| First Author | Baron WF | Year | 1998 |
| Journal | Gene | Volume | 215 |
| Issue | 2 | Pages | 291-301 |
| PubMed ID | 9714828 | Mgi Jnum | J:49550 |
| Mgi Id | MGI:1277687 | Doi | 10.1016/s0378-1119(98)00281-9 |
| Citation | Baron WF, et al. (1998) Cloning and characterization of an actin-resistant DNase I-like endonuclease secreted by macrophages. Gene 215(2):291-301 |
| abstractText | We have cloned human and murine DNase I-like cDNAs, termed LS-DNase, which are expressed at high levels in liver and spleen tissues. LS-DNase expression is highly specific to macrophage populations within these and other tissues. Mature LS-DNase from both species is a secreted, non-glycosylated protein containing 285 residues, with a calculated molecular mass of 33 kDa and a basic isoelectric point. Human and murine LS-DNase are highly conserved and share 83% identity. Sequence analysis reveals that LS-DNase shares 46% amino acid sequence identity with DNase I. However, several residues identified as important for interaction of human DNase I with actin are not conserved in both human and murine LS-DNase. Consistent with this observation, recombinant human LS-DNase possesses a DNA hydrolytic activity which, unlike DNase I, is not inhibited by G-actin. The existence of a family of DNase I-like molecules that have tissue-specific expression patterns and the possible role of a macrophage specific DNase are discussed. |
