High impact information on Pepd

• The gene for apoE, designated Apoe, is located on chromosome 7, linked to genes for glucose phosphate isomerase and peptidase 4 [1].
• Therefore, we suspected phosphorylation of prolidase as a potential mechanism regulating enzyme activation [2].
• Nitric oxide regulates prolidase activity by serine/threonine phosphorylation [2].
• We observed increased serine/threonine phosphorylation on prolidase protein in cells treated with NO donors and in cells transfected with iNOS [2].
• Prolidase [E.C. 3.4.13.9], a member of the matrix metalloproteinase (MMP) family, is a manganese-dependent cytosolic exopeptidase that cleaves imidodipeptides containing C-terminal proline or hydroxyproline [2].

Biological context of Pepd

• Analysis of progeny from reciprocal backcrosses established that the electrophoretic forms are expressed codominantly and that Pep-4 is located between the genes for glucosephosphate isomerase (Gpi-1) and pink-eyed dilution (p) on chromosome 7 [3].
• We cloned mouse prolidase cDNA from a mouse liver cDNA library [4].

Associations of Pepd with chemical compounds

• These results demonstrate that NO stimulates prolidase activity by increasing serine/threonine phosphorylation through PKG-cGMP pathway, but independent of MAPK and suggest an interaction between inflammatory signaling pathways and regulation of the terminal step of matrix degradation [2].
• To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation [2].
• Comparative gene mapping in man and mouse: assignment of the genes for lactate dehydrogenase-A, peptidase-D, and isocitrate dehydrogenase-2 to mouse chromosome 7 [5].

Analytical, diagnostic and therapeutic context of Pepd

• Northern blot analysis showed that while prolidase mRNA was transcribed in brain, heart, liver, and muscle, it was predominantly transcribed in kidney [4].

References