Disease relevance of PDE7B

• Recombinant PDE7B protein expressed in a Baculovirus expression system is specific for cAMP with a K(m) of 0.03 microM [1].

High impact information on PDE7B

• PDE7A and PDE7B exhibit the same general pattern of inhibitor specificity among the several drugs tested [1].
• Based on sequence homologies, we designate this PDE as PDE7B [1].
• High PDE7B and PDE8B mRNA signal intensities were found in the hippocampal formation [2].
• Other standard PDE inhibitors including zaprinast, rolipram, and milrinone do not significantly inhibit PDE7B [3].
• We isolated a human cAMP-specific phosphodiesterase (PDE7B) cDNA from human caudate nucleus [4].

Biological context of PDE7B

• Comparison of the predicted protein sequences of PDE7A and PDE7B reveals an identity of 70% in the catalytic domain [1].
• Thus, the PDE7B exhibited unique tissue distribution in humans and kinetic profiles [4].

Anatomical context of PDE7B

• Recombinant PDE7B expressed in transfected COS-7 cells had a low cAMP K(m) value of 0 [4].
• Northern blot analysis demonstrated that PDE7B transcripts were abundantly expressed in the putamen, caudate nucleus, and heart followed by skeletal muscle, pancreas, and occipital pole [4].

Associations of PDE7B with chemical compounds

• The PDE7B activity was inhibited by dipyridamole and SCH51866, with IC(50) values of 1.1 microM and 1.5 microM, respectively [4].

Other interactions of PDE7B

• The predicted protein sequence of PDE7B showed highest homology (70% identity) to that of PDE7A [3].

Analytical, diagnostic and therapeutic context of PDE7B

• Northern blotting indicates that the mRNA of PDE7B is 5.6 kb [1].

References