Origin and Expansion of the Serine Protease Repertoire in the Myelomonocyte Lineage release_ylw5gyh33basbmgqsqsgy2gcge

by Stefanie A. I. Weiss, Salome R. T. Rehm, Natascha C. Perera, Martin L. Biniossek, Oliver Schilling, Dieter E. Jenne

Published in International Journal of Molecular Sciences by MDPI AG.

2021   Volume 22, Issue 4, p1658

Abstract

The deepest evolutionary branches of the trypsin/chymotrypsin family of serine proteases are represented by the digestive enzymes of the gastrointestinal tract and the multi-domain proteases of the blood coagulation and complement system. Similar to the very old digestive system, highly diverse cleavage specificities emerged in various cell lineages of the immune defense system during vertebrate evolution. The four neutrophil serine proteases (NSPs) expressed in the myelomonocyte lineage, neutrophil elastase, proteinase 3, cathepsin G, and neutrophil serine protease 4, collectively display a broad repertoire of (S1) specificities. The origin of NSPs can be traced back to a circulating liver-derived trypsin-like protease, the complement factor D ancestor, whose activity is tightly controlled by substrate-induced activation and TNFα-induced locally upregulated protein secretion. However, the present-day descendants are produced and converted to mature enzymes in precursor cells of the bone marrow and are safely sequestered in granules of circulating neutrophils. The potential site and duration of action of these cell-associated serine proteases are tightly controlled by the recruitment and activation of neutrophils, by stimulus-dependent regulated secretion of the granules, and by various soluble inhibitors in plasma, interstitial fluids, and in the inflammatory exudate. An extraordinary dynamic range and acceleration of immediate defense responses have been achieved by exploiting the high structural plasticity of the trypsin fold.
In application/xml+jats format

Archived Files and Locations

application/pdf  2.1 MB
file_62ei6kqos5djdbejamlcuujfj4
res.mdpi.com (publisher)
web.archive.org (webarchive)
application/pdf  2.1 MB
file_rdflbj3psnaqpgtfcwr2hb5lmu
res.mdpi.com (web)
web.archive.org (webarchive)

Web Captures

https://www.mdpi.com/1422-0067/22/4/1658/htm
2022-08-11 00:21:06 | 43 resources
webcapture_3x2ub22a7vgffbsjqaur76jkau
web.archive.org (webarchive)
Read Archived PDF
Preserved and Accessible
Type  article-journal
Stage   published
Date   2021-02-07
Language   en ?
Journal Metadata
Open Access Publication
In DOAJ
In ISSN ROAD
In Keepers Registry
ISSN-L:  1422-0067
Work Entity
access all versions, variants, and formats of this works (eg, pre-prints)
Catalog Record
Revision: 090a2800-b6b9-4b31-84fc-9ff0d3030774
API URL: JSON