|
TRANSGENIC APPROACHES FOR THE REDUCTION IN EXPRESSION OF GALalpha(1,3)GAL FOR XENOTRANSPLANTATION
Mauro S. Sandrin, Narin Osman, Ian F.C. McKenzie
Molecular Immunogenetics Laboratory, Austin Research Institute, Austin & Repatriation Medical Center, Heidelberg Vic. 3084, Australia
Received 12/31/96; Accepted 3/12/97; On-line 4/1/97
TABLE OF CONTENTS
- 1. Abstract
- 2. Introduction
- 3. Hyperacute rejection
- 4. The major xenoepitope: Galalpha(1,3)Gal
- 4.1 Carbohydrate inhibition
- 4.2 Absorption studies
- 4.3 Transfection studies
- 4.4 In vivo studies
- 4.5 Are all the human anti-pig antibodies directed to Galalpha(1,3)Gal?
- 4.6 Cellular and molecular distribution of Galalpha(1,3)Gal
- 5. alpha1,3Galactosyltransferase
- 6. Elimination of Galalpha(1,3)Gal by gene inactivation strategies
- 7. Elimination of Galalpha(1,3)Gal by transgenic strategies
- 7.1 The alpha1,2Fucosyltransferase enzyme
- 7.1.1. Expression in COS cells
- 7.1.2. Expression in porcine cells
- 7.1.3. Expression in transgenic mice
- 7.1.4 . Expression in transgenic pigs
- 7.1.5 Molecular mechanisms for suppression of Galalpha(1,3)Gal production
- 7.1.6 Secretor type alpha1,2fucosyltransferase
- 7.2. alphaGalactosidase
- 7.2.1 Expression of alphagalactosidase cDNA in COS cells
- 7.2.2 Expression of alphagalactosidase cDNA in a pig cell line
- 7.2.3 In vivo expression of alphagalactosidase
- 7.3 Combination of alpha1,2fucosyltransferase and alphagalactosidase
- 8. Conclusions
- 9. References
- 10. Entire manuscript
Key Words: xenotransplantation, Galalpha(1,3)Gal, transgenesis, glycosyltransferase.
Search OMIM (Online Mendelian Inheritance in Man) to find related articles
This form requires a WWW Client such as Netscape, XMosaic, Lynx that supports fill-in forms.
|
