High impact information on Pde7a

• Since a single point mutation in the SNAG domain (P2A) inhibits both the Gfi-1-mediated transcriptional repression and the G1 arrest induced by IL-2 starvation, we conclude that the latter depends on the repressor activity of the SNAG domain [1].
• Phosphodiesterase 7A-deficient mice have functional T cells [2].
• P2A had L-PHA-reactive Asn-linked oligosaccharides with polylactosamine sequences as well as a large component of sialylated O-linked carbohydrates [3].
• The major L-PHA-binding glycoproteins in the highly metastatic lymphoid tumour cell line called MDAY-D2 were purified and resolved into two major species, termed P2A (110 kDa) and P2B (130 kDa) [3].
• The specificity activity of CNPase of the purified myelin and P2A from shiverer did not differ significantly from that of the controls [4].

Anatomical context of Pde7a

• From subcellular fractionation of sciatic nerves, it was found from the SDS-polyacrylamide gel electrophoresis that the Pl and Pr proteins equivalent to myelin basic protein of CNS and PM protein were missing in the shiverer in both P2A and P3A fractions in which PNS myelin is recovered [5].

Associations of Pde7a with chemical compounds

• The activities of 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNPase) of P2A and P3A fractions were high, but that of the P3X fraction which floated over 0.32 M sucrose was the highest among the fractions examined in both the shiverer and the control [5].

References