50= 20 nM. Corresponding with inhibition of RNA polymerase II, the short half-life, anti-apoptotic protein Mcl-1 is rapidly depleted from cells, coincident with the phosphorylation of p53. Expression of Mcl-1 is a candidate predictor of aggressive disease and resistance to chemotherapy in CLL and is essential for survival of B-cell lymphoma and multiple myelomas, supporting the use of SNS-032 as a treatment for these diseases. SNS-032, a selective inhibitor of multiple CDKs involved in apoptosis and cell cycle regulation, has potential for antitumor activity in both solid and hematological cancers. SNS-032 is currently in phase 1 clinical studies.

Why it matters

OpenAlex reports 10 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

2079 The cell cycle-regulated CDKs, CDK1, 2, and 4 have been extensively studied as potential therapeutic targets in cancer. Recent research has additionally underscored the potential role of several constitutively active CDKs including CDK7 and 9 as cancer targets. Phosphorylation of the c-terminal domain (CTD) of RNA Polymerase II by CDK7 and 9 are critical steps in transcriptional regulation. Inhibition of these kinases is predicted to have the greatest effect on the expression of proteins with short T \(\frac{1}{2}\) and short-lived mRNA, including proteins involved in apoptotic regulation. CDK7 also activates cell-cycle CDKs 1, 2, 4 and 6. SNS-032 (formerly BMS-387032) has previously been described as a selective inhibitor of CDK2 with potent antitumor activity in animal models. Here we show that in addition to inhibition of CDK2, SNS-032 also inhibits CDK7/cyclinH and CDK9/cyclinT at low nanomolar concentrations in biochemical assays. The compound is highly selective for CDK inhibition; in a panel of 208 kinases, only four non-CDK proteins were inhibited by >50% at 1 μM SNS-032. The cellular pharmacology of SNS-032 mirrors the biochemical data. Cells treated with SNS-032 show a rapid cell cycle arrest and onset of cell death that corresponds with inhibition of multiple substrates of CDK2, 7, and 9. For instance, inhibition of pRb phosphorylation, accumulation of cyclin E protein, and cell-cycle arrest at G1 and G2 are observed in multiple cell lines in a time- and dose-dependent manner, consistent with inhibition of CDK2 and CAK. Furthermore, SNS-032 inhibits CDK9-mediated phosphorylation of Ser2 in the CTD with an IC50= 20 nM. Corresponding with inhibition of RNA polymerase II, the short half-life, anti-apoptotic protein Mcl-1 is rapidly depleted from cells, coincident with the phosphorylation of p53. Expression of Mcl-1 is a candidate predictor of aggressive disease and resistance to chemotherapy in CLL and is essential for survival of B-cell lymphoma and multiple myelomas, supporting the use of SNS-032 as a treatment for these diseases. SNS-032, a selective inhibitor of multiple CDKs involved in apoptosis and cell cycle regulation, has potential for antitumor activity in both solid and hematological cancers. SNS-032 is currently in phase 1 clinical studies.

Key concepts: Cyclin-dependent kinase, Cyclin-dependent kinase 2, Cyclin-dependent kinase 1, CDK inhibitor, G1 phase, Cell cycle, Kinase, Cell biology

Related papers

Back to paper searchBrowse research topicsOriginal source
SNS-032 is a potent and selective inhibitor of CDK2, 7 and 9 and induces cell death by inhibiting cell cycle progression and the expression of antiapoptotic proteins — Research Paper | ScholarLens