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Results for “PLACENTAL EXTRACTS”

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At least 703 records · Page 39Linked to original sources
PubMed1979

Whole-blood fibrinolytic activity in normal and hypertensive pregnancies and its relation to the placental concentration of urokinase inhibitor.

Whole-blood fibrinolytic activity was measured in 68 pregnant and 29 nonpregnant women with a sensitive, solid-state assay in which 125I-labeled fibrin was bound to polystyrene tubes. Antepartum fibrinolytic activity in 36 normotensive gravid women [234.5 +/- 29.2 (mean +/- standard error of the mean) ng fibrin lysed/30 min] was significantly (p less than 0.001) greater than that found in 28 nonpregnant normotensive women not taking oral contraceptives (63.61 +/- 7.66 ng fibrin lysed/30 min) and not different from the activity observed during the active phase of labor (198.50 +/- 16.5 ng fibrin lysed/30 min.) Normotensive pregnant patients had a significant (p less than 0.001) increase in whole-blood fibrinolytic activity (341.04 +/- 25.7 ng fibrin lysed/30 min) within the first 24 hours after delivery which persisted in measurements taken the second postpartum day. Fibrinolytic activity values before labor, in the active phase of labor, and in the first and second postpartum days in 17 patients with mild to moderate pregnancy-induced or pregd or pregnancy-aggravated hypertension were not different from those found in the normotensive group. However, patients with severe pregnancy-induced or pregnancy-aggravated hypertension had significantly (p less than 0.01) lower levels of fibrinolytic activity than normotensive patients before labor, during the active phase of labor, and on the first and second postpartum days. The placental 800 X g and 110,000 X g fractions of patients with severe hypertension had a significantly (p less than 0.001) greater capacity to inhibit "in vitro" urokinase-induced fibrinolysis than similar fractions obtained from placentas of normotensive women, and there was a significant inverse correlation (r = 0.61; p less than 0.01) between whole-blood fibrinolytic activity and urokinase inhibition by placental fractions. Our findings indicate that contrary to widely held views, fibrinolysis is extremely active in term pregnancies and during labor and that a derangement of this activity is present in cases of severe pregnancy-induced or pregnancy-aggravated hypertension.

Adolescent↗
PubMed1992

Glycosylation of annexin I and annexin II.

Human placental annexin I and annexin II were shown to be glycosylated by one-dimensional affinity blotting with the lectin concanavalin A, which recognizes D-mannose and D-glucose residues. Further evidence that annexin I and annexin II are glycosylated was provided by the finding that these proteins incorporated D-[2,6-3H]mannose and D-[6-3H]glucose when they were biosynthesized by the human squamous carcinoma cell line SqCC/Y1. Annexin I and annexin II could be rapidly purified from a human placental membrane extract by concanavalin A-Sepharose, which indicated that these proteins contain two biantennary mannosyl residues.

Annexin A1↗
PubMed1994

Effect of tumour promoting agents on protein phosphorylation in human placenta.

1. The effects of okadaic acid (OA) and phorbol-12-myristate-13-acetate (PMA) on protein phosphorylation were studied in human term placentas. 2. When samples treated with tumour promoters were compared with untreated samples, the phosphorylation of a 135 kDa protein was significantly decreased; OA also produced a decrease in phosphorylation of a 24 kDa protein. 3. Both substances produced an alteration in the proportions of bands of masses 170, 65 and 24 kDa, relative to total phosphorylation; PMA treatment also affected the band of mass 135 kDa. 4. Placental cell extracts were also subjected to Western blotting with a protein kinase C (PKC) antibody, reportedly specific for the alpha- and beta-isoforms. 5. Two immunoreactive proteins were detected; an 80 kDa band, presumably corresponding to the alpha- or beta-PKC, and a 64 kDa protein, which could be a degradation production of the 80 kDa protein or it could correspond to another form of the enzyme. The expression of PKC did not change on treatment with PMA.

Autoradiography↗
PubMed1983

Human placental steroid sulfatase: purification and properties.

Steroid sulfatase is recovered quantitatively from the 105,000 g h supernatant of human placental microsomes extracted with Triton X-100. The solubilized enzyme has been purified using conventional techniques. Throughout the purification procedure, steroid sulfatase appears to be heterogeneous as evidenced by certain, but not all, criteria. Following polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the final preparation exhibits a major component and varying amounts of two minor ones. Antibodies raised in rabbits with the heterogeneous immunogen give rise to a single precipitation line when the native enzyme is analyzed by double immunodiffusion or by immunoelectrophoresis. In addition, using aged preparations of microsomes and immunoaffinity techniques, steroid sulfatase activity was found to be associated with the fastest migrating minor component. This finding would suggest that the apparent heterogeneity of purified steroid sulfatase is linked to degradation processes occurring within the microsomal preparations. Steroid sulfatase has a Stokes radius of 56 A, a sedimentation coefficient of 4.85 +/- 0.15S (in Triton-containing buffers) and binds 1.3 g of Triton X-100-per g of protein. The molecular weight of the Triton-protein complex was calculated to be 166,000 in which the glycoprotein portion contribution is about 43% (72,000). In contrast, the apparent molecular weight of the major polypeptide determined on calibrated SDS-gels is 62,000. The purified enzyme exhibits two pH optima with cholesterol sulfate as substrate, an acidic one at pH 5.0 and a second one at pH 7.5. The Km values for cholesterol sulfate, dehydroandrosterone sulfate and p-nitrophenylsulfate were 5.26, 14 and 1,320 microM, respectively.

Detergents↗
PubMed1988

Dose-dependent enhancement of morphine-induced analgesia by ingestion of amniotic fluid and placenta.

Ingestion of amniotic fluid and placenta by rats has been shown to enhance opioid-mediated analgesia. The present studies were designed to examine the effect of several doses and volumes of placenta and amniotic fluid on tail-flick latency in rats treated with 3 mg/kg morphine. The optimal dose of amniotic fluid was found to be 0.25 ml, although 0.50 and 1.0 ml also produced significant enhancement. Doses of 0.125 and 2 ml of amniotic fluid were ineffective, as was a dose of 0.25 ml diluted to 2 ml with saline. The optimal dose of placenta was found to be 1 placenta, although the resulting enhancement was not significantly greater than that produced by 025, 0.50, 2.0 or 4.0 placentas. Doses smaller than 0.25 placenta or larger than 4.0 placentas were ineffective. The most effective doses of amniotic fluid and placenta correspond to the amounts delivered with each pup during parturition.

Amniotic Fluid↗
PubMed1988

Modulation of cellular phorbol ester binding and/or protein kinase C activity by human placental fractions.

We describe two factors in human placenta that modulate the interaction of phorbol ester tumor promoters with cell membranes or with protein kinase C. One, phorbol ester binding inhibitory factor, can inhibit binding of [3H]phorbol-12,13-dibutyrate to cultured cells or to a membrane fraction but does not inhibit its binding to a homogeneous C kinase preparation (phorbol ester binding sites). The other, C kinase activating factor, stimulates C kinase activity in a calcium-dependent manner. We separated these two biochemical activities from a crude human placental fraction by gel filtration.

Animals↗
PubMed1988

Oral submucous fibrosis--a new treatment regimen.

Successful treatment of oral submucous fibrosis with local injections of chymotrypsin, hyaluronidase, and dexamethasone is reported. In resistant cases, surgical excision of the fibrotic bands with submucosal placement of fresh human placental grafts was found to be successful.

Chymotrypsin↗
PubMed2006

Differential release of plasminogen activator inhibitors (PAIs) during dual perfusion of human placenta: implications in preeclampsia.

Plasminogen activator inhibitors (PAIs) play critical roles in regulating cellular invasion and fibrinolysis. An increase in the ratio of PAI-1/PAI-2 in placenta and maternal serum is suggested to result in excessive intervillous fibrin deposition and placental infarction in pregnancies complicated by preeclampsia (PE) and intrauterine growth restriction (IUGR). In the current study we used dual (maternal and fetal) perfusion of human term placentas to examine the release of PAIs to the intervillous space. ELISA revealed a significant time-dependent increase in total PAI-1 levels in maternal perfusate (MP) between 1 and 7h of perfusion. Conversely, PAI-2 levels decreased resulting in a 3-fold increase in the PAI-1/PAI-2 ratio in MP. Levels of PAI-1, but not PAI-2, in placental tissue extracts increased during perfusion. In perfusions carried out with xanthine and xanthine oxidase (X + XO), compounds used to generate reactive oxygen species (ROS), no time-dependent increase in total PAI-1 levels was observed. In addition, X + XO treatment promoted a 3-fold reduction in active PAI-1 levels in MP, indicating that ROS decrease PAI-1 release to MP. The finding of a time-dependent change in patterns of PAI expression and response to ROS indicates the utility of dual perfusion as a model to dissect mechanism(s) promoting aberrant fibrinolysis in pregnancies complicated by PE and IUGR.

Adult↗
PubMed2000

Calumenin interacts with serum amyloid P component.

We recently reported the identification of human calumenin, a novel Ca(2+) binding, transformation-sensitive and secreted protein [Vorum et al. (1998) Biochim. Biophys. Acta 1386, 121-131; Vorum et al. (1999) Exp. Cell Res. 248, 473-481] belonging to the family of multiple EF-hand proteins of the secretory pathway that include reticulocalbin, ERC-55, Cab45 and crocalbin. In order to further investigate the extracellular functions of calumenin we immobilized the recombinant protein to a column. After application of a placental tissue extract we were able to elute one protein that interacts with calumenin in the presence of Ca(2+). Amino acid sequencing identified this protein as serum amyloid P component (SAP). Furthermore, we verified and characterized the calumenin-SAP interaction by the surface plasmon resonance technique. The findings indicate that calumenin may participate in the immunological defense system and could be involved in the pathological process of amyloidosis that leads to formation of amyloid deposits seen in different types of tissues.

Amino Acid Sequence↗