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Biomedical subjects

R Koistinen

Publications and source records attributed to R Koistinen.

107 records · Page 6Linked to original sources
PubMed1984

Comparison of three methods for investigating placental protein 12(PP12)-like immunoreactive substance from preovulatory follicular fluid and purified PP12 from human placenta.

Placental protein 12(PP12)-like immunoreactive fraction of preovulatory follicular fluid from Sephadex G-100 and purified placental PP12 were subjected to reverse phase high performance liquid chromatography (HPLC). The elution was carried out with acetonitrile gradient. PP12-like immunoreactivity of both samples had the same retention time. This fraction of follicular fluid from HPLC and placental PP12 were then run on a sodium dodecyl sulfate-polyacrylamide gel and transferred electrophoretically to a nitrocellulose (NC) sheet. Protein bands on the NC sheet were then detected immunologically with anti-PP12 antisera. After visualising the bands which had reacted with antisera it was obvious that PP12-like immunoreactive substance from follicular fluid and from placenta had an electrophoretic mobility corresponding to the same molecular mass.

Body Fluids↗
PubMed1984

Hyperstimulated human preovulatory follicular fluid, luteinized cells of unruptured follicles, and corpus luteum contain pregnancy-associated plasma protein A (PAPP-A).

Radioimmunoassay, gel filtration, and immunoperoxidase methods were used to study the occurrence, properties, and concentration of pregnancy-associated plasma protein A (PAPP-A) in the human ovary and in the follicular fluid from 97 hyperstimulated follicles from 29 infertile women participating in an in vitro fertilization program. At the detection level of 15 micrograms/l, PAPP-A was found in 83 of 97 follicular fluids, the levels ranging from undetectable to 483 micrograms/l (median, 130 micrograms/l). In gel filtration, PAPP-A immunoreactivity of follicular fluid eluted in the same volume as placental PAPP-A, and the dose-response curves of follicular fluid PAPP-A and purified PAPP-A were parallel. The PAPP-A concentration was not affected by prior treatment with a protease inhibitor. Follicular fluid aspirates containing the ovum had a higher PAPP-A concentration than those in which no ovum was detected (P less than 0.01), whereas no difference was found in the PAPP-A concentrations between follicles yielding an ovum which was fertilized and cleaved and those yielding an unfertilizable oocyte. There was a correlation between PAPP-A and estradiol or progesterone concentrations, and between the PAPP-A concentration and the volume of follicular fluid aspirate. In hyperstimulated unruptured follicles, PAPP-A was localized in the luteinized granulosa and theca interna cells, but not if luteinization was not observed. Corpus luteum cells were also PAPP-A positive, whereas unstimulated Graafian follicles were negative. Our results indicate that PAPP-A appears in the hyperstimulated follicle shortly before ovulation and may thus play a part in the early events of human reproduction.

Chromatography, Gel↗
PubMed1984

Placental protein 12 (PP12) in menstrual fluid.

In a previous study we found placental protein 12 (PP12) in the human endometrium. We now show that PP12-like immunoreactive material is released into menstrual fluid where it occurs at concentrations from 43 to 32 000 micrograms/1. The PP12 levels in menstrual fluid are 2- to 2000-fold higher than in serum of the same individuals thus suggesting that the protein either concentrates or is produced in the endometrium. The addition of protease inhibitors has no effect on the PP12 levels. In radioimmunoassay, the dose-response curves of menstrual fluid PP12 and placental PP12 are parallel. Experiments with fused rocket immuno-electrophoresis show that menstrual and placental PP12 are indistinguishable from each other. In gel filtration, menstrual PP12 has the same molecular weight as that of purified placental PP12. By immuno-peroxidase staining, PP12 is localized in the glandular epithelial cells of the menstrual endometrium. The glandular localization and high concentration of PP12 in menstrual fluid, as compared with PP12 levels in serum and endometrium, suggest that PP12 may be secreted by the endometrium.

Adult↗
PubMed1984

The content of placental protein 12 in decidua and fetal membranes is greater than in placenta.

Radioimmunoassay, gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis were used to study the content and properties of placental protein 12 (PP12) in the placenta, decidua and fetal membranes. The tissues were obtained from early pregnancy in 12 cases, and after normal term delivery in eight cases in seven of which chorion and amnion laeve were also studied. There was more PP12 in decidua and fetal membranes than in placenta. The decidua/placenta ratio of PP12 content ranged from 2 to 1154 (mean 193, SEM 66). These results suggest that PP12 is a decidual rather than placental protein.

Adolescent↗
PubMed1984

Placental protein 12 (PP12) in the human endometrium: tissue concentration in relation to histology and serum levels of PP12, progesterone and oestradiol.

Placental protein 12 (PP12) was measured by radio-immuno-assay in serum and endometrial extracts of 25 women at various phases of the menstrual cycle, and in the decidua from six women undergoing legal abortion in early pregnancy. The results were analysed with respect to endometrial histology and serum oestradiol, progesterone and PP12 concentrations. PP12 was detected in the secretory phase endometrium and decidua, but not in the proliferative phase endometrium. The PP12 concentration in tissue increased from early (1.3-9.4 micrograms/g protein) to late secretory phase (5.3-155 micrograms/g), and considerably higher levels were found in decidua (282-3846 micrograms/g). There was a correlation (P less than 0.001) between endometrial PP12 and serum progesterone levels in non-pregnant women, and there also was a slight correlation (P less than 0.05) between endometrial and serum PP12 concentrations. These results show that PP12 is not pregnancy specific and suggest that the occurrence of PP12 is dependent on progesterone.

Adult↗
PubMed1984

Human preovulatory follicular fluid, luteinized cells of hyperstimulated preovulatory follicles, and corpus luteum contain placental protein 12.

RIA gel filtration, isoelectric focusing; and immunoperoxidase staining were employed to study the occurrence and physicochemical characteristics of placental protein 12 (PP12) in the human ovary, corpus luteum, and preovulatory follicular fluid. Fluid aspirated from 75 follicles from 22 women hyperstimulated for in vitro fertilization contained 6-230 micrograms/liter PP12-like immunoreactive material. The dose-response curves of follicular fluid PP12, amniotic fluid PP12, and purified human placental PP12 were parallel in the PP12 RIA. In gel filtration, follicular fluid PP12 eluted in the same volume as purified PP12. The isoelectric point of follicular fluid PP12 was 4.9 and that of purified placental PP12 4.6-4.7. A positive correlation was found between follicular fluid estradiol and PP12, progesterone and PP12, and follicular fluid volume and PP12 concentrations. By immunoperoxidase staining, PP12 was not detectable in unstimulated ovarian tissue before ovulation. In hyperstimulated preovulatory follicles biopsied in connection with follicle aspiration, PP12 was found in the granulosa cells which were luteinized (n = 3), whereas in those hyperstimulated follicles (n = 5) with no luteinization, no PP12 was found either. PP12 was seen in all corpora lutea (n = 5) from unstimulated menstrual cycles. These results show that the occurrence of PP12 is not limited to the placenta. The correlation between follicular fluid steroid and PP12 levels and the findings by immunoperoxidase staining suggest that PP12 is related to endocrine phenomena of the ovary, possibly to the luteinization process.

Chromatography, Gel↗
PubMed1984

Placental protein 12 (PP12) in primary liver cancer and cirrhosis.

Serum concentrations of the placental protein 12 (PP12), measured by radioimmunoassay, were found to be elevated in 15 out of 16 (94%) patients with primary liver cancer, 10 out of 68 (15%) patients with other gastrointestinal malignancies, 5 out of 10 (50%) patients with cirrhosis; and 1 out of 33 (3%) patients with benign gastrointestinal disease. No correlation was observed between the serum levels of alphafetoprotein (AFP) and PP12 in patients with primary liver cancer. Using immunoperoxidase staining, PP12 was localised in malignant hepatocytes and hyperactive nodules of cirrhosis, but rarely in malignant cells of other gastrointestinal cancers. Fetal liver was PP12 positive, while adult normal liver was negative. These results indicate that PP12 has certain oncodevelopmental characteristics.

Carcinoma, Hepatocellular↗
PubMed1984

Detection and localization of placental protein 14-like protein in human seminal plasma and in the male genital tract.

The concentration of PP14 in seminal plasma was determined by radioimmunoassay. The levels were 13-362 mg/liter in normospermic specimens (n = 36), 10-252 mg/liter in samples from 46 infertile men (oligo-, astheno-, terato- or necrospermia), and 30-233 mg/liter in 7 vasectomized men. No significant difference was found in the PP14 levels in the groups examined. Low PP14 levels (13-25 micrograms/liter) were detected in male sera. In RIA, serial dilutions of seminal plasma and purified PP14 gave parallel dose-response curves. In tandem-crossed immunoelectrophoresis, seminal plasma PP14 showed a reaction of identity with PP14 purified from human term placenta. The isoelectric point of seminal plasma PP14 was 5.2-5.4 and that of early maternal serum PP14 was 4.8-4.9. In the normospermic group a moderate negative correlation (p less than 0.05) was found between the volume of seminal plasma and the PP14 level, whereas the correlation was positive (p less than 0.05) in the infertile group. There also was a negative correlation (p less than 0.05) between the percentage of motile spermatozoa and PP14 concentration. No correlation was observed between the sperm count or age of men and PP14 level in seminal plasma. The origin of seminal plasma PP14 is not from the testes, as the levels in vasectomized and nonvasectomized men were similar. By immunoperoxidase staining, PP14 was detected in the epithelium of seminal vesicles but not in the testis.

Adult↗
PubMed1984

Hyperstimulated human preovulatory follicular fluid contains placental protein 5 (PP5).

Placental protein 5 (PP5)-like immunoreactivity was found in 22 of 28 fluids aspirated from hyperstimulated preovulatory follicles of women who participated in an in vitro fertilization program. When detectable, the PP5 levels varied from 7 to 67 micrograms/l, which are of the same order of magnitude as those seen in pregnancy sera. In gel filtration, the PP5-like immunoreactivity of follicular fluid eluted in the same volume as purified human placental PP5; and in radioimmunoassay, this substance gave an inhibition curve which was parallel to that of the PP5 standard. A positive correlation was observed between the follicular fluid concentration of estradiol and PP5 (r = 0.60; P less than 0.001), but not between the levels of progesterone, testosterone, or follicular volume and the PP5 concentration. In light of the protease inhibitor nature of PP5, its detection in preovulatory follicular fluid is intriguing in relation to its possible role in the rupture of the follicle.

Chorionic Gonadotropin↗
PubMed1983

Immunologic and biological properties and clinical significance of placental proteins PP5 and PP12.

Among the number of newly isolated placental proteins, PP5 and PP12 share some common characteristics: Both are present in the syncytiotrophoblast of normal placenta and hydatidiform mole, but less frequently, if at all, in choriocarcinoma. The levels in heparinized plasma of both proteins are lower than those in serum, and both are heat-labile. The function of PP12 is completely unknown, whereas PP5 appears to be related to the blood coagulation and fibrinolytic systems at the placental site through its antiplasmin activity. Many exciting avenues of research have been opened to uncover the biological role of these proteins in fetal development and cancer. We are pursuing this research with the immediate goal of assessing the role of PP12 in the blood coagulation system and of studying the expression of both proteins in various forms of cancer.

Amniotic Fluid↗
PubMed1982

Immunochemical demonstration of an ovarian cancer-associated urinary peptide.

Immunization with a peptide fraction from ovarian cancer urine resulted in an antiserum that reacts with a 6,000 dalton (6K) peptide. In urine from some patients with advanced gynaecological cancer, the concentration of 6K peptide was high enough to be detected by immunodiffusion. By radioimmunoassay the levels in normal serum could be determined. The concentrations in serum was 5-20 microgram/l and that in urine 5-50 microgram/l. Elevated levels were observed in urine from 5 out of 8 patients with ovarian cancer, 10 out of 14 patients with cervical cancer and 9 out of 14 patients with endometrial cancer. The highest level observed was 12,000 microgram/l. High concentrations of the 6K peptide (100-300 microgram/l) were observed in amniotic fluid from 14-16 weeks of pregnancy. Some tumor extracts also had a high concentration of the 6K peptide. No immunological relationship was observed between the peptide and known tumor-associated antigens or serum proteins. These results suggest that the peptide is a new oncodevelopmental peptide which may have significance as a tumor marker.

Antibodies, Neoplasm↗
PubMed1982

Placental protein 5 is related to blood coagulation and fibrinolytic systems.

Previous studies have shown that placental protein 5 (PP5) forms complexes with heparin. In order to further elucidate the biological role of PP5 we studied the effect of plasmin and thrombin on the immunoreactivity of PP5, and the possible functional antiplasmin and antithrombin effects of purified PP5. Varying concentrations of plasmin and thrombin were added to pregnancy plasma, and the PP5 levels, measured by radioimmunoassay, were found to be elevated by 558% (plasmin and 48-87% (thrombin). Incubation of radiolabeled PP5 with plasmin resulted in the formation of radioactive fragments with smaller molecular weights. Functional studies using a chromogenic substrate confirmed that purified PP5 has an antiplasmin activity. An average increase of 15% was observed in the antiplasmin activity when 200 ng purified PP5 was added to 150 microliters of pregnancy serum. Thus, there are certain similarities between PP5 and antihrombin III. Both form complexes with heparin and have antiplasmin properties, and both were found to be heat labile. But, functional studies utilizing a chromogenic substrate failed to demonstrate any antithrombin III-like activity in the purified PP5 preparation that had antiplasmin activity. Our results show that the function of PP5 is related to the blood coagulation and fibrinolytic systems, at least through its inhibitory action on plasmin.

Antithrombin III↗
PubMed1982

Placental protein 5 (PP5)-like immunoreactivity in human urine.

Placental protein 5 (PP5)-like immunoreactive material was detected in human male urine in small concentrations (17-60 pg/ml). Part of the PP5 immunoreactivity in the urine had a molecular weight of 36 000-42 500, which is the molecular weight of purified PP5 from the human placenta. In radioimmunoassay, serial dilutions of the 36 000-42 500 molecular weight material gave an inhibition curve parallel to that of the PP5 standard. The source of PP5-like immunoreactivity in the urine is not known. It may be related to urokinase, which coeluted with PP5-immunoreactive material in gel filtration.

Chromatography, Gel↗
PubMed1981

Human seminal plasma contains a protein that shares physicochemical and immunochemical properties with placental protein 5 from the human placenta.

Placental protein 5 (PP5)-like immunoreactive material was detected in human seminal plasma at high concentrations (32-1000 ng/ml). This was not due to interference with proteases or binding to seminal plasma proteins, since immunoreactivity was not affected by treatment with protease inhibitors, and incubation with seminal plasma of [125I]PP5 did not bring about any significant change in the elution pattern in gel filtration. Part of the PP5 immunoreactivity in seminal plasma had a molecular weight of 36,000-42,500 which is the molecular weight of purified PP5 from the human placenta. In RIa, serial dilutions of the 36,000-42,500 molecular weight material gave an inhibition curve parallel to that of the PP5 standard. The source of seminal plasma PP5-like material is not from the testes, as the levels in vasectomized men were similar to those in nonvasectomized men.

Chromatography, Gel↗
PubMed1981

Concanavalin A binding of pregnancy-specific beta-1-glycoprotein in normal pregnancy and trophoblastic disease.

The binding of pregnancy-specific beta-1-glycoprotein (SP1) to Concanavalin A (Con A) has been studied in serum samples from 34 pregnant women and 13 patients with trophoblastic diseases. In normal pregnancy and in hydatidiform moles, the fraction that did not bind to Con A accounted for 0.5--4.3% of the total SP1 concentration whereas, in 5 out of 6 patients with choriocarcinoma, the fraction was 4.8--30%. The secretion of Con A non-binding SP1 appears to be an inherent characteristic of some malignant trophoblast tissues and may result from its altered glycosylation.

Choriocarcinoma↗
PubMedDate not supplied

Seminal plasma glycodelin and fertilization in vitro.

Endometrium-derived glycodelin-A inhibits sperm-egg binding, whereas differentially glycosylated seminal plasma glycodelin-S does not. The difference has been ascribed to the specific type of glycosylation of glycodelin-A. We studied whether the total glycodelin concentration or the relative glycodelin-A concentration in seminal plasma are related to the in vitro fertilization rate of oocytes. We found that total glycodelin levels were significantly higher in a quartile of men with the lowest in vitro fertilization rate compared with the remaining 3 quartiles combined (P = .01). However, for predicting low fertilization capacity of sperm, combining the glycodelin and sperm concentrations by logistic regression analysis did not significantly increase the information obtained from sperm concentration alone. We used specific lectin-immunoassays to determine whether increased glycodelin-A-type glycosylation in seminal plasma would be related to failure to fertilize. No difference was found between the groups with high fertilization and no fertilization in vitro. It is concluded that, although high seminal plasma total glycodelin level has a tendency of being associated with a lower fertilization rate, the difference has limited value to predict fertilization in vitro.

Blood Proteins↗