Amniotic fluid proteins: Maternal and fetal contributions

Johnson, A. Myron; Umansky, Irving; Alper, Chester A.; Everett, Catherine; Greenspan, Gary

doi:10.1016/s0022-3476(74)80687-6

Cited by 51 publications

(13 citation statements)

References 34 publications

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“…These results are consistent with those of previous studies that have also indicated a maternal origin for the plasma proteins in the amniotic fluid of late pregnancy (5,10,11). a,-Antichymotrypsin was observed to be present in some amniotic fluids at higher con centrations than would be expected for a pro tein of its size if it passed from the maternal blood by filtration alone.…”

Section: Discussionsupporting

confidence: 92%

“…The contribu tion from each source varies during gestation but in the last trimester most of the proteins are derived from maternal plasma (10). The evidence for this has come from studies of protein phenotypes (3,5,11), fetal protein deficiencies (4,12) and measurements of am niotic fluid/serum concentration ratios (2,5). The latter work has shown that the concentra tions of proteins in amniotic fluid are depen dent on their molecular sizes.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Origin of Plasma Proteins in Human Amniotic Fluid: the Significance of Alpha<sub>1</sub>-Antichymotrypsin Complexes

Burnett

Bradwell²

1980

Neonatology

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12 proteins were studied in serum and amniotic fluid from 20 women in late pregnancy by two-dimensional immunoelectrophoresis. A close inverse relationship was observed between the amniotic fluid/serum concentration ratios of 11 proteins and their Stokes radii. These proteins enter the liquor from the maternal blood by molecular filtration. The concentration of Α₁-antichymotrypsin in amniotic fluid was often higher than expected and the protein was often partially complexed. Α₁-Antichymotrypsin is probably not actively secreted into amniotic fluid but may be selectively retained after complexing.

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

The Origin of Plasma Proteins in Human Amniotic Fluid: the Significance of Alpha<sub>1</sub>-Antichymotrypsin Complexes

Burnett

Bradwell²

1980

Neonatology

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“…The inability of the AFP contained within native MAF to induce uterine desensitization (Table 1, line J) suggests the presence in MAF of a substance that interferes with this action. Such a substance might be an adult material contained in those maternal serum components which gain access to amniotic fluid (27). This hypothesis is supported by the complete elimination of the inhibitory activity of purified AFP when adult mouse serum is added to the AFP/E2 incubate (unpublished data).…”

Section: Discussionmentioning

confidence: 84%

Estradiol-activated alpha-fetoprotein suppresses the uterotropic response to estrogens.

Mizejewski¹,

Vonnegut²,

Jacobson³

1983

Proc. Natl. Acad. Sci. U.S.A.

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The binding of estrogen to a-fetoprotein (AFP) in the plasma cannot account for the impaired estrogen response seen in immature rodents because estradiol (E2) doses that far exceed the total body burden of AFP will stimulate only modest uterine growth. We investigated this phenomenon in immature female mice by determining their uterine weights 23 hr after intraperitoneal injection of estrogens or AFP or both. Administration of either 0.5 gg of E2 or 10 ng of moxestrol (MOX) approximately doubled the uterine weight. Giving 1 pg of AFP 1 hr before injection of either estrogen did not alter thatresponse. Combining the E2 and AFP just prior to injection resulted in decreased uterine growth (34% inhibition). Preincubating the estrogens with purified AFP (0.1-50 jug) did not affect the growth response to moxestrol but markedly decreased the response to E2. This was not due to sequestering of hormone because maximal reduction of the E2 response (ca. 65% inhibition) required only 1.0 jug of AFP(AFP/ E2 molar ratio, 1:130), and higher AFP doses inhibited less. About 40% of the growth elicited by injection of either 0.5 jig of E2 or 10 ng of MOX was inhibited when these doses were preceded by injection of the preincubated AFP/E2 mixture but not when preceded by either of the components. In each experiment, the mitotic index of luminal epithelium was affected to the same degree as uterine weight. AFP and E2 incubated for 1 hr thus produce a potent inhibitor of estrogen-stimulated mitotic activity and growth. This inhibitor might act upon estrogen-responsive cells at specific sites at which competition by an inactive component of AFP can block the process.The estrogen contained in the amniotic fluid of pregnant rats and mice is largely protein-bound. The binding component that imparts that property is a-fetoprotein (AFP) which constitutes about one-third of the total protein present in rodent amniotic fluid. In fetal and newborn rodents the plasma contains this protein in high concentrations (3-5 mg/ml) which persist for a few days post partum. The concentration then declines rapidly over the next 3 weeks of life and, in most rodent strains, attains the low levels common to adults after the fifth week (1).Rodent AFP molecules bear sites that bind the ovarian estrogens with high affinity and specificity (2, 3). These properties would ensure that, in animals given submicrogram doses of estradiol (E2), even up to 15 days of age, the concentration of unbound hormone in the circulation that would be available for interaction with target cells is small. This argument has been advanced to account for the apparent insensitivity to E2 exhibited by those immature rodent organs which in the adult are quite sensitive to estrogen (4). However, this assertion seems flawed in that the uterotropic response to administered estrogen in immature rodents is impaired even when the estrogen doses are well in excess of the total body burden of AFP.At the developmental state of the immature rodent, high plasma.AFP levels and insensitivity...

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“…Most of the proteins present in amniotic fluid are serum proteins, probably of maternal origin (Drohse et al, 1998). It has been estimated that only 5% of the total protein content is likely to be of decidual or fetal origin (Johnson et al, 1974). Our results demonstrated that the shed ectodomain of collagen XVII present in amniotic fluid originates from the epithelial cells of amniotic membrane as well as amniotic fluid cells.…”

Section: Discussionmentioning

confidence: 55%

Pemphigoid gestationis autoantigen, transmembrane collagen XVII, promotes the migration of cytotrophoblastic cells of placenta and is a structural component of fetal membranes

et al. 2008

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Amniotic fluid proteins: Maternal and fetal contributions

Cited by 51 publications

References 34 publications

The Origin of Plasma Proteins in Human Amniotic Fluid: the Significance of Alpha<sub>1</sub>-Antichymotrypsin Complexes

The Origin of Plasma Proteins in Human Amniotic Fluid: the Significance of Alpha<sub>1</sub>-Antichymotrypsin Complexes

Estradiol-activated alpha-fetoprotein suppresses the uterotropic response to estrogens.

Pemphigoid gestationis autoantigen, transmembrane collagen XVII, promotes the migration of cytotrophoblastic cells of placenta and is a structural component of fetal membranes

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