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Primary structure of human neutrophil elastase.

S Sinha, W Watorek, S Karr

Proceedings of the National Academy of Sciences of the United States of America

|April 1, 1987

Summary

The complete amino acid sequence of human neutrophil elastase was determined, revealing a unique structure. This finding suggests distinct functional mechanisms compared to other serine proteases.

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Area of Science:

Biochemistry
Proteomics
Molecular Biology

Background:

Human neutrophil elastase (HNE) is a key serine protease involved in inflammatory processes.
Understanding HNE's structure is crucial for developing targeted therapeutics.

Purpose of the Study:

To determine the complete amino acid sequence of human neutrophil elastase.
To compare HNE's sequence with other related serine proteases.

Main Methods:

Amino acid sequencing
Sequence homology analysis

Main Results:

The complete amino acid sequence of HNE, comprising 218 residues, was elucidated.
HNE contains two asparagine-linked carbohydrate chains and four disulfide bonds.

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Sequence comparison revealed moderate homology with porcine pancreatic elastase (43.0%) and neutrophil cathepsin G (37.2%).

Significant differences in key residues suggest alternative binding mechanisms for HNE compared to pancreatic elastase.

Conclusions:

The determined sequence provides a foundation for understanding HNE's structure-function relationship.
HNE exhibits unique structural features that differentiate it from other serine proteases.
These findings may guide the development of selective HNE inhibitors.