Literature DB >> 33740660

Complement component factor B has thrombin-like activity.

Kazue Takahashi1, Nirmal K Banda2, V Michael Holers2, Elizabeth M Van Cott3.   

Abstract

Serine proteases are fundamental components of biology, including innate immunity, which is systematically orchestrated in an orderly, balanced fashion in the healthy host. Such serine proteases are found in two well-recognized pathways of an innate immune network, coagulation and complement. Both pathways, if uncontrolled due to a variety of causes, are pathogenic in numerous diseases, including coagulation disorders and infectious diseases. Previous studies have reported sequence homologies, functional similarities and interplay between these two pathways with some implications in health and disease. The current study newly reveals that complement component factor B (Bf), the second component of the alternative complement pathway, has thrombin-like activity, which is supported by a characteristic homology of the trypsin-like domain of Bf to that of thrombin. Moreover, we newly report that the trypsin-like domain of Bf is closely related to Limulus clotting factor C, the LPS sensitive clotting factor of the innate immune system. We will also discuss potential implications of our findings in diseases.
Copyright © 2021 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Coagulation diseases; Complement factor B; Infectious diseases; MBL-Associated serine protease (MASP); Serine proteases; Thrombin; Trypsin-like domain

Mesh:

Substances:

Year:  2021        PMID: 33740660      PMCID: PMC8035301          DOI: 10.1016/j.bbrc.2021.02.134

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  25 in total

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