NDLI: MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis

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MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis

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MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tan, Ying S. Takahashi, Kazue Takahashi, Minoru Stahl, Gregory L. Banda, Nirmal K. Fujita, Teizo Zou, Chenhui La Bonte, Laura R. Pavlov, Vasile I.
Description	Country affiliation: United States Author Affiliation: La Bonte LR ( Department of Anesthesiology, Perioperative and Pain Medicine, Center for Experimental Therapeutics and Reperfusion Injury, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.)
Abstract	Bleeding disorders and thrombotic complications constitute a major cause of death and disability worldwide. Although it is known that the complement and coagulation systems interact, no studies have investigated the specific role or mechanisms of lectin-mediated coagulation in vivo. FeCl(3) treatment resulted in intra-arterial occlusive thrombogenesis within 10 min in wild-type (WT) and C2/factor B-null mice. In contrast, mannose-binding lectin (MBL)-null and MBL-associated serine protease (MASP)-1/-3 knockout (KO) mice had significantly decreased FeCl(3)-induced thrombogenesis. Reconstitution with recombinant human (rh) MBL restored FeCl(3)-induced thrombogenesis in MBL-null mice to levels comparable to WT mice, suggesting a significant role of the MBL/MASP complex for in vivo coagulation. Additionally, whole blood aggregation demonstrated increased MBL/MASP complex-dependent platelet aggregation. In vitro, MBL/MASP complexes were captured on mannan-coated plates, and cleavage of a chromogenic thrombin substrate (S2238) was measured. We observed no significant differences in S2238 cleavage between WT, C2/factor B-null, MBL-A(-/-), or MBL-C(-/-) sera; however, MBL-null or MASP-1/-3 KO mouse sera demonstrated significantly decreased S2238 cleavage. rhMBL alone failed to cleave S2238, but cleavage was restored when rMASP-1 was added to either MASP-1/-3 KO sera or rhMBL. Taken together, these findings indicate that MBL/MASP complexes, and specifically MASP-1, play a key role in thrombus formation in vitro and in vivo.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1102916
Journal	The Journal of Immunology
Issue Number	2
Volume Number	188
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2012-01-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Blood Coagulation Carotid Artery Thrombosis Enzymology Complement Pathway, Mannose-binding Lectin Mannose-binding Protein-associated Serine Proteases Physiology Animals Immunology Chemically Induced Genetics Chlorides Toxicity Disease Models, Animal Ferric Compounds Immunity, Innate Mannose-binding Lectins Deficiency Adverse Effects Mice Thrombin Research Support, N.i.h., Extramural Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis

Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway.

Complement lectin pathway components MBL and MASP-1 promote haemostasis upon vessel injury in a microvascular bleeding model

Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2.

Crystal Structure and Functional Characterization of the Complement Regulator Mannose-binding Lectin (MBL)/Ficolin-associated Protein-1 (MAP-1)

Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation.

Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway

Comment on 'Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function'.

Response to comment on 'Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function'.

MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis

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MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis

Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway.

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Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway

Comment on 'Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function'.

Response to comment on 'Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function'.

MBL-Associated Serine Protease -1 (MASP-1) is a Significant Contributor to Coagulation in a Murine Model of Occlusive Thrombosis