Studies on ADP-Ribose Polymer Metabolism in Cultured Mammalian Cells Following DNA Damage

PDF Version Also Available for Download.

Description

ADP-ribose polymer metabolism has been studied in human cells derived from a patient with Glutamyl Ribose Phosphate Storage Disease (GRPSD) and in mouse C3H1OT1/2 cells following oxidative stress induced by hydrogen peroxide (H202 ). It has been postulated that GRPSD resulted from an abnormality in ADP-ribose polymer metabolism. This study has shown that these cells exhibit reduced poly(ADP ribose) polymerase activity which is proposed to result from modification of the enzyme with ribose phosphate groups. The modification in the polymerase is proposed to be secondary to a defect in either ADP-ribosyl proteinlyase or an overproduction of a cellular phosphodiesterase. The ... continued below

Physical Description

x, 130 leaves, ill. ; 28 cm.

Creation Information

Maharaj, Geeta May 1991.

Context

This thesis is part of the collection entitled: UNT Theses and Dissertations and was provided by UNT Libraries to Digital Library, a digital repository hosted by the UNT Libraries. More information about this thesis can be viewed below.

Who

People and organizations associated with either the creation of this thesis or its content.

Chair

Publisher

Rights Holder

For guidance see Citations, Rights, Re-Use.

  • Maharaj, Geeta

Provided By

UNT Libraries

With locations on the Denton campus of the University of North Texas and one in Dallas, UNT Libraries serves the school and the community by providing access to physical and online collections; The Portal to Texas History and UNT Digital Libraries; academic research, and much, much more.

Contact Us

What

Descriptive information to help identify this thesis. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

ADP-ribose polymer metabolism has been studied in human cells derived from a patient with Glutamyl Ribose Phosphate Storage Disease (GRPSD) and in mouse C3H1OT1/2 cells following oxidative stress induced by hydrogen peroxide (H202 ). It has been postulated that GRPSD resulted from an abnormality in ADP-ribose polymer metabolism. This study has shown that these cells exhibit reduced poly(ADP ribose) polymerase activity which is proposed to result from modification of the enzyme with ribose phosphate groups. The modification in the polymerase is proposed to be secondary to a defect in either ADP-ribosyl proteinlyase or an overproduction of a cellular phosphodiesterase. The metabolism of ADP-ribose polymers was rapidly altered by H202 and there were independent effects on adenine nucleotide pools. The results suggest that ADP-ribose polymer metabolism is involved in cellular defenses to oxidative stress.

Physical Description

x, 130 leaves, ill. ; 28 cm.

Language

Identifier

Unique identifying numbers for this thesis in the Digital Library or other systems.

Collections

This thesis is part of the following collection of related materials.

UNT Theses and Dissertations

Theses and dissertations represent a wealth of scholarly and artistic content created by masters and doctoral students in the degree-seeking process. Some ETDs in this collection are restricted to use by the UNT community.

What responsibilities do I have when using this thesis?

When

Dates and time periods associated with this thesis.

Creation Date

  • May 1991

Added to The UNT Digital Library

  • March 9, 2015, 8:15 a.m.

Description Last Updated

  • Oct. 4, 2017, 10:18 a.m.

Usage Statistics

When was this thesis last used?

Yesterday: 0
Past 30 days: 3
Total Uses: 10

Interact With This Thesis

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

Citations, Rights, Re-Use

Maharaj, Geeta. Studies on ADP-Ribose Polymer Metabolism in Cultured Mammalian Cells Following DNA Damage, thesis, May 1991; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc500354/: accessed October 23, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .