TY - JOUR
T1 - Galα(1,3)gal epitope in porcine small intestinal submucosa
AU - McPherson, T. B.
AU - Liang, H.
AU - Record, R. D.
AU - Badylak, Stephen F.
PY - 2000/6
Y1 - 2000/6
N2 - Small intestinal submucosa (SIS) is a naturally occurring, acellular biomaterial derived from porcine jejunum, which promotes constructive tissue remodeling when applied as a xenogeneic graft material. Galactosyl- α(l,3)galactose (Gal) is a cell-associated epitope responsible for hyperacute rejection of porcine whole-organ xenografts in primates. Because SIS is harvested from porcine tissue, it may contain the Gal epitope. The goals of this study were to determine if Gal is present in SIS and, if it is present, to determine if human serum complement can be activated in vitro following exposure to porcine-derived SIS. SIS was probed for Gal by immunohistochemical methods and by lectin-peroxidase staining. SIS stained strongly positive with human serum, which contains naturally occurring antibodies to Gal, followed by anti-immunoglobulin G (IgG) or anti-IgM peroxidase conjugate. Blocking with the lectin I-B4, which is specific for the Gal epitope, decreased the intensity of staining. Exposure of SIS to α- galactosidase reduced staining to negligible amounts. The Gal epitope is distributed transmurally throughout the SIS material. Sub typing of the immunoglobulins that bind to SIS showed that IgG2 is the major immunoglobulin of human plasma that binds to SIS. SIS did not activate complement in vitro as measured by radioimmunoassay for C3a.
AB - Small intestinal submucosa (SIS) is a naturally occurring, acellular biomaterial derived from porcine jejunum, which promotes constructive tissue remodeling when applied as a xenogeneic graft material. Galactosyl- α(l,3)galactose (Gal) is a cell-associated epitope responsible for hyperacute rejection of porcine whole-organ xenografts in primates. Because SIS is harvested from porcine tissue, it may contain the Gal epitope. The goals of this study were to determine if Gal is present in SIS and, if it is present, to determine if human serum complement can be activated in vitro following exposure to porcine-derived SIS. SIS was probed for Gal by immunohistochemical methods and by lectin-peroxidase staining. SIS stained strongly positive with human serum, which contains naturally occurring antibodies to Gal, followed by anti-immunoglobulin G (IgG) or anti-IgM peroxidase conjugate. Blocking with the lectin I-B4, which is specific for the Gal epitope, decreased the intensity of staining. Exposure of SIS to α- galactosidase reduced staining to negligible amounts. The Gal epitope is distributed transmurally throughout the SIS material. Sub typing of the immunoglobulins that bind to SIS showed that IgG2 is the major immunoglobulin of human plasma that binds to SIS. SIS did not activate complement in vitro as measured by radioimmunoassay for C3a.
UR - http://www.scopus.com/inward/record.url?scp=0033624687&partnerID=8YFLogxK
U2 - 10.1089/10763270050044416
DO - 10.1089/10763270050044416
M3 - Article
C2 - 10941218
AN - SCOPUS:0033624687
SN - 1076-3279
VL - 6
SP - 233
EP - 239
JO - Tissue Engineering
JF - Tissue Engineering
IS - 3
ER -