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Biochemical changes in the equine capsule following prostaglandin‐induced pregnancy failure
Author(s) -
Chu J.W.K.,
Sharom F.J.,
Oriol J.G.,
Betteridge K.J.,
Cleaver B.D.,
Sharp D.C.
Publication year - 1997
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/(sici)1098-2795(199703)46:3<286::aid-mrd7>3.0.co;2-l
Subject(s) - conceptus , biology , sialic acid , andrology , trypsin , embryo , prostaglandin , medicine , endocrinology , pregnancy , biochemistry , fetus , microbiology and biotechnology , genetics , enzyme
The equine embryonic capsule, an acellular covering that envelops the conceptus during the second and third weeks of pregnancy, is composed of mucin‐like glycoproteins. Its structure is consistent with a dual role during early pregnancy: protection of the conceptus, and communication between the embryo and the mother. Loss of sialic acid from the capsular glycoproteins at day 16 correlates with the time of “fixation,” or loss of conceptus mobility throughout the uterine horns. This study investigated how the structure of the capsule is linked to the maintenance of pregnancy. Six pregnancies, confirmed by ultrasound, were terminated by prostaglandin injection on day 14, prior to the time of embryo fixation. These “defective” conceptuses were collected at day 17, and the structure and molecular properties of their capsules were compared to those of day 17 conceptuses collected from 5 normal pregnancies. Defective capsules were not significantly different from normal capsules in terms of dry weight, amino acid composition, and content of neutral and amino sugars. However, defective capsules failed to show the loss of sialic acid normally occurring around the time of embryo fixation. Analysis of the capsular mucins following trypsin digestion was carried out by radioactive labeling with 3 H on sialyl‐oligosaccharides and 125 I on tyrosine residues, followed by fast protein liquid chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Differences in the trypsin fragmentation patterns indicated increased susceptibility of the defective capsules to proteolysis. We conclude that there is a temporal association between desialylation of the equine capsule and embryonic survival, and that failure to desialylate alters the properties of the capsule. Mol. Reprod. Dev. 46:286–295, 1997. © 1997 Wiley‐Liss, Inc.