Synthesis and Processing of Ovine Trophoblast Protein-1 and Bovine Trophoblast Protein-1, Conceptus Secretory Proteins Involved in the Maternal Recognition of Pregnancy*
- 1 September 1988
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 123 (3) , 1274-1280
- https://doi.org/10.1210/endo-123-3-1274
Abstract
Ovine and bovine trophoblast protein-1 (oTP-1 and bTP-1) are newly discovered proteins produced by embryonic tissues for a limited period in early gestation. They appear to act as agents that prevent regression of the corpus luteum during early pregnancy in the ewe and cow. Ovine TP-1 [mol wt (Mr), 17,000] consists of three or four isoelectric variants (pi 5.4–5.7), whereas bTP-1, which cross-reacts with antiserum to oTP-1, is found as two predominant Mr classes (Mr, 22,000 and 24,000), each with several isoelectric variants (in the pi range 6.3–6.8). Cell-free translation of ovine conceptus mRNA yields pre-oTP-1 of 21,000 Mr which is processed to a 17,000 Mr form in the presence of canine pancreatic microsomes. However, preoTP- 1 also consists of three or four isoelectric variants, assumed to have arisen by translation of multiple mRNA species. Ovine TP-1 is not glycosylated. When bovine conceptus mRNA is translated, a group of four or five isoforms of pre-bTP-1 are generated, each with a Mr of 19,000. In the presence of microsomes the Mr shifts upward to about 21,500. Bovine conceptuses cultured in presence of either [3H]glucosamine or [3H]mannose incorporate label into both size classes of bTP-1 (Mr, 22,000 and 24,000). Culture in presence of [35S]methionine and tunicamycin gave rise to a nonglycosylated form of bTP-1 with an apparent Mr of 18,000. Treatment of [35S]methionine-labeled bTP-1 with either endoglycosidase-H or peptide:N-glycosidase F yielded products with Mr of 17,000 and 16,000, respectively. bTP-1, although functionally and structurally related to oTP-1, appears to be a glycoprotein carrying at least two Asn-linked oligosaccharides. The two Mr classes of bTP-1 arise as a result of differences in either the number or structure of the carbohydrate chains. Like oTP-1, bTP-1 is probably translated from multiple mRNA species. (Endocrinology123: 1274–1280,1988)Keywords
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