Maintenance of ribosomal protein S19 in plasma by complex formation with prothrombin

We have demonstrated that the cross‐linking of ribosomal protein S19 (RP S19) on platelets by activated factor XIII provides chemotactic potency to monocytes/macrophages for a resolution of coagulum. Factor XIII is activated by an active form of prothrombin, thrombin. We here report that RP S19 is p...

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Bibliographic Details
Published in:European journal of haematology 2011-05, Vol.86 (5), p.436-441
Main Authors: Nishiura, Hiroshi, Tanase, Sumio, Tsujita, Kenichi, Sugiyama, Seigo, Ogawa, Hisao, Nakagaki, Tomohiro, Semba, Umeko, Yamamoto, Tetsuro
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anticoagulants - pharmacology
Binding Sites
Blood coagulation
Blood Coagulation - physiology
Blood Platelets - metabolism
Calcium - blood
Cross-Linking Reagents
Factor X - metabolism
Factor XIIIa - metabolism
Gla domain
Humans
In Vitro Techniques
Multiprotein Complexes - blood
Multiprotein Complexes - chemistry
plasma proteins
Protein Structure, Tertiary
prothrombin
Prothrombin - chemistry
Prothrombin - genetics
Prothrombin - metabolism
ribosomal protein S19
Ribosomal Proteins - blood
Ribosomal Proteins - chemistry
Warfarin - pharmacology
warfarin treatment
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Summary:We have demonstrated that the cross‐linking of ribosomal protein S19 (RP S19) on platelets by activated factor XIII provides chemotactic potency to monocytes/macrophages for a resolution of coagulum. Factor XIII is activated by an active form of prothrombin, thrombin. We here report that RP S19 is present as a complex with prothrombin in the blood stream. Formation of this complex was blocked by a mutation of the glycosaminoglycan‐binding basic cluster (Lys23–Lys29) in RP S19. Prothrombin–RP S19 interaction was enhanced by an absence of Ca2+ and the plasma RP S19 concentration was significantly low in the patient treated with warfarin, indicating participation of the γ‐carboxyl glutamic acid domain of prothrombin making a salt bridge with the basic cluster. The complex formation likely explains why a protein as small as RP S19 can prevent from a filtering system of renal glomeruli at a steady state. The translocation of RP S19 from prothrombin to platelets during blood coagulation seems to be also advantageous for RP S19 from the perspective of oligomerisation by activated factor XIII, which should have been activated by thrombin.
ISSN:0902-4441
1600-0609
DOI:10.1111/j.1600-0609.2011.01585.x