An abnormal fibrinogen Fukuoka II (Gly-Bβ15 → Cys) characterized by defective fibrin lateral association and mixed disulfide formation

T. Kamura, H. Tsuda, Y. Yae, S. Hattori, Shoichi Ohga, Y. Shibata, Shun-Ichiro Kawabata, N. Hamasaki

研究成果: ジャーナルへの寄稿記事

17 引用 (Scopus)

抄録

A dysfibrinogenemia was attributable to a single amino acid substitution from glycine to cysteine at residue 15 of the Bβ chain in a fibrinogen molecule designated as fibrinogen Fukuoka II. The fibrinogen Fukuoka II showed prolonged thrombin and reptilase times and impaired fibrinopeptide B release by thrombin, resulting in abolition of fibrin monomer repolymerization under physiological conditions. Repolymerization of the des- (Bβ 1-42)-fibrin monomers, however, was not distinguished from the normal pattern of des-(Bβ 1-42)-fibrin monomers, suggesting that no other abnormality existed in fibrinogen Fukuoka II. Although an additional cysteine was substituted at residue 15 of the Bβ chain, fibrinogen Fukuoka II had no free sulfhydryl group within the molecule. Instead, fibrinogen Fukuoka II formed a disulfide bond with cysteine, albumin, another mutated B~ chain within the same molecule, or intermolecular dimeric fibrinogen Fukuoka II. The mutation in fibrinogen Fukuoka II was the same as that in fibrinogen Ise published previously (Yoshida, N., Wada, H., Morita, K., Hirata, H., Matsuda, M., Yamazumi, K., Asakura, S., and Shirakawa, S. (1991) Blood 77, 19581963). Fibrinogen Ise, however, has been described as having prolonged thrombin time but normal reptilase time. Reasons for the discrepancy were not clear. Analysis of the Bβ 1-42 fragment showed that fibrinogen was heterogeneous at position 31 of the Bβ chain with respect to proline or hydroxyproline.

元の言語英語
ページ(範囲)29392-29399
ページ数8
ジャーナルJournal of Biological Chemistry
270
発行部数49
DOI
出版物ステータス出版済み - 1 1 1995

Fingerprint

Abnormal Fibrinogens
Fibrin
Disulfides
Fibrinogen
Association reactions
Thrombin Time
Batroxobin
Thrombin
Cysteine
Molecules
Fibrinopeptide B
Hydroxyproline
Amino Acid Substitution
Proline
Glycine
Albumins
Blood
Substitution reactions

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

An abnormal fibrinogen Fukuoka II (Gly-Bβ15 → Cys) characterized by defective fibrin lateral association and mixed disulfide formation. / Kamura, T.; Tsuda, H.; Yae, Y.; Hattori, S.; Ohga, Shoichi; Shibata, Y.; Kawabata, Shun-Ichiro; Hamasaki, N.

:: Journal of Biological Chemistry, 巻 270, 番号 49, 01.01.1995, p. 29392-29399.

研究成果: ジャーナルへの寄稿記事

@article{79eb6d34cacc43be86a30780500d0310,
title = "An abnormal fibrinogen Fukuoka II (Gly-Bβ15 → Cys) characterized by defective fibrin lateral association and mixed disulfide formation",
abstract = "A dysfibrinogenemia was attributable to a single amino acid substitution from glycine to cysteine at residue 15 of the Bβ chain in a fibrinogen molecule designated as fibrinogen Fukuoka II. The fibrinogen Fukuoka II showed prolonged thrombin and reptilase times and impaired fibrinopeptide B release by thrombin, resulting in abolition of fibrin monomer repolymerization under physiological conditions. Repolymerization of the des- (Bβ 1-42)-fibrin monomers, however, was not distinguished from the normal pattern of des-(Bβ 1-42)-fibrin monomers, suggesting that no other abnormality existed in fibrinogen Fukuoka II. Although an additional cysteine was substituted at residue 15 of the Bβ chain, fibrinogen Fukuoka II had no free sulfhydryl group within the molecule. Instead, fibrinogen Fukuoka II formed a disulfide bond with cysteine, albumin, another mutated B~ chain within the same molecule, or intermolecular dimeric fibrinogen Fukuoka II. The mutation in fibrinogen Fukuoka II was the same as that in fibrinogen Ise published previously (Yoshida, N., Wada, H., Morita, K., Hirata, H., Matsuda, M., Yamazumi, K., Asakura, S., and Shirakawa, S. (1991) Blood 77, 19581963). Fibrinogen Ise, however, has been described as having prolonged thrombin time but normal reptilase time. Reasons for the discrepancy were not clear. Analysis of the Bβ 1-42 fragment showed that fibrinogen was heterogeneous at position 31 of the Bβ chain with respect to proline or hydroxyproline.",
author = "T. Kamura and H. Tsuda and Y. Yae and S. Hattori and Shoichi Ohga and Y. Shibata and Shun-Ichiro Kawabata and N. Hamasaki",
year = "1995",
month = "1",
day = "1",
doi = "10.1074/jbc.270.49.29392",
language = "English",
volume = "270",
pages = "29392--29399",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "49",

}

TY - JOUR

T1 - An abnormal fibrinogen Fukuoka II (Gly-Bβ15 → Cys) characterized by defective fibrin lateral association and mixed disulfide formation

AU - Kamura, T.

AU - Tsuda, H.

AU - Yae, Y.

AU - Hattori, S.

AU - Ohga, Shoichi

AU - Shibata, Y.

AU - Kawabata, Shun-Ichiro

AU - Hamasaki, N.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - A dysfibrinogenemia was attributable to a single amino acid substitution from glycine to cysteine at residue 15 of the Bβ chain in a fibrinogen molecule designated as fibrinogen Fukuoka II. The fibrinogen Fukuoka II showed prolonged thrombin and reptilase times and impaired fibrinopeptide B release by thrombin, resulting in abolition of fibrin monomer repolymerization under physiological conditions. Repolymerization of the des- (Bβ 1-42)-fibrin monomers, however, was not distinguished from the normal pattern of des-(Bβ 1-42)-fibrin monomers, suggesting that no other abnormality existed in fibrinogen Fukuoka II. Although an additional cysteine was substituted at residue 15 of the Bβ chain, fibrinogen Fukuoka II had no free sulfhydryl group within the molecule. Instead, fibrinogen Fukuoka II formed a disulfide bond with cysteine, albumin, another mutated B~ chain within the same molecule, or intermolecular dimeric fibrinogen Fukuoka II. The mutation in fibrinogen Fukuoka II was the same as that in fibrinogen Ise published previously (Yoshida, N., Wada, H., Morita, K., Hirata, H., Matsuda, M., Yamazumi, K., Asakura, S., and Shirakawa, S. (1991) Blood 77, 19581963). Fibrinogen Ise, however, has been described as having prolonged thrombin time but normal reptilase time. Reasons for the discrepancy were not clear. Analysis of the Bβ 1-42 fragment showed that fibrinogen was heterogeneous at position 31 of the Bβ chain with respect to proline or hydroxyproline.

AB - A dysfibrinogenemia was attributable to a single amino acid substitution from glycine to cysteine at residue 15 of the Bβ chain in a fibrinogen molecule designated as fibrinogen Fukuoka II. The fibrinogen Fukuoka II showed prolonged thrombin and reptilase times and impaired fibrinopeptide B release by thrombin, resulting in abolition of fibrin monomer repolymerization under physiological conditions. Repolymerization of the des- (Bβ 1-42)-fibrin monomers, however, was not distinguished from the normal pattern of des-(Bβ 1-42)-fibrin monomers, suggesting that no other abnormality existed in fibrinogen Fukuoka II. Although an additional cysteine was substituted at residue 15 of the Bβ chain, fibrinogen Fukuoka II had no free sulfhydryl group within the molecule. Instead, fibrinogen Fukuoka II formed a disulfide bond with cysteine, albumin, another mutated B~ chain within the same molecule, or intermolecular dimeric fibrinogen Fukuoka II. The mutation in fibrinogen Fukuoka II was the same as that in fibrinogen Ise published previously (Yoshida, N., Wada, H., Morita, K., Hirata, H., Matsuda, M., Yamazumi, K., Asakura, S., and Shirakawa, S. (1991) Blood 77, 19581963). Fibrinogen Ise, however, has been described as having prolonged thrombin time but normal reptilase time. Reasons for the discrepancy were not clear. Analysis of the Bβ 1-42 fragment showed that fibrinogen was heterogeneous at position 31 of the Bβ chain with respect to proline or hydroxyproline.

UR - http://www.scopus.com/inward/record.url?scp=0028874921&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028874921&partnerID=8YFLogxK

U2 - 10.1074/jbc.270.49.29392

DO - 10.1074/jbc.270.49.29392

M3 - Article

C2 - 7493975

AN - SCOPUS:0028874921

VL - 270

SP - 29392

EP - 29399

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 49

ER -