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Position of cyclization in cyclic ADP-ribose
H Kim1, E L Jacobson, M K Jacobson
1Division of Medicinal Chemistry & Pharmaceutics, College of Pharmacy, University of Kentucky, Lexington 40536.
Biochemical and Biophysical Research Communications
|August 16, 1993
Summary
Cyclic adenosine diphosphoribose (cADPR) is a calcium signaling molecule. This study
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Signaling
Background:
- Cyclic adenosine diphosphoribose (cADPR) is recognized as a second messenger involved in calcium homeostasis.
- Its synthesis from NAD involves cleavage and cyclization reactions.
- The precise structure of cADPR, specifically the cyclization site on the adenine ring, has been a subject of debate.
Purpose of the Study:
- To elucidate the exact structure of cyclic adenosine diphosphoribose (cADPR).
- To determine the specific position of cyclization on the adenine ring in cADPR.
- To resolve conflicting proposals regarding cADPR's molecular structure.
Main Methods:
- Spectroscopic analysis of cADPR using ultraviolet (UV) absorption.
- pH-dependent studies of cADPR's UV absorption spectra.
- Comparative spectral analysis with adenine ring compounds of known structures.
Main Results:
- The UV absorption spectra of cADPR were characterized across a range of pH values.
- Comparison with related adenine compounds provided structural insights.
- The spectral data strongly support a specific cyclization site for cADPR.
Conclusions:
- The findings confirm that cADPR cyclization occurs at position 1 of the adenine ring.
- This contradicts previous hypotheses suggesting cyclization at the N6 position.
- The study clarifies the molecular structure of cADPR, impacting understanding of calcium signaling pathways.