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DNA double-strand break repair: a theoretical framework and its application.

Murray PJ, Cornelissen B, Vallis KA, Chapman SJ - J R Soc Interface (2016)

Bottom Line: It has previously been shown that anti-γH2AX antibodies, modified by the addition of the cell-penetrating peptide TAT and a fluorescent or radionuclide label, can be used to visualize and quantify DSBs in vivo.Equations that describe stochastic mean behaviours at individual DSB sites are derived and parametrized using population-scale, time-series measurements from two different cancer cell lines.This work supports the conclusion that DSB kinetics are largely unaffected by the introduction of the anti-γH2AX antibody, a result that has been validated experimentally, and hence the hypothesis that the use of anti-γH2AX antibody to quantify DSBs does not violate the image tracer principle.

View Article: PubMed Central - PubMed

Affiliation: Division of Mathematics, University of Dundee, Dundee, UK pmurray@dundee.ac.uk.

No MeSH data available.


Related in: MedlinePlus

A schematic of inclusion of the anti-γH2AX antibody.
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RSIF20150679F6: A schematic of inclusion of the anti-γH2AX antibody.

Mentions: To account for the effect of the anti-γH2AX-TAT antibody, it is assumed that anti-γH2AX-TAT binds reversibly to γH2AX and that the bound complex is inert (i.e. it prevents interaction of γH2AX with pATM, see schematic diagram presented in figure 6). Following a similar procedure to that outlined in §2.2 (see appendix A), we obtain4.1where 〈Q〉(t) is the expected numbers of bound antibody–γH2AX molecules,4.2[TAT]0 is the concentration of anti-γH2AX-TAT antibody, and k7 and k8 are dissociation and binding rates, respectively.Figure 6.


DNA double-strand break repair: a theoretical framework and its application.

Murray PJ, Cornelissen B, Vallis KA, Chapman SJ - J R Soc Interface (2016)

A schematic of inclusion of the anti-γH2AX antibody.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4759787&req=5

RSIF20150679F6: A schematic of inclusion of the anti-γH2AX antibody.
Mentions: To account for the effect of the anti-γH2AX-TAT antibody, it is assumed that anti-γH2AX-TAT binds reversibly to γH2AX and that the bound complex is inert (i.e. it prevents interaction of γH2AX with pATM, see schematic diagram presented in figure 6). Following a similar procedure to that outlined in §2.2 (see appendix A), we obtain4.1where 〈Q〉(t) is the expected numbers of bound antibody–γH2AX molecules,4.2[TAT]0 is the concentration of anti-γH2AX-TAT antibody, and k7 and k8 are dissociation and binding rates, respectively.Figure 6.

Bottom Line: It has previously been shown that anti-γH2AX antibodies, modified by the addition of the cell-penetrating peptide TAT and a fluorescent or radionuclide label, can be used to visualize and quantify DSBs in vivo.Equations that describe stochastic mean behaviours at individual DSB sites are derived and parametrized using population-scale, time-series measurements from two different cancer cell lines.This work supports the conclusion that DSB kinetics are largely unaffected by the introduction of the anti-γH2AX antibody, a result that has been validated experimentally, and hence the hypothesis that the use of anti-γH2AX antibody to quantify DSBs does not violate the image tracer principle.

View Article: PubMed Central - PubMed

Affiliation: Division of Mathematics, University of Dundee, Dundee, UK pmurray@dundee.ac.uk.

No MeSH data available.


Related in: MedlinePlus