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Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A

It has been reported that the immune response due to α-Gal epitopes is an important factor in tissue valve failure. The elimination of the interaction between the natural anti-Gal antibodies and α-gal epitopes on the xenografts is a prerequisite to the success of xenografts in humans. Previously, we...

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Autores principales: Park, Seongsik, Kim, Woong-Han, Choi, Sun-Young, Kim, Yong-Jin
Formato: Texto
Lenguaje:English
Publicado: The Korean Academy of Medical Sciences 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775862/
https://www.ncbi.nlm.nih.gov/pubmed/19949670
http://dx.doi.org/10.3346/jkms.2009.24.6.1126
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author Park, Seongsik
Kim, Woong-Han
Choi, Sun-Young
Kim, Yong-Jin
author_facet Park, Seongsik
Kim, Woong-Han
Choi, Sun-Young
Kim, Yong-Jin
author_sort Park, Seongsik
collection PubMed
description It has been reported that the immune response due to α-Gal epitopes is an important factor in tissue valve failure. The elimination of the interaction between the natural anti-Gal antibodies and α-gal epitopes on the xenografts is a prerequisite to the success of xenografts in humans. Previously, we reported that the green coffee bean α-galactosidase could remove all α-Gal epitopes from cell surface of porcine aortic valve and pericardial tissue, but it has limitations on cost effectiveness. In this study we wanted to know whether the recently produced recombinant human α-galactosidase A has the same effective enzymatic activity as green coffee bean α-galactosidase in removing α-Gal epitopes from the same tissues. After treating fresh porcine aortic valve and pericardial tissue with recombinant α-galactosidase A, each sample was stained with Griffonia simplicifolia type I isolectin B4 indirect immunoperoxidase avidin-biotin technique. We then examined whether the α-Gal epitopes were reduced or abolished in each consecutive concentration of recombinant α-galactosidase A by comparing the degree of the Griffonia simplicifolia isolectin B4 staining. As a result, the recombinant α-galactosidase A could remove cell surface α-Gals on porcine aortic valve and pericardial tissue as effectively as green coffee bean α-galactosidase.
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spelling pubmed-27758622009-12-01 Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A Park, Seongsik Kim, Woong-Han Choi, Sun-Young Kim, Yong-Jin J Korean Med Sci Original Article It has been reported that the immune response due to α-Gal epitopes is an important factor in tissue valve failure. The elimination of the interaction between the natural anti-Gal antibodies and α-gal epitopes on the xenografts is a prerequisite to the success of xenografts in humans. Previously, we reported that the green coffee bean α-galactosidase could remove all α-Gal epitopes from cell surface of porcine aortic valve and pericardial tissue, but it has limitations on cost effectiveness. In this study we wanted to know whether the recently produced recombinant human α-galactosidase A has the same effective enzymatic activity as green coffee bean α-galactosidase in removing α-Gal epitopes from the same tissues. After treating fresh porcine aortic valve and pericardial tissue with recombinant α-galactosidase A, each sample was stained with Griffonia simplicifolia type I isolectin B4 indirect immunoperoxidase avidin-biotin technique. We then examined whether the α-Gal epitopes were reduced or abolished in each consecutive concentration of recombinant α-galactosidase A by comparing the degree of the Griffonia simplicifolia isolectin B4 staining. As a result, the recombinant α-galactosidase A could remove cell surface α-Gals on porcine aortic valve and pericardial tissue as effectively as green coffee bean α-galactosidase. The Korean Academy of Medical Sciences 2009-12 2009-11-09 /pmc/articles/PMC2775862/ /pubmed/19949670 http://dx.doi.org/10.3346/jkms.2009.24.6.1126 Text en Copyright © 2009 The Korean Academy of Medical Sciences http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Park, Seongsik
Kim, Woong-Han
Choi, Sun-Young
Kim, Yong-Jin
Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A
title Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A
title_full Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A
title_fullStr Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A
title_full_unstemmed Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A
title_short Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A
title_sort removal of alpha-gal epitopes from porcine aortic valve and pericardium using recombinant human alpha galactosidase a
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2775862/
https://www.ncbi.nlm.nih.gov/pubmed/19949670
http://dx.doi.org/10.3346/jkms.2009.24.6.1126
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