Disease relevance of Dpep1

• 4-(Methyl)benzenediazonium sulfate (MBD) was administered to Swiss mice by subcutaneous injection at weekly intervals 19 or 16 times at 50 micrograms/g body weight [1].

High impact information on Dpep1

• However, we found that MBD1-/- neural stem cells exhibited reduced neuronal differentiation and increased genomic instability [2].
• Methyl-CpG binding protein 1 (MBD1), a member of the methylated DNA-binding protein family, has been shown to bind methylated gene promoters and facilitate transcriptional repression in vitro [2].
• Furthermore, adult MBD1-/- mice had decreased neurogenesis, impaired spatial learning, and a significant reduction in long-term potentiation in the dentate gyrus of the hippocampus [2].
• Leukotriene D4 and cystinyl-bis-glycine metabolism in membrane-bound dipeptidase-deficient mice [3].
• We have developed mice deficient in membrane-bound dipeptidase (MBD, EC 3.4.13.19), the enzyme believed to be responsible for the conversion of leukotriene D4 (LTD4) to leukotriene E4 (LTE4) [3].

Biological context of Dpep1

• The MBD-3 and MBD-1 cDNAs share a 55% nucleotide identity and a 39% predicted amino acid sequence identity [4].
• MBD gene deletion had no effect on viability or fertility [3].
• Null mutations have been generated in mice for several MBD family members, the phenotypes of the mutant animals raise important questions regarding the functions of the MBD family [5].
• Repression of nonmethylated reporter genes depends on the CXXC-3 domain, whereas repression of methylated reporters requires the MBD [6].
• MBD1 is a vertebrate methyl-CpG binding domain protein (MBD) that can bring about repression of methylated promoter DNA sequences [6].

Anatomical context of Dpep1

• MBD-1 is expressed at highest levels in kidney, lung, and heart and is absent in spleen, while MBD-2 is expressed at highest levels in lung, heart, and testis and at somewhat lower levels in spleen [4].
• The MBD mutation generated by us was demonstrated to be a null mutation by Northern blot analysis and the absence of beta-lactamase activity in lung, kidney, small intestine, and heart [3].

Associations of Dpep1 with chemical compounds

• These enzymes are closely related to MBD-1 (EC 3.4.13.19), which is known to cleave leukotriene D4 (LTD4) and cystinyl-bis-glycine [4].
• MBD is also believed to function consecutively after gamma-glutamyl transpeptidase to cleave cystinyl-bis-glycine (cys-bis-gly) generated from glutathione cleavage [3].
• These observations demonstrate that the conversion of LTD4 to LTE4 and the degradation of cys-bis-gly are catalyzed by at least two alternative pathways (one of which is MBD) that complement each other to varying extents in different tissues [3].
• The preparation of mutual pro-drugs of the olivanic acids and an inhibitor of the renal dipeptidase enzyme is described [7].
• MBD is closely related to 4-(hydroxymethyl)benzenediazonium ion (HMBD), an ingredient of the cultivated mushroom Agaricus bisporus [1].

Other interactions of Dpep1

• MBD-2 cDNA is 56% identical to MBD-1 with a predicted amino acid identity of 33% [4].
• However, in the lung, MBD is expressed at high levels, whereas GGT is almost undetectable [8].

Analytical, diagnostic and therapeutic context of Dpep1

• After saturation of MBD with nickel or cobalt, scFv:MBD was imaged with electron spectroscopic imaging at each element's specific energy loss, thus generating the element's map [9].

References