Cathepsin G activates protease-activated receptor-4 in human platelets (Q22253276)

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scientific article

Language	Label	Description	Also known as
English	Cathepsin G activates protease-activated receptor-4 in human platelets	scientific article

Statements

scholarly article

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Cathepsin G activates protease-activated receptor-4 in human platelets (English)

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F2R like thrombin or trypsin receptor 3

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GOA release 2020-03-11

signal transduction

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GOA release 2020-03-11

author name string

G R Sambrano

1

author given names

G R

author last names

Sambrano

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PubMed publication ID

8 February 2023

W Huang

2

author given names

W

author last names

Huang

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PubMed publication ID

8 February 2023

T Faruqi

3

author given names

T

author last names

Faruqi

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PubMed publication ID

8 February 2023

S Mahrus

4

author given names

S

author last names

Mahrus

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PubMed publication ID

8 February 2023

C Craik

5

author given names

C

author last names

Craik

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PubMed publication ID

8 February 2023

S R Coughlin

6

author given names

S R

author last names

Coughlin

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PubMed publication ID

8 February 2023

language of work or name

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publication date

10 March 2000

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Journal of Biological Chemistry

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275

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10

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6819-23

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Augmented inflammatory responses and altered wound healing in cathepsin G-deficient mice

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Engineering bidentate macromolecular inhibitors for trypsin and urokinase-type plasminogen activator

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Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors

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17 The kinetics of reversible tight-binding inhibition

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based on heuristic

inferred from DOI database lookup

Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation

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Susceptibility to infection and altered hematopoiesis in mice deficient in both P- and E-selectins

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Human neutrophil cathepsin G is a potent platelet activator

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https://api.crossref.org/works/10.1074%2FJBC.275.10.6819

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Development of potent thrombin receptor antagonist peptides

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A dual thrombin receptor system for platelet activation

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inferred from DOI database lookup

Protease-activated receptor 3 is a second thrombin receptor in humans

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based on heuristic

inferred from DOI database lookup

Cathepsin G binding to human platelets. Evidence for a specific receptor

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based on heuristic

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Intracellular Ca2+ rise in human platelets induced by polymorphonuclear-leucocyte-derived cathepsin G.

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based on heuristic

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Cathepsin G and thrombin: evidence for two different platelet receptors

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based on heuristic

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Shwartzman reaction

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based on heuristic

inferred from DOI database lookup

Molecular cloning of a potential proteinase activated receptor

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based on heuristic

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Cloning and characterization of human protease-activated receptor 4

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based on heuristic

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Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G.

1 reference

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based on heuristic

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The cloned thrombin receptor is necessary and sufficient for activation of mitogen-activated protein kinase and mitogenesis in mouse lung fibroblasts. Loss of responses in fibroblasts from receptor knockout mice

1 reference

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Human neutrophil elastase proteolytically activates the platelet integrin alphaIIbbeta3 through cleavage of the carboxyl terminus of the alphaIIb subunit heavy chain. Involvement in the potentiation of platelet aggregation

1 reference

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based on heuristic

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Thrombin-induced events in non-platelet cells are mediated by the unique proteolytic mechanism established for the cloned platelet thrombin receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.10.6819

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based on heuristic

inferred from DOI database lookup

Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.10.6819

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based on heuristic

inferred from DOI database lookup

Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.10.6819

7 January 2021

based on heuristic

inferred from DOI database lookup

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