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Updated: Aug 19, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
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.
Abstract:
Human monocyte/neutrophil Elastase Inhibitor (M/NEI) is a proteinase inhibitor that regulates the activity of the neutrophil proteases: elastase, cathepsin G and proteinase-3. Evidence indicates that M/NEI belongs to the Ov-serpin family (ovalbumin-related serpins), functionally diverse proteins with shared structural features. Recombinant lambda phage clones were isolated that encompass the full-length M/NEI gene plus upstream and downstream regions. The gene, 9.5kb long, consists of 7 exons and 6 introns. The 5' transcription start site identified by primer extension corresponds to a 60bp exon 1; the translation start site is in exon 2. Southern blots established a gene copy number of one. The 3' untranslated region (UTR) contains three AATAAA/AATTAA sites; these were shown to function as alternative polyadenylation signals. A 14-nucleotide upstream motif including the atypical TATA box TATAAGAG otherwise occurs only twice in GenBank, in the genes encoding neutrophil elastase and proteinase-3, target proteases inhibited by M/NEI. Comparison of M/NEI and previously characterized related genes strongly suggests that all Ov-serpins, despite a difference in chromosomal localization and exon number, nonetheless, share a common basic gene structure.
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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