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Journal of reproduction and fertility1995; 105(1); 65-70; doi: 10.1530/jrf.0.1050065

A novel uterine protein that associates with the embryonic capsule in equids.

Abstract: An apparently unique protein produced in large quantities by the endometrium of the mare which adheres to, or is incorporated into, the acellular capsule that surrounds the equine conceptus in early pregnancy, has been characterized and partially sequenced. It has a molecular mass of approximately 18 kDa on SDS-PAGE gels and is nonglycosylated as assessed by a sensitive carbohydrate detection kit. Comparison of its first 24 amino-terminal amino acids with all entries in the databases failed to show any significant identity with any other protein sequence. Secretion of the protein appears to be progesterone dependent, as its presence in uterine flushings correlates with peripheral serum progesterone profiles during the oestrous cycle and its secretion can be induced in anoestrous mares by administration of a synthetic progestagen. However, in pregnant mares, the protein disappears from the uterus after about day 20 (term = 320-340 days), despite the persistence of high serum concentrations of progesterone, indicating that additional mechanisms control its synthesis and secretion. The strong association of the protein with the glycoprotein capsule that surrounds the equine blastocyst suggests that it may be incorporated into the capsule as the capsule expands from day 11 after ovulation. Alternatively, or additionally, it may be involved in the transport of nutrients or other substances through the capsule, and may therefore play an important role in the maintenance of pregnancy.
Publication Date: 1995-09-01 PubMed ID: 7490716DOI: 10.1530/jrf.0.1050065Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research discusses the identification of a new protein in the horse’s uterus that interacts with the embryonic capsule during the early stages of pregnancy. The protein is progesterone dependent, but stops being produced around day 20 of pregnancy, and may be crucial in pregnancy preservation.

Characterization of the Novel Protein

In this study, a unique protein was detected in enormous quantities in the mare’s endometrium— the innermost layer of the uterus. This protein appears to stick to, or become part of, the capsule devoid of cells that engulfs the equine conceptus during the early phase of pregnancy. It was scrutinized and sequenced in part. The protein had an estimated molecular weight of around 18 kDa when tested on SDS-PAGE gels. A sensitive carbohydrate detection kit revealed it was nonglycosylated.

  • The initial 24 amino-terminal amino acids of the protein were compared with all database entries. Researchers found no significant identity with any known protein sequence, suggesting this is a distinctly novel protein.
  • The protein’s secretive nature seems to rely on progesterone, as evidence of it correlated to peripheral serum progesterone profiles during the ovulation cycle.

The Role of the Protein in Pregnancy

The presence of the protein could be prompted in non-reproductive mares through the administration of synthetic progestagen, a man-made hormone similar to progesterone. Yet, despite ongoing high levels of progesterone in the serum, the protein leaves the uterus about day 20 into the mare’s gestation.

  • The disappearance of the protein suggests that its synthesis and secretion are governed by additional mechanisms, not solely the presence of progesterone.
  • The protein’s potent association with the glycoprotein capsule surrounding the equine blastocyst hints that it might integrate into the capsule when it expands on day 11 post-ovulation.

Potential Functions of the Protein

The protein not only could contribute to the structure of the embryonic capsule but might also have a role in sustaining pregnancy.

  • One possibility, among others, is that the protein helps in the transportation of nutrients or other substrates through the capsule. This transport role could be crucial for the success of the pregnancy.

Cite This Article

APA
Stewart F, Charleston B, Crossett B, Barker PJ, Allen WR. (1995). A novel uterine protein that associates with the embryonic capsule in equids. J Reprod Fertil, 105(1), 65-70. https://doi.org/10.1530/jrf.0.1050065

Publication

ISSN: 0022-4251
NlmUniqueID: 0376367
Country: England
Language: English
Volume: 105
Issue: 1
Pages: 65-70

Researcher Affiliations

Stewart, F
  • Thoroughbred Breeders' Association Equine Fertility Unit, Mertown Paddocks, Suffolk, UK.
Charleston, B
    Crossett, B
      Barker, P J
        Allen, W R

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Electrophoresis, Polyacrylamide Gel
          • Endometrium / chemistry
          • Endometrium / metabolism
          • Estrus / blood
          • Female
          • Gestational Age
          • Gonadotropins, Equine / chemistry
          • Gonadotropins, Equine / isolation & purification
          • Horses / metabolism
          • Molecular Sequence Data
          • Pregnancy
          • Pregnancy, Animal / metabolism
          • Progesterone / blood

          Citations

          This article has been cited 3 times.
          1. Almiñana C, Rudolf Vegas A, Tekin M, Hassan M, Uzbekov R, Fröhlich T, Bollwein H, Bauersachs S. Isolation and Characterization of Equine Uterine Extracellular Vesicles: A Comparative Methodological Study.. Int J Mol Sci 2021 Jan 19;22(2).
            doi: 10.3390/ijms22020979pubmed: 33478136google scholar: lookup
          2. Smits K, Willems S, Van Steendam K, Van De Velde M, De Lange V, Ververs C, Roels K, Govaere J, Van Nieuwerburgh F, Peelman L, Deforce D, Van Soom A. Proteins involved in embryo-maternal interaction around the signalling of maternal recognition of pregnancy in the horse.. Sci Rep 2018 Mar 27;8(1):5249.
            doi: 10.1038/s41598-018-23537-6pubmed: 29588480google scholar: lookup
          3. Crossett B, Allen WR, Stewart F. A 19 kDa protein secreted by the endometrium of the mare is a novel member of the lipocalin family.. Biochem J 1996 Nov 15;320 ( Pt 1)(Pt 1):137-43.
            doi: 10.1042/bj3200137pubmed: 8947478google scholar: lookup