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We demonstrated markedly delayed thrombin-catalysed fibrin polymerisation, through B:b interactions alone, of recombinant gamma D364H-fibrinogen with impaired hole \u0027a\u0027. To determine whether recombinant variant fibrinogens with no release of fibrinopeptide A (FpA) polymerise similarly to gamma D364H-fibrinoge, we examined two variant fibrinogens with substitutions altering knob \u0027A\u0027, A alpha 17A- and A alpha 17C-fibrinogen. We examined thrombin- or batroxobin-catalysed fibrinopeptide release by HPLC, fibrin clot formation by turbidity and fibrin clot structure by scanning electron microscopy (SEM) and compared the results of the variants with those for gamma D364H-fibrinogen. Thrombin-catalysed FpA release of A alpha 17A-fibrinogen was substantially delayed and none observed for A alpha 17C-fibrinogen; fibrinopeptide B (FpB) release was delayed for all variants. All variant fibrinogens showed substantially impaired thrombin-catalysed polymerisation; for A alpha 17A-fibrinogen it was delayed less, and for A alpha 17C more than for gamma D364H-fibrinogen. No variants polymerised with batroxobin, which exposed only knob \u0027A\u0027. The inhibition of variant fibrinogens\u0027 polymerisation was dose-dependent on the concentration of either GPRP or GHRP, and both peptides that block holes \u0027b\u0027. SEM showed that the variant clots from A alpha 17A- and gamma D364H-fibrinogen had uniform, ordered fibres, thicker than normal, whereas A alpha 17C-fibrinogen formed less organised clots with shorter, thinner, and tapered ends. 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We demonstrated markedly delayed thrombin-catalysed fibrin polymerisation, through B:b interactions alone, of recombinant gamma D364H-fibrinogen with impaired hole \u0027a\u0027. To determine whether recombinant variant fibrinogens with no release of fibrinopeptide A (FpA) polymerise similarly to gamma D364H-fibrinoge, we examined two variant fibrinogens with substitutions altering knob \u0027A\u0027, A alpha 17A- and A alpha 17C-fibrinogen. We examined thrombin- or batroxobin-catalysed fibrinopeptide release by HPLC, fibrin clot formation by turbidity and fibrin clot structure by scanning electron microscopy (SEM) and compared the results of the variants with those for gamma D364H-fibrinogen. Thrombin-catalysed FpA release of A alpha 17A-fibrinogen was substantially delayed and none observed for A alpha 17C-fibrinogen; fibrinopeptide B (FpB) release was delayed for all variants. All variant fibrinogens showed substantially impaired thrombin-catalysed polymerisation; for A alpha 17A-fibrinogen it was delayed less, and for A alpha 17C more than for gamma D364H-fibrinogen. No variants polymerised with batroxobin, which exposed only knob \u0027A\u0027. The inhibition of variant fibrinogens\u0027 polymerisation was dose-dependent on the concentration of either GPRP or GHRP, and both peptides that block holes \u0027b\u0027. SEM showed that the variant clots from A alpha 17A- and gamma D364H-fibrinogen had uniform, ordered fibres, thicker than normal, whereas A alpha 17C-fibrinogen formed less organised clots with shorter, thinner, and tapered ends. 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Fibrinopeptide A release is necessary for effective B:b interactions in polymerisation of variant fibrinogens with impaired A:a interactions
http://hdl.handle.net/10091/17324
http://hdl.handle.net/10091/17324aac5df6d-3764-4f94-bbaa-875bf82eaf75
名前 / ファイル | ライセンス | アクション |
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Fibrinopeptide_A_release_is_necessary_for_effective.pdf (751.9 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2013-12-27 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Fibrinopeptide A release is necessary for effective B:b interactions in polymerisation of variant fibrinogens with impaired A:a interactions | |||||
言語 | ||||||
言語 | eng | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1160/TH12-09-0684 | |||||
関連名称 | 10.1160/TH12-09-0684 | |||||
キーワード | ||||||
主題 | Fibrin polymerisation, B:b interaction, fibrinopeptide A release, knob 'A', hole 'a' | |||||
資源タイプ | ||||||
資源 | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | journal article | |||||
著者 |
Soya, Keisuke
× Soya, Keisuke× Terasawa, Fumiko× Okumura, Nobuo |
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信州大学研究者総覧へのリンク | ||||||
氏名 | Okumura, Nobuo | |||||
URL | http://soar-rd.shinshu-u.ac.jp/profile/ja.OVnmgCkh.html | |||||
出版者 | ||||||
出版者 | SCHATTAUER GMBH-VERLAG MEDIZIN NATURWISSENSCHAFTEN | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | THROMBOSIS AND HAEMOSTASIS. 109(2):221-228 (2013) | |||||
書誌情報 |
THROMBOSIS AND HAEMOSTASIS 巻 109, 号 2, p. 221-228, 発行日 2013-02 |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Fibrin polymerisation is mediated by interactions between knobs 'A' and 'B' exposed by thrombin cleavage, and holes 'a' and 'b'. We demonstrated markedly delayed thrombin-catalysed fibrin polymerisation, through B:b interactions alone, of recombinant gamma D364H-fibrinogen with impaired hole 'a'. To determine whether recombinant variant fibrinogens with no release of fibrinopeptide A (FpA) polymerise similarly to gamma D364H-fibrinoge, we examined two variant fibrinogens with substitutions altering knob 'A', A alpha 17A- and A alpha 17C-fibrinogen. We examined thrombin- or batroxobin-catalysed fibrinopeptide release by HPLC, fibrin clot formation by turbidity and fibrin clot structure by scanning electron microscopy (SEM) and compared the results of the variants with those for gamma D364H-fibrinogen. Thrombin-catalysed FpA release of A alpha 17A-fibrinogen was substantially delayed and none observed for A alpha 17C-fibrinogen; fibrinopeptide B (FpB) release was delayed for all variants. All variant fibrinogens showed substantially impaired thrombin-catalysed polymerisation; for A alpha 17A-fibrinogen it was delayed less, and for A alpha 17C more than for gamma D364H-fibrinogen. No variants polymerised with batroxobin, which exposed only knob 'A'. The inhibition of variant fibrinogens' polymerisation was dose-dependent on the concentration of either GPRP or GHRP, and both peptides that block holes 'b'. SEM showed that the variant clots from A alpha 17A- and gamma D364H-fibrinogen had uniform, ordered fibres, thicker than normal, whereas A alpha 17C-fibrinogen formed less organised clots with shorter, thinner, and tapered ends. These results demonstrate that FpA release per se is necessary for effective B:b interactions during polymerisation of variant fibrinogens with impaired A:a interactions. | |||||
資源タイプ(コンテンツの種類) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Article | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0340-6245 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00863137 | |||||
PubMed | ||||||
識別子タイプ | PMID | |||||
関連識別子 | https://pubmed.ncbi.nlm.nih.gov/23238100 | |||||
関連名称 | 23238100 | |||||
権利 | ||||||
権利情報 | This article is not an exact copy of the original published article in Thrombosis and Haemostasis. The definitive publisher-authenticated version of Thromb Haemost 2013 109 2: 221-228 is available online at: https://doi.org/10.1160/TH12-09-0684 . | |||||
出版タイプ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
WoS | ||||||
表示名 | Web of Science | |||||
URL | http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000314734500010 |