Disease relevance of DNASE2B

• The DLAD-/- mice develop cataracts of the nucleus lentis, and their response to light on electroretinograms is severely reduced [1].
• Furthermore, the third ORF of the fowlpox virus genome is found to encode a DLAD homologue showing 37 [2].

High impact information on DNASE2B

• Although a recombinant protein for the putative human DLAD has a divalent cation-independent acid DNase activity, expression of the DLAD mRNA containing the entire open reading frame was not detected in any human tissues tested, except for lung, in which a short 1.1 kb transcript lacking the first two exons is expressed [3].
• The head-to-head organization of DLAD and UOX is conserved in the human genomic sequence [3].
• We have identified a novel DNase that shows homology to DNase II, named DLAD, from a search of an expressed sequence tag data base [4].
• The full-length cDNA for rat DLAD cloned by polymerase chain reaction encodes a 356-amino acid polypeptide containing a putative N-terminal signal peptide and 5 potential N-glycosylation sites; there is a predicted catalytic domain resemblance to rat DNase II [4].
• 2. Among known DNase inhibitors tested, aurintricarboxylic acid and Zn(2+)are found to be effective inhibitors of the DLAD activity [2].

Biological context of DNASE2B

• These results indicate that DLAD is responsible for the degradation of nuclear DNA during lens cell differentiation, and that if DNA is left undigested in the lens, it causes cataracts of the nucleus lentis, blocking the light path [1].

Analytical, diagnostic and therapeutic context of DNASE2B

• Northern blot analysis reveals that expression of the DLAD mRNA is highly restricted to the liver [2].

References