Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress

Yuta Taniuchi, Tomihisa Kawasaki, Yoshihiro Fujimura, Masami Suzuki, Koiti Titani, Yumiko Sakai, Seiji Kaku, Nami Hisamichi, Noboru Satoh, Toichi Takenaka, Makoto Handa, Yoshio Sawai

研究成果: Article

74 引用 (Scopus)

抄録

Two high molecular mass proteins, flavocetin-A and flavocetin-B, were purified from Trimeresurus flavoviridis venom. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the apparent molecular mass of flavocetin-A and -B were 149 and 139 kDa, respectively, under nonreducing conditions. On reduction, flavocetin-A showed two distinct subunits (17 and 14 kDa), and flavocetin-B three distinct subunits (17, 15 and 14 kDa). At 1 μg/ml, flavocetin-A and -B (flavocetins) inhibited the von Willebrand factor (vWF)-dependent aggregation of fixed human platelets. However, flavocetins (10 μg/ml) had no effect on ADP- and collagen-induced platelet aggregation in PRP. Flavocetins (3 μg/ml) also inhibited shear-induced platelet aggregation at high shear stress. Furthermore, flavocetin-A completely inhibited the aggregation of and ATP release from washed platelets stimulated with a low concentration of thrombin. Flavocetin-A specifically bound to platelet with high affinity (Kd = 0.35 ± 0.13 nM) at 21 500 ± 1760 binding sites per platelet. The N-terminal amino acid sequences of the subunits of flavocetin-A show a high degree of homology with those of echicetin, botrocetin, alboaggregin-B and factor IX/factor X-binding protein. These results suggest that flavocetins may be a useful tool for further investigation of the GPIb-vWF interaction.

元の言語English
ページ(範囲)331-338
ページ数8
ジャーナルBBA - General Subjects
1244
発行部数2-3
DOI
出版物ステータスPublished - 1995 6 9

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Platelet Glycoprotein GPIb-IX Complex
Venoms
Molecular mass
Platelets
Platelet Aggregation
Shear stress
Carrier Proteins
Agglomeration
Blood Platelets
von Willebrand Factor
Factor X
Factor IX
flavocetin A
Trimeresurus venoms
Electrophoresis
Thrombin
Sodium Dodecyl Sulfate
Adenosine Diphosphate
Polyacrylamide Gel Electrophoresis
Amino Acid Sequence

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

これを引用

Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress. / Taniuchi, Yuta; Kawasaki, Tomihisa; Fujimura, Yoshihiro; Suzuki, Masami; Titani, Koiti; Sakai, Yumiko; Kaku, Seiji; Hisamichi, Nami; Satoh, Noboru; Takenaka, Toichi; Handa, Makoto; Sawai, Yoshio.

:: BBA - General Subjects, 巻 1244, 番号 2-3, 09.06.1995, p. 331-338.

研究成果: Article

Taniuchi, Y, Kawasaki, T, Fujimura, Y, Suzuki, M, Titani, K, Sakai, Y, Kaku, S, Hisamichi, N, Satoh, N, Takenaka, T, Handa, M & Sawai, Y 1995, 'Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress', BBA - General Subjects, 巻. 1244, 番号 2-3, pp. 331-338. https://doi.org/10.1016/0304-4165(95)00052-D
Taniuchi, Yuta ; Kawasaki, Tomihisa ; Fujimura, Yoshihiro ; Suzuki, Masami ; Titani, Koiti ; Sakai, Yumiko ; Kaku, Seiji ; Hisamichi, Nami ; Satoh, Noboru ; Takenaka, Toichi ; Handa, Makoto ; Sawai, Yoshio. / Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress. :: BBA - General Subjects. 1995 ; 巻 1244, 番号 2-3. pp. 331-338.
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abstract = "Two high molecular mass proteins, flavocetin-A and flavocetin-B, were purified from Trimeresurus flavoviridis venom. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the apparent molecular mass of flavocetin-A and -B were 149 and 139 kDa, respectively, under nonreducing conditions. On reduction, flavocetin-A showed two distinct subunits (17 and 14 kDa), and flavocetin-B three distinct subunits (17, 15 and 14 kDa). At 1 μg/ml, flavocetin-A and -B (flavocetins) inhibited the von Willebrand factor (vWF)-dependent aggregation of fixed human platelets. However, flavocetins (10 μg/ml) had no effect on ADP- and collagen-induced platelet aggregation in PRP. Flavocetins (3 μg/ml) also inhibited shear-induced platelet aggregation at high shear stress. Furthermore, flavocetin-A completely inhibited the aggregation of and ATP release from washed platelets stimulated with a low concentration of thrombin. Flavocetin-A specifically bound to platelet with high affinity (Kd = 0.35 ± 0.13 nM) at 21 500 ± 1760 binding sites per platelet. The N-terminal amino acid sequences of the subunits of flavocetin-A show a high degree of homology with those of echicetin, botrocetin, alboaggregin-B and factor IX/factor X-binding protein. These results suggest that flavocetins may be a useful tool for further investigation of the GPIb-vWF interaction.",
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T1 - Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress

AU - Taniuchi, Yuta

AU - Kawasaki, Tomihisa

AU - Fujimura, Yoshihiro

AU - Suzuki, Masami

AU - Titani, Koiti

AU - Sakai, Yumiko

AU - Kaku, Seiji

AU - Hisamichi, Nami

AU - Satoh, Noboru

AU - Takenaka, Toichi

AU - Handa, Makoto

AU - Sawai, Yoshio

PY - 1995/6/9

Y1 - 1995/6/9

N2 - Two high molecular mass proteins, flavocetin-A and flavocetin-B, were purified from Trimeresurus flavoviridis venom. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the apparent molecular mass of flavocetin-A and -B were 149 and 139 kDa, respectively, under nonreducing conditions. On reduction, flavocetin-A showed two distinct subunits (17 and 14 kDa), and flavocetin-B three distinct subunits (17, 15 and 14 kDa). At 1 μg/ml, flavocetin-A and -B (flavocetins) inhibited the von Willebrand factor (vWF)-dependent aggregation of fixed human platelets. However, flavocetins (10 μg/ml) had no effect on ADP- and collagen-induced platelet aggregation in PRP. Flavocetins (3 μg/ml) also inhibited shear-induced platelet aggregation at high shear stress. Furthermore, flavocetin-A completely inhibited the aggregation of and ATP release from washed platelets stimulated with a low concentration of thrombin. Flavocetin-A specifically bound to platelet with high affinity (Kd = 0.35 ± 0.13 nM) at 21 500 ± 1760 binding sites per platelet. The N-terminal amino acid sequences of the subunits of flavocetin-A show a high degree of homology with those of echicetin, botrocetin, alboaggregin-B and factor IX/factor X-binding protein. These results suggest that flavocetins may be a useful tool for further investigation of the GPIb-vWF interaction.

AB - Two high molecular mass proteins, flavocetin-A and flavocetin-B, were purified from Trimeresurus flavoviridis venom. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the apparent molecular mass of flavocetin-A and -B were 149 and 139 kDa, respectively, under nonreducing conditions. On reduction, flavocetin-A showed two distinct subunits (17 and 14 kDa), and flavocetin-B three distinct subunits (17, 15 and 14 kDa). At 1 μg/ml, flavocetin-A and -B (flavocetins) inhibited the von Willebrand factor (vWF)-dependent aggregation of fixed human platelets. However, flavocetins (10 μg/ml) had no effect on ADP- and collagen-induced platelet aggregation in PRP. Flavocetins (3 μg/ml) also inhibited shear-induced platelet aggregation at high shear stress. Furthermore, flavocetin-A completely inhibited the aggregation of and ATP release from washed platelets stimulated with a low concentration of thrombin. Flavocetin-A specifically bound to platelet with high affinity (Kd = 0.35 ± 0.13 nM) at 21 500 ± 1760 binding sites per platelet. The N-terminal amino acid sequences of the subunits of flavocetin-A show a high degree of homology with those of echicetin, botrocetin, alboaggregin-B and factor IX/factor X-binding protein. These results suggest that flavocetins may be a useful tool for further investigation of the GPIb-vWF interaction.

KW - (Snake venom)

KW - Flavocetin-A and -B

KW - Glycoprotein Ib

KW - Platelet aggregation

KW - Shear stress

KW - Von Willebrand factor

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U2 - 10.1016/0304-4165(95)00052-D

DO - 10.1016/0304-4165(95)00052-D

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C2 - 7599152

AN - SCOPUS:0028998182

VL - 1244

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EP - 338

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

SN - 0006-3002

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