Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation

Dobó, József; Schroeder, Verena; Jenny, Lorenz; Cervenak, László; Závodszky, Péter; Gál, Péter (2014). Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation. Molecular immunology, 61(2), pp. 69-78. Elsevier 10.1016/j.molimm.2014.05.013

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MASP-1 is a versatile serine protease that cleaves a number of substrates in human blood. In recent years it became evident that besides playing a crucial role in complement activation MASP-1 also triggers other cascade systems and even cells to mount a more powerful innate immune response. In this review we summarize the latest discoveries about the diverse functions of this multi-faceted protease. Recent studies revealed that among MBL-associated serine proteases, MASP-1 is the one responsible for triggering the lectin pathway via its ability to rapidly autoactivate then cleave MASP-2, and possibly MASP-3. The crystal structure of MASP-1 explains its more relaxed substrate specificity compared to the related complement enzymes. Due to the relaxed specificity, MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Clinic of Haematology and Central Haematological Laboratory

UniBE Contributor:

Schröder, Verena

Subjects:

600 Technology > 610 Medicine & health

ISSN:

0161-5890

Publisher:

Elsevier

Language:

English

Submitter:

Verena Zwahlen

Date Deposited:

26 Mar 2015 11:49

Last Modified:

10 Dec 2019 14:47

Publisher DOI:

10.1016/j.molimm.2014.05.013

PubMed ID:

24935208

Uncontrolled Keywords:

Blood coagulation, Bradykinin, Complement system, Endothelial cell, Lectin pathway, Serine protease

BORIS DOI:

10.7892/boris.66096

URI:

https://boris.unibe.ch/id/eprint/66096

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