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The amino acid sequences of the amino-terminal of the two different polypeptide chains of the human decidua-associated protein hDP200, with apparent molecular masses of 55 and 25 kDa, were determined. The amino-terminal sequence of the 55 kDa chain revealed that it is an immunoglobulin heavy chain, of the VH–III subgroup and the amino-terminal sequence of the 25 kDa chain showed that it is a human kappa V–III light chain. The sequence data indicate that hDP200 is an immunoglobulin. The ability of the hDP200 molecules to form high molecular weight complexes with immunoglobulins of other classes suggest that hDP200 is a rheumatoid factor.
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Summary. A crude extract of pooled early-pregnancy decidual tissue was enriched for soluble decidual proteins by exhaustive affinity absorption with antibodies to human serum proteins immobilized on Eupergit C. The partly purified extract was used to prepare monoclonal antibodies. A monoclonal antibody was obtained recognizing an antigen present in extract of decidual tissue and not in extract of proliferative endometrium. The monoclonal antibody was used for immunoaffinity purification of the decidua-associated protein. By SDS-PAGE analysis, under reducing conditions it yielded 2 bands at apparent molecular weights of 55 000 and 25 000. Under non-reducing conditions a single protein band at apparent molecular weight of 200 000 was observed. The M r 200 000 protein was named hDP200 and the M r 55 000 protein was named hDP55. It is suggested that hDP55 is a subunit of the hDP200. The hDP200 did not react with polyclonal antibodies specific for PP12 and PP14. PP14 has been shown to be immunologically indistinguishable from PEP and α2-PEG. Our data therefore suggest that hDP200 is a novel human decidua-associated protein.
Keywords: monoclonal antibody; decidua-associated secretory protein; man
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The possibility of using the rat as an experimental model for the further research of human decidua-associated protein (hDP) 200 was examined. A rat protein similar to the hDP 200 was identified and immunoaffinity purified, using a monoclonal antibody recognizing hDP 200. The protein was named rat decidua-associated protein (rDP) 200. The abundance of rDP 200 in endometrial tissue extracts and in uterine washings was measured throughout the oestrous cycle and on consecutive days, starting the day after the rats mated until the day after the blastocyst implantation. The results indicate that the highest concentration of rDP 200 in uterine washings may be related to oestrogen control and probably to the implantation process. Further studies are needed to confirm these findings.
