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2. CHARACTERIZATION OF THE GENE ENCODING MOUSE PLATELET GLYCOPROTEIN Ibβ 1 1The nucleotide sequence data reported in this paper will appear in the DDBJ, EMBL and GenBank nucleotide sequence databases with the accession number AB001419

Author

Yasuo Ikeda, Hironobu Anbo, Takanori Moriki, Mitsuru Murata, and Tetsuya Kitaguchi

Subjects
chemistry.chemical_classification, Glycosylation, Protein subunit, Nucleic acid sequence, Sequence alignment, Hematology, Biology, Platelet membrane glycoprotein, Molecular biology, Amino acid, chemistry.chemical_compound, chemistry, Glycoprotein, Peptide sequence
Abstract

Platelet glycoprotein (GP) Ib/IX/V complex is a major receptor for von Willebrand factor (vWF), which mediates platelet adhesion and aggregation under high shear stress conditions. It is composed of GPIbα, GPIbβ, GPIX, and GPV. All subunits for the human receptor have been cloned and characterized. However, the function of GPIbβ is still elusive. To obtain further information of GPIbβ, we have determined the genomic sequence of mouse GPIbβ (1466 bp). The deduced amino acid sequence (206aa) was 88% identical to the human GPIbβ protein. All cysteine residues, putative N-linked glycosylation site (Asn41), and putative phosphorylation site (Ser166) were conserved. The promoter region contained putative GATA and ets binding motif implicated in megakaryocytic expression. Mouse GPIbβ also contained a leucine-rich glycoprotein (LRG) sequence of 24 amino acids same as human GPIbβ. © 1997 Elsevier Science Ltd

Published
1997
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6. CHARACTERIZATION OF THE GENE ENCODING MOUSE PLATELET GLYCOPROTEIN Ibβ11The nucleotide sequence data reported in this paper will appear in the DDBJ, EMBL and GenBank nucleotide sequence databases with the accession number AB001419.

Author

Kitaguchi, Tetsuya, Murata, Mitsuru, Anbo, Hironobu, Moriki, Takanori, and Ikeda, Yasuo

Abstract

Platelet glycoprotein (GP) Ib/IX/V complex is a major receptor for von Willebrand factor (vWF), which mediates platelet adhesion and aggregation under high shear stress conditions. It is composed of GPIbα, GPIbβ, GPIX, and GPV. All subunits for the human receptor have been cloned and characterized. However, the function of GPIbβ is still elusive. To obtain further information of GPIbβ, we have determined the genomic sequence of mouse GPIbβ (1466 bp). The deduced amino acid sequence (206aa) was 88% identical to the human GPIbβ protein. All cysteine residues, putative N-linked glycosylation site (Asn41), and putative phosphorylation site (Ser166) were conserved. The promoter region contained putative GATA and etsbinding motif implicated in megakaryocytic expression. Mouse GPIbβ also contained a leucine-rich glycoprotein (LRG) sequence of 24 amino acids same as human GPIbβ. © 1997 Elsevier Science Ltd

Published
1997
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25. Hypercoagulation screening as an innovative tool for risk assessment, early diagnosis and prognosis in cancer: the HYPERCAN study

Author

Falanga, Anna, Barcella, Luca, Brevi, Shenaz, Gamba, Sara, Giaccherini, Cinzia, Marchetti, Marina, Milesi, Viola, Piras, Francesca, Rio, Francesca, Russo, Laura, Tartari, Carmen J., Tessarolo, Serena, Verzeroli, Cristina, Vignoli, Alfonso, Iacoviello, Licia, Donati, Maria Benedetta, Santoro, Armando, Masci, Giovanna, Nardozza, Angelo, Labianca, Roberto, Tondini, Carlo, Mandalà, Mario, Merelli, Barbara, De Braud, Filippo, Celio, Luigi, Martinetti, Antonia, Gasparini, Giampietro, De Maria, Ilaria, Meoni, Guido, Minelli, Mauro, Sarmiento, Roberta, Tarantini, Paola, D’Alessio, Andrea, Oliva, Nadia, Barni, Sandro, Ghilardi, Mara, Malighetti, Paolo, Spinelli, Daniele, and Sampietro, Giuseppe

Published
2016
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35. Standard measurement of clot-bound thrombin by using a chromogenic substrate for thrombin

Author

Meddahi, Sadia, Bara, Lucienne, Fessi, Hatem, and Samama, Meyer Michel

Subjects
*CHROMOGENIC compounds, *INDICATORS & test-papers, *THROMBIN, *BLOOD coagulation factors
Abstract

We have developed an in vitro protocol for the measurement of clot-bound thrombin. This protocol uses a chromogenic substrate for thrombin and a microtiter plate reader and is suitable for screening inhibitors for thrombin that are directed to clot-bound thrombin. Clots were obtained after recalcification of human plasma. For the measurement of clot-bound thrombin, we read the optical density (OD) at 405 nm on a spectrophotometer and compared the results to that obtained with a standard curve of human alpha thrombin. We stopped the amidolytic reaction at 10 min because the optical density was linear until 20 min under our experimental conditions. We suggest that clot-bound thrombin can be measured using a chromogenic substrate specific for thrombin under our experimental condition. [Copyright &y& Elsevier]

Published
2004
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