Study of the sites of plasminogen molecule which are responsible for inhibitory effect of Lys-plasminogen on platelet aggregation
Plasminogen/plasmin system is involved in such important processes as thrombosis, inflammation and cancer. Plasmin and plasminogen mediate their action through plasminogen-binding proteins on the cell surface. Lys-plasminogen, but not Glu-plasminogen, shows inhibitory effect on platelet aggregation induced by ADP, collagen and thrombin in preparations of both: platelet-rich plasma and washed platelets. We have shown that the kringle domains of Lys-plasminogen mediate interaction of this proenzyme with platelet- surface proteins. The aim of the work is to study the role of certain kringle domains in the inhibitory effect of Lys-plasminogen and to determine possible plasminogen-binding proteins on the platelet surface. All studied plasminogen fragments (K1-3, K4 and K5) abolished the inhibitory effect of Lys-plasminogen on platelet aggregation. We observed that K5 was more effective than K1-3 and K4. Biotin-labeled Lys-plasminogen, Glu-plasminogen and plasminogen fragment K1-3 possessed the highest affinity for actin, whereas the binding of biotin-labeled mini-plasminogen and K4 to actin was negligible. We have suggested that inhibitory effect of Lys-plasminogen is due to the interaction of kringle domains of this proenzyme with membrane-bound proteins which are exposed on the platelet surface during activation and are involved in thrombus formation.
| Medienart: |
Artikel |
|---|
| Erscheinungsjahr: |
2014 |
|---|---|
| Erschienen: |
2014 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:86 |
|---|---|
| Enthalten in: |
Ukrainian biochemical journal - 86(2014), 5 vom: 01. Sept., Seite 82-8 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Roka-Moya, Y M [VerfasserIn] |
|---|
| Themen: |
9001-32-5 |
|---|
| Anmerkungen: |
Date Completed 17.04.2015 Date Revised 13.11.2019 published: Print Citation Status MEDLINE |
|---|
| Förderinstitution / Projekttitel: |
|
|---|
| PPN (Katalog-ID): |
NLM247499862 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM247499862 | ||
| 003 | DE-627 | ||
| 005 | 20231224145347.0 | ||
| 007 | tu | ||
| 008 | 231224s2014 xx ||||| 00| ||eng c | ||
| 028 | 5 | 2 | |a pubmed24n0825.xml |
| 035 | |a (DE-627)NLM247499862 | ||
| 035 | |a (NLM)25816591 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Roka-Moya, Y M |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Study of the sites of plasminogen molecule which are responsible for inhibitory effect of Lys-plasminogen on platelet aggregation |
| 264 | 1 | |c 2014 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 17.04.2015 | ||
| 500 | |a Date Revised 13.11.2019 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Plasminogen/plasmin system is involved in such important processes as thrombosis, inflammation and cancer. Plasmin and plasminogen mediate their action through plasminogen-binding proteins on the cell surface. Lys-plasminogen, but not Glu-plasminogen, shows inhibitory effect on platelet aggregation induced by ADP, collagen and thrombin in preparations of both: platelet-rich plasma and washed platelets. We have shown that the kringle domains of Lys-plasminogen mediate interaction of this proenzyme with platelet- surface proteins. The aim of the work is to study the role of certain kringle domains in the inhibitory effect of Lys-plasminogen and to determine possible plasminogen-binding proteins on the platelet surface. All studied plasminogen fragments (K1-3, K4 and K5) abolished the inhibitory effect of Lys-plasminogen on platelet aggregation. We observed that K5 was more effective than K1-3 and K4. Biotin-labeled Lys-plasminogen, Glu-plasminogen and plasminogen fragment K1-3 possessed the highest affinity for actin, whereas the binding of biotin-labeled mini-plasminogen and K4 to actin was negligible. We have suggested that inhibitory effect of Lys-plasminogen is due to the interaction of kringle domains of this proenzyme with membrane-bound proteins which are exposed on the platelet surface during activation and are involved in thrombus formation | ||
| 650 | 4 | |a Journal Article | |
| 650 | 7 | |a Actins |2 NLM | |
| 650 | 7 | |a Peptide Fragments |2 NLM | |
| 650 | 7 | |a Thrombospondins |2 NLM | |
| 650 | 7 | |a lysyl-plasminogen |2 NLM | |
| 650 | 7 | |a miniplasminogen |2 NLM | |
| 650 | 7 | |a Fibrinogen |2 NLM | |
| 650 | 7 | |a 9001-32-5 |2 NLM | |
| 650 | 7 | |a Plasminogen |2 NLM | |
| 650 | 7 | |a 9001-91-6 |2 NLM | |
| 650 | 7 | |a Thrombin |2 NLM | |
| 650 | 7 | |a EC 3.4.21.5 |2 NLM | |
| 650 | 7 | |a Fibrinolysin |2 NLM | |
| 650 | 7 | |a EC 3.4.21.7 |2 NLM | |
| 700 | 1 | |a Zhernossekov, D D |e verfasserin |4 aut | |
| 700 | 1 | |a Yusova, E I |e verfasserin |4 aut | |
| 700 | 1 | |a Kapustianenko, L G |e verfasserin |4 aut | |
| 700 | 1 | |a Grinenko, T V |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Ukrainian biochemical journal |d 2014 |g 86(2014), 5 vom: 01. Sept., Seite 82-8 |w (DE-627)NLM238310728 |x 2409-4943 |7 nnns |
| 773 | 1 | 8 | |g volume:86 |g year:2014 |g number:5 |g day:01 |g month:09 |g pages:82-8 |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 86 |j 2014 |e 5 |b 01 |c 09 |h 82-8 | ||