Disease relevance of NRD1

• Whereas aminopeptidase-B expression is enhanced in most cases, NRD convertase appears to undergo opposite regulation in proliferating versus differentiating neuroblastoma cells [1].

Psychiatry related information on NRD1

• However, the NRDC review 'Developmental Dyslexia in Adults: A Research Review' contains so many methodological flaws, including the highly selective way in which the research has been used, that the overall value of the report is questionable [2].

High impact information on NRD1

• N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration [3].
• Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell lines [4].
• The mechanism whereby NRD-C expression is regulated at the transcriptional level has been examined by reporter-gene assay and electrophoretic-mobility-shift assays [4].
• NRD convertase (N-arginine dibasic convertase, NRD-C) is a dibasic selective metalloprotease which cleaves on the N-terminal side of an arginine residue in a dibasic pair [4].
• We report the cloning of two human testis cDNA species encoding isoforms of NRD convertase, hNRD1 and hNRD2 [5].

Chemical compound and disease context of NRD1

• Expression and retinoid modulation of N-arginine dibasic convertase and an aminopeptidase-B in human neuroblastoma cell lines [1].

Biological context of NRD1

• These contain a predicted Nrd1p-binding site, potentially sequestering the protein and disrupting its autoregulation [6].
• The N-terminal region contains the HXXEH(X)76E catalytic domain that is conserved in the members of pitrilysin family, namely insulin-degrading enzyme and NRD convertase [7].

Anatomical context of NRD1

• Recently, it was recognized that the metalloendopeptidase N-arginine dibasic convertase (NRDc; nardilysin), which cleaves at the N-terminus side of basic residues in dibasic pairs, is localized both in the cytosol and at the cell surface or in the extracellular milieu [8].

Associations of NRD1 with chemical compounds

• We have used this model system to study the modulation of the transcriptional expression of putative processing enzymes, two novel metallopeptidases; i.e. N-arginine dibasic convertase (NRD convertase; EC 3.4,24,61) and an aminopeptidase-B after exposure of the cells either to retinoic acid or to synthetic retinoid analogs [1].
• Acute intoxication with cypermethrin (NRDC 149) [9].

References