Differences in the fractional abundances of carbohydrates of natural and recombinant human tissue factor
BACKGROUND: Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf...
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| Published in | Biochimica et biophysica acta Vol. 1810; no. 4; pp. 398 - 405 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier B.V
01.04.2011
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| Abstract | BACKGROUND: Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf9 insect cells is different (Krudysz-Amblo, J. et al (2010) J. Biol. Chem. 285, 3371–3382). METHODS: In this study, using mass spectrometry, we show by quantitative analysis that the extent of glycosylation varies on each protein. RESULTS AND CONCLUSIONS: Fractional abundance of each glycan composition at each of the three glycosylation sites reveals the most pronounced difference to be at asparagine (Asn) 11. This residue is located in the region of extensive TF-factor VIIa (FVIIa) interaction. Carbohydrate fractional abundance at Asn11 revealed that glycosylation in the natural placental TF is much more prevalent (~76%) than in the recombinant protein (~20%). The extent of glycosylation on Asn124 and Asn137 is similar in the two proteins, despite the pronounced differences in the carbohydrate composition. Additionally, 77% of rTF exists as TF des-1, 2 (missing the first two amino acids from the N-terminus). In contrast, only 31% of pTF is found in the des-1, 2 form. CONCLUSION: These observations may attribute to the difference in the ability of TF–FVIIa complex to activate factor X (FX). GENERAL SIGNIFICANCE: Structural and functional comparison of the recombinant and natural protein advances our understanding and knowledge on the biological activity of TF. |
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| AbstractList | Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf9 insect cells is different (Krudysz-Amblo, J. et al (2010) J. Biol. Chem. 285, 3371-3382).
In this study, using mass spectrometry, we show by quantitative analysis that the extent of glycosylation varies on each protein.
Fractional abundance of each glycan composition at each of the three glycosylation sites reveals the most pronounced difference to be at asparagine (Asn) 11. This residue is located in the region of extensive TF-factor VIIa (FVIIa) interaction. Carbohydrate fractional abundance at Asn11 revealed that glycosylation in the natural placental TF is much more prevalent (~76%) than in the recombinant protein (~20%). The extent of glycosylation on Asn124 and Asn137 is similar in the two proteins, despite the pronounced differences in the carbohydrate composition. Additionally, 77% of rTF exists as TF des-1, 2 (missing the first two amino acids from the N-terminus). In contrast, only 31% of pTF is found in the des-1, 2 form.
These observations may attribute to the difference in the ability of TF-FVIIa complex to activate factor X (FX).
Structural and functional comparison of the recombinant and natural protein advances our understanding and knowledge on the biological activity of TF. BACKGROUND: Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf9 insect cells is different (Krudysz-Amblo, J. et al (2010) J. Biol. Chem. 285, 3371–3382). METHODS: In this study, using mass spectrometry, we show by quantitative analysis that the extent of glycosylation varies on each protein. RESULTS AND CONCLUSIONS: Fractional abundance of each glycan composition at each of the three glycosylation sites reveals the most pronounced difference to be at asparagine (Asn) 11. This residue is located in the region of extensive TF-factor VIIa (FVIIa) interaction. Carbohydrate fractional abundance at Asn11 revealed that glycosylation in the natural placental TF is much more prevalent (~76%) than in the recombinant protein (~20%). The extent of glycosylation on Asn124 and Asn137 is similar in the two proteins, despite the pronounced differences in the carbohydrate composition. Additionally, 77% of rTF exists as TF des-1, 2 (missing the first two amino acids from the N-terminus). In contrast, only 31% of pTF is found in the des-1, 2 form. CONCLUSION: These observations may attribute to the difference in the ability of TF–FVIIa complex to activate factor X (FX). GENERAL SIGNIFICANCE: Structural and functional comparison of the recombinant and natural protein advances our understanding and knowledge on the biological activity of TF. Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf9 insect cells is different (Krudysz-Amblo, J. et al (2010) J. Biol. Chem. 285, 3371-3382).BACKGROUNDTissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of blood coagulation. Previously we have shown that the activity of the natural placental TF (pTF) and the recombinant TF (rTF) from Sf9 insect cells is different (Krudysz-Amblo, J. et al (2010) J. Biol. Chem. 285, 3371-3382).In this study, using mass spectrometry, we show by quantitative analysis that the extent of glycosylation varies on each protein.METHODSIn this study, using mass spectrometry, we show by quantitative analysis that the extent of glycosylation varies on each protein.Fractional abundance of each glycan composition at each of the three glycosylation sites reveals the most pronounced difference to be at asparagine (Asn) 11. This residue is located in the region of extensive TF-factor VIIa (FVIIa) interaction. Carbohydrate fractional abundance at Asn11 revealed that glycosylation in the natural placental TF is much more prevalent (~76%) than in the recombinant protein (~20%). The extent of glycosylation on Asn124 and Asn137 is similar in the two proteins, despite the pronounced differences in the carbohydrate composition. Additionally, 77% of rTF exists as TF des-1, 2 (missing the first two amino acids from the N-terminus). In contrast, only 31% of pTF is found in the des-1, 2 form.RESULTS AND CONCLUSIONSFractional abundance of each glycan composition at each of the three glycosylation sites reveals the most pronounced difference to be at asparagine (Asn) 11. This residue is located in the region of extensive TF-factor VIIa (FVIIa) interaction. Carbohydrate fractional abundance at Asn11 revealed that glycosylation in the natural placental TF is much more prevalent (~76%) than in the recombinant protein (~20%). The extent of glycosylation on Asn124 and Asn137 is similar in the two proteins, despite the pronounced differences in the carbohydrate composition. Additionally, 77% of rTF exists as TF des-1, 2 (missing the first two amino acids from the N-terminus). In contrast, only 31% of pTF is found in the des-1, 2 form.These observations may attribute to the difference in the ability of TF-FVIIa complex to activate factor X (FX).CONCLUSIONThese observations may attribute to the difference in the ability of TF-FVIIa complex to activate factor X (FX).Structural and functional comparison of the recombinant and natural protein advances our understanding and knowledge on the biological activity of TF.GENERAL SIGNIFICANCEStructural and functional comparison of the recombinant and natural protein advances our understanding and knowledge on the biological activity of TF. |
| Author | Krudysz-Amblo, Jolanta Jennings, Mark E., II Matthews, Dwight E Mann, Kenneth G Butenas, Saulius |
| AuthorAffiliation | Department of Chemistry, University of Vermont, Burlington, Vermont 05405, USA Department of Medicine-Cardiology, University of Vermont, Burlington, Vermont 05405, USA Department of Biochemistry, University of Vermont, Burlington, Vermont 05405, USA |
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| Author_xml | – sequence: 1 fullname: Krudysz-Amblo, Jolanta – sequence: 2 fullname: Jennings, Mark E., II – sequence: 3 fullname: Matthews, Dwight E – sequence: 4 fullname: Mann, Kenneth G – sequence: 5 fullname: Butenas, Saulius |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21172408$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1111_jth_12003 crossref_primary_10_1016_j_thromres_2012_02_018 crossref_primary_10_1111_j_1538_7836_2011_04404_x crossref_primary_10_1021_acs_analchem_0c04292 crossref_primary_10_1182_blood_2012_10_415000 crossref_primary_10_1080_09537104_2019_1624708 crossref_primary_10_6064_2012_964862 |
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| Snippet | BACKGROUND: Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the... Tissue factor (TF) is a single polypeptide integral membrane glycoprotein composed of 263 residues and is essential to life in its role as the initiator of... |
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| SubjectTerms | Animals asparagine bioactive properties blood coagulation carbohydrate composition carbohydrates Carbohydrates - analysis Cell Line Glycosylation Humans Insecta - cytology insects Mass Spectrometry membrane glycoproteins polypeptides quantitative analysis recombinant proteins Recombinant Proteins - chemistry Thromboplastin - chemistry |
| Title | Differences in the fractional abundances of carbohydrates of natural and recombinant human tissue factor |
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