Structure and sequence of human M/NEI (monocyte/neutrophil elastase inhibitor), an Ov-serpin family gene

W Zeng1, G A Silverman, E Remold-O'Donnell

  • 1The Center for Blood Research, 800 Huntington Avenue, Boston, MA 02115, USA.

Gene
|June 19, 1998
PubMed

Insights

Human monocyte/neutrophil Elastase Inhibitor (M/NEI) regulates neutrophil proteases. This study characterizes the M/NEI gene structure, revealing conserved features among Ov-serpins.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Human monocyte/neutrophil Elastase Inhibitor (M/NEI) is a key regulator of neutrophil proteases.
  • M/NEI belongs to the functionally diverse Ov-serpin family, sharing structural similarities.

Purpose of the Study:

  • To isolate and characterize the full-length M/NEI gene, including upstream and downstream regulatory regions.
  • To investigate the gene structure, transcription start site, and polyadenylation signals of M/NEI.
  • To compare the M/NEI gene structure with related Ov-serpins.

Main Methods:

  • Isolation of recombinant lambda phage clones containing the M/NEI gene.
  • Primer extension to identify the transcription start site.
  • Southern blotting to determine gene copy number.
  • Analysis of 3' untranslated regions for polyadenylation signals.

Main Results:

  • The M/NEI gene is 9.5kb long, comprising 7 exons and 6 introns.
  • The transcription start site is in exon 1, and translation begins in exon 2.
  • Alternative polyadenylation signals (AATAAA/AATTAA) were identified in the 3' UTR.
  • A conserved upstream motif with an atypical TATA box was found, shared with target protease genes.

Conclusions:

  • The M/NEI gene structure provides insights into the regulation of neutrophil protease activity.
  • Ov-serpins share a common basic gene structure despite variations in chromosomal localization and exon number.
  • The identified upstream motif may play a role in the coordinated regulation of M/NEI and its target proteases.

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