Abstract

Using rabbit as a model, the roles of uteroglobin (UG) and transglutaminase (TG) in masking the antigenicity of early developing mammalian embryo have been investigated. Maternal lymphocytes in vitro, when mixed with mitomycin-C inactivated blastomeres, incorporated H3-thymidine, suggesting recognition of embryonic antigens by these cells. However, pretreatment of blastomeres with pregnant uterine fluid (PUF) or with UG alone or in combination with TG (coagulation factor XIIIa), resulted in a significant and dose-dependent suppression of H3-thymidine incorporation into these lymphocytes. A complete suppression was achieved at a concentration of 250 micrograms of UG/ml, in the absence of TG. However, in the presence of TG, only 1.0 micrograms of UG/ml was required for total suppression. Neither nonpregnant uterine fluid (NPUF), nor myoglobin, a nonspecific protein similar in molecular weight to UG, had any suppressive effect. Incubation of uteroglobin with anti-UG or TG with its antiserum prior to the pretreatment of blastomeres eliminated the suppressive effect of these proteins. Inhibition of TG by neopentyl chloroethyl nitrosourea (NPCNU) also eliminated the suppressive effects of uteroglobin on H3-thymidine incorporation into maternal lymphocytes. These results suggest that in the pregnant uterus UG in conjunction with TG may play a specific role in masking the antigenicity of developing embryos during implantation.

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