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Cloning and characterization of an actin-resistant DNase I-like endonuclease secreted by macrophages
Affiliation:1. Instituto de Investigación Médica M. y M. Ferreyra (INIMEC – CONICET – Universidad Nacional de Córdoba), Córdoba C.P 5000, Argentina;2. Facultad de Psicología, Universidad Nacional de Córdoba, Córdoba C.P 5000, Argentina
Abstract: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 isolelectric 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.
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