2013
DOI: 10.1515/hsz-2013-0211
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: Cells from several of the hematopoietic cell lineages including mast cells, basophils, neutrophils, cytotoxic T cells, and natural killer (NK) cells store proteases at very high levels within their cytoplasmic granules. In mast cells, these proteases can account for up to 35% of the total cellular protein, and the absolute majority of these belong to the chymotrypsin-related serine protease family. A number of very diverse functions have been identified for these proteases, including apoptosis induction, blood… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
85
1
1

Year Published

2015
2015
2022
2022

Publication Types

Select...
5
2

Relationship

0
7

Authors

Journals

citations
Cited by 50 publications
(87 citation statements)
references
References 62 publications
0
85
1
1
Order By: Relevance
“…Interactions with Granule Contents. Heparin proteoglycan (serglycin) is packed into mast cell secretory granules, along with histamine and abundant serine proteases (in humans, principally chymase 1, b-tryptase, and carboxypeptidase A3) (Hellman and Thorpe, 2014;Wernersson and Pejler, 2014). In this context, heparin, and sometimes chondroitin or dermatan sulfate, is assumed to act simply as a polyelectrolyte, allowing efficient packing of the basic proteins and histamine .…”
Section: G Interactions Between Heparin and Pathogensmentioning
confidence: 99%
“…Interactions with Granule Contents. Heparin proteoglycan (serglycin) is packed into mast cell secretory granules, along with histamine and abundant serine proteases (in humans, principally chymase 1, b-tryptase, and carboxypeptidase A3) (Hellman and Thorpe, 2014;Wernersson and Pejler, 2014). In this context, heparin, and sometimes chondroitin or dermatan sulfate, is assumed to act simply as a polyelectrolyte, allowing efficient packing of the basic proteins and histamine .…”
Section: G Interactions Between Heparin and Pathogensmentioning
confidence: 99%
“…Due to this tetrameric organization, tryptases are resistant to all endogenous protease inhibitors and have a relatively narrow substrate cleavage profile. In addition to the tetrameric tryptases, MCs express a monomeric transmembrane tryptase (γ-tryptase; Prss31; TPSG1) and an additional, enzymatically inactive tryptase denoted δ-tryptase (TPSD1) (Hellman & Thorpe, 2014). …”
Section: Mast Cell Biologymentioning
confidence: 99%
“…In contrast, the corresponding chymase locus in mice has undergone extensive expansion, and encompasses several different MC chymase genes, including one α-chymase (mMCP-5) but also several β-chymases: MC protease (Mcpt)1, Mcpt2, Mcpt4, Mcpt9 , and Mcpt10 (Hellman & Thorpe, 2014; Pejler et al, 2007) (the corresponding proteins are denoted mMCP-1, -2, -4, -5, -9, and -10, respectively). Based on amino acid sequence similarities, mMCP-5 may be regarded as the homologue to human chymase, which would suggest that Mcpt5 −/− animals might represent the most relevant model for studies of human chymase function.…”
Section: Mast Cell Biologymentioning
confidence: 99%
See 1 more Smart Citation
“…In addition to their intracellular role, NSPs are also important components of neutrophil degranulation fluid and NETs [9]. NSPs belong to the chymotrypsin family of serine proteases, in which a charge-relay system of His-Asp-Ser forms the catalytic site (for excellent reviews on NSP biochemistry please read [10] and [11]). Despite their similar sequences (35–56 % identical) and tertiary structures, however, they display different substrate specificities.…”
Section: Introductionmentioning
confidence: 99%