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Biomedical subjects

Y Ota

Publications and source records attributed to Y Ota.

At least 163 records · Page 9Linked to original sources
PubMed1990

Enzyme immunoassay for placental protein 4 (PP4) and its possible diagnostic significance in patients with genital tract cancer.

We have established an enzyme immunoassay for placental protein 4 (PP4), by using avidin-biotin binding reaction, and set its normal range below 10.9 ng/ml (mean + 2 sigma). Throughout the menstrual cycle, the serum PP4 profile was similar to that of serum progesterone. In the follicular and ovulatory phase, PP4 remained relatively low, with the mean levels of 1.5 ng/ml and 1.8 ng/ml, respectively. In the luteal phase, the mean level was 3.2 ng/ml. In normal pregnancy, serum PP4 levels were low irrespective of gestational age, with a mean level of 3.0 ng/ml. There was only one case in which the serum PP4 level over 10.9 ng/ml. Mean serum PP4 levels and the frequencies of elevated serum PP4 levels were respectively 6.3 ng/ml and 11% in patients with benign ovarian neoplasms, 4.7 ng/ml and 6% in patients with endometriosis, and 5.5 ng/ml and 18% in patients with uterine myomata. The frequency of raised PP4 levels was 48% and the mean value was 13.3 ng/ml in patients with endometrial carcinoma, and the values were 44% and 13.4 ng/ml respectively in patients with cervical carcinoma. In patients with ovarian malignancy, the respective values were 15% and 7.0 ng/ml. The results did not relate to clinical stages of disease (FIGO), while the frequencies of elevated serum PP4 in patients with uterine carcinoma was over 40% in stage I diseases. Compared with other tumor markers such as carcino-embryonic antigen (CEA), tissue polypeptide antigen (TPA) and cancer antigen 125 (CA125), PP4 seems to be more promising as a marker of endometrial carcinoma.(ABSTRACT TRUNCATED AT 250 WORDS)

Annexin A5↗
PubMed1990

Deletion of D-helix in bovine pancreatic phospholipase A2.

D-Helix-deleted bovine pancreatic phospholipase A2 was designed using molecular mechanic calculations, and synthesized. Effects of the deletion on the enzymatic activity and on the structure were investigated. The enzymatic activity of the mutant protein was about 40% of that of the native one for a micellar substrate of 1,2-dioctanoyl-phosphatidylcholine. Although the Michaelis constant of the mutant enzyme was not changed, the catalytic constant was decreased. The dissociation constant of calcium ion was also changed. 1H NMR study revealed a slight conformation change around the active site of the mutant enzyme in addition to changes around the mutated region. The effect on the activity of the mutation seems to be due to the conformational changes around the active site.

Amino Acid Sequence↗
PubMed1990

[Six cases of Sjögren's syndrome with lichen mucosae--studies on the histopathology of salivary gland and clinical manifestation of sicca features in the patients with lichen mucosae].

A case of a 54-year old man with lichen mucosae and Sjögren's syndrome was reported. Clinical and histopathological analysis was made on the presence of sicca features in 6 patients with lichen mucosae. All patients complained either xerophthalmia or xerostomia and 5 out of 6 cases showed specific lymphocytic foci seen in Sjögren's syndrome in addition to lichenoid tissue reaction in the specimen obtained from buccal mucosae. Objective keratoconjunctivitis sicca was demonstrated in 3 cases. Immunologically, abnormal laboratory findings were observed in 5 cases (4 cases with a positive ANA and 3 cases with a positive anti microsome antibody). These findings suggest that lichen mucosae might develop in a close association with Sjögren's syndrome and relationship between these two disease was discussed in this article.

Aged↗
PubMed1989

[A fundamental and clinical investigation of cancer antigen 130 (CA 130) in the field of obstetrics and gynecology].

Two murine monoclonal antibodies designated 130-22 and 145-9 have been recently established by immunizing mice with a pulmonary carcinoma cell line (PC-9). With use of these monoclonal antibodies a sensitive sandwich immunoradiometric assay (IRMA) for cancer antigen 130 (CA130) was developed in Daiichi Radioisotope Laboratories (Tokyo). Applying this IRMA kit CA130 concentrations were measured in various body fluids with special reference to obstetrics and gynecology. The results are as follows; 1) A CA130-IRMA showed excellent sensitivity, specificity, reproducibility and analytical recovery. The standard dose-response curve covered the range from 10 to 500 U/ml. 2) Serum CA130 levels measured by this assay system were closely correlated with serum CA125 levels, demonstrating quite a high correlation coefficient (r = 0.965). 3) In pregnancy maternal CA130 levels increased moderately (less than 300 U/ml) in the first trimester, and thereafter fell rapidly under normal upper limit (less than 35 U/ml). Immediately after deliveries maternal CA130 levels showed a rapid increase, reaching 269 U/ml (mean levels). In amniotic fluids CA130 concentrations were greatly elevated (3,236 U/ml mean levels), while the levels were almost within normal limit in the umbilical arterial and venous blood. Accordingly it is necessary to measure Schwangerschaftsprotein 1 or human chorionic gonadotropin simultaneously with CA130 to rule out possible pregnancy. 4) CA130 was clearly localized in the amniotic epithelium and umbilical sheath and other placental tissue components remained negative for this antigen. Taking the lower CA130 levels in the umbilical sera into consideration, these immunohistochemical results suggest CA130 is not oncofetal but oncoplacental. 5) Serum CA130 levels increased pretherapeutically beyond 35 U/ml in 87% of ovarian malignancies, and in 56% of endometrial carcinoma. The mean levels of serum CA130 reached 931 and 143 U/ml, respectively. These data indicate clinical usefulness of CA130 as a tumor marker for those diseases. By contrast serum CA130 levels were lower, and very few cases showed serum CA130 levels over 35 U/ml in cervical cancer. 6) In endometriosis 88% of the cases demonstrated increased serum CA130 levels, indicating its usefulness for monitoring therapeutic courses, just like CA125. In benign gynecologic diseases over 80% of cases showed increased serum CA130 levels while only slight increase in serum CA130 was found (mean levels less than 84.0 U/ml). This disadvantage could be lessened by a combination assay with CA72-4 and others whose serum levels were very low in the benign diseases.

Antigens, Tumor-Associated, Carbohydrate↗
PubMed1989

Clinical significance of a solid-phase immunoradiometrical assay for sialyl SSEA-1 antigen in obstetrics and gynecology.

The clinical usefulness of sialyl SSEA-1 antigen was evaluated in obstetrics and gynecology. Serum levels of sialyl SSEA-1 were measured in patients with benign or malignant gynecologic diseases, and in normal pregnant women. Moreover, in 10 cases of full term delivery, samples of maternal sera immediately prior to delivery, soon after delivery and 5-day-puerperium, cord sera from the umbilical artery and vein, and amniotic fluid were taken to measure its concentration. During the course of pregnancy, serum SSEA-1 levels were within the normal range (below 38 U/ml), showing no significant correlation with gestational weeks. Of patients with gynecologic diseases, those with malignant ovarian neoplasms, uterine cervical carcinoma and benign ovarian neoplasms exhibited elevated (over 38 U/ml) levels in 26%, 15% and 6% of all cases, respectively. In cases of full term delivery, the concentrations of sialyl SSEA-1 in the maternal and cord sera were within the normal range. Concentrations were extremely high, however, in the amniotic fluid.

Amniotic Fluid↗
PubMed1988

Secretion of the proenzyme and active bovine pancreatic phospholipase A2 enzyme by Saccharomyces cerevisiae: design and use of a synthetic gene.

We have developed a phospholipase A2(PLA2)-producing system using Saccharomyces cerevisiae. A 456-bp synthetic DNA fragment was constructed encoding bovine pancreatic phospholipase A2 (proPLA2; zymogen) along with the signal sequence of dog pancreatic PLA2. Yeast-preferred codons were chosen and unique restriction enzyme sites were incorporated. 22 oligodeoxynucleotides that varied in size from 33 to 48 nucleotides were chemically synthesized and assembled into the DNA fragment, which was then placed under the control of the yeast acid phosphatase repressible promoter. The resulting plasmid, transformed into S. cerevisiae, directed the synthesis of about 2.8 micrograms/ml of PLA2, most of which was secreted into the culture fluid. The secreted PLA2 comprised 18 to 26% of active enzyme, the remainder being proenzyme. Both had the expected N-terminal amino acid sequences, indicating that the yeast accurately released the signal peptide and the activation peptide (N-terminal heptapeptide of proPLA2). The specific activity of PLA2 thus produced is the same as that of the authentic bovine enzyme.

Amino Acid Sequence↗
PubMed1988

Relation between serum levels of tissue polypeptide antigen (TPA) and cancer antigen 125 (CA125) and their immunohistochemical identification in benign and malignant gynecological disease.

We studied immunohistochemical stains for TPA and CA125 in patients with benign and malignant gynecologic diseases. The results were as follows: (1) CA125 was not found in ovarian mucinous cystadenocarcinoma but was demonstrated immunohistochemically in 82% of ovarian serous cystadenocarcinomas and 83% of Krukenberg's tumors. (2) TPA was demonstrated in 65% of ovarian serous and 75% of ovarian mucinous cystadenocarcinomas, and in 58% of endometrial carcinomas. (3) TPA was found in all trophoblastic tumors examined, while CA125 was found in none. Eighty-three percent of patients with trophoblastic diseases had raised serum TPA levels. (4) When serum CA125 levels were raised CA125 was demonstrated immunohistochemically in 71% of patients with ovarian serous cystadenocarcinomas, 67% of patients with Krukenberg's tumors and 100% of patients with tubal carcinomas. (5) Despite elevated serum levels, CA125 and TPA were not identified by immunohistochemistry in 64% cases of benign ovarian disease and in 80% of patients with uterine myomata. (6) It would seem that CA125 was more easily released from tumor cells than TPA.

Antigens, Neoplasm↗
PubMed1988

Serum levels of six tumor markers in patients with benign and malignant gynecological disease.

We studied the pretreatment serum levels of 6 tumor markers in gynecological patients with and without malignant disease. The tumor markers were carcinoembryonic antigen (CEA), tissue polypeptide antigen (TPA), ferritin, Schwangerschaftsprotein 1 (SP1), Schwangerschaftsprotein 3 (SP3) and cancer antigen 125 (CA125). The results were as follows: (1) Serum CA125 and TPA levels were raised in 81% and 57% of patients with ovarian serous cystadenocarcinoma; CEA and SP3, in 52% and 43% respectively of patients with ovarian mucinous cystadenocarcinoma; CA125, TPA and SP3, in 76%, 48% and 48% respectively of patients with other ovarian malignancies; and TPA and SP3, in 56% and 40% respectively of patients with endometrial carcinoma. (2) Serum levels of TPA, ferritin and CA125 were more often raised with advancing stages of malignant disease. (3) Serum TPA levels were elevated in 55% of patients with stage I endometrial carcinoma, and serum SP3 levels were elevated in 35% of patients with a stage I malignant ovarian neoplasm and in 45% of patients with endometrial carcinoma. (4) One of the 6 tumor markers showed a raised level in 84% of patients with gynecologic malignancy as against 56% in those with benign gynecologic diseases.

Antigens↗
PubMed1988

Experiments with tissue cultures from a human ovarian serous cystadenocarcinoma producing cancer antigen 125 (CA125), tissue polypeptide antigen (TPA) and carcinoembryonic antigen (CEA).

The patient was a 57-year-old woman with ovarian serous cystadenocarcinoma in FIGO clinical stage IV. Cancer antigen 125 (CA125), tissue polypeptide antigen (TPA) and carcinoembryonic antigen (CEA) were immunohistochemically demonstrated in tumor cells, and the variations of serum CA125 and TPA levels reflected the clinical course. The tumor tissue obtained at exploratory laparotomy was minced with scissors, and transplanted subcutaneously into female nude mice for in vivo maintenance. The tumor cells from 5th generation nude mice were dispersed in Eagle's minimal essential medium supplemented with 10% fetal calf serum, and incubated in Falcon tissue culture dishes at 37 degrees C in 5% CO2 in air for in vitro maintenance. The results were as follows: Histopathologically the tumor transplanted into nude mice showed a cystadenocarcinoma, which closely resembled the original human tumor. Immunohistochemically CA125, TPA and CEA were demonstrated in the tumor transplanted into nude mice as well as in the original human tumor. From the growth curve in nude mice, the doubling time was estimated to be about 3.5 days. Serum TPA levels in nude mice were increased in proportion to the tumor growth after transplantation, but serum levels CA125 and CEA were normal. The concentrations of CA125 and TPA were increased in the conditioned media compared with the control media, although the elevated values were decreased with subsequent passages. CEA concentrations in the conditioned media were unchanged.

Animals↗
PubMed1988

Immunohistochemical studies of ameloblastoma with special emphasis on keratin.

Ten cases of ameloblastoma including a case of gingival origin and a case of atypical ameloblastoma were studied immunohistochemically, especially with monoclonal and polyclonal anti-keratin antibodies. Stellate reticulum cells reacted strongly with monoclonal and polyclonal anti-keratin antibodies but columnar cells were reacted weakly. The level of keratinization of columnar cells was similar to that of the basal cell layer of the gingival squamous epithelium. Our immunohistochemical studies suggested that the process of keratinization-ameloblastoma follows the sequence of 1) cuboidal cells 2) columnar cells 3) stellate reticulum cells and 4) metaplastic squamous cells. The findings also disclosed the epithelial nature of granular cells. The reactivity of the components of atypical ameloblastoma differed from that of other cases. Other positive "markers" in ameloblastomas included CEA and CA19-9, but no particular histologic differences were observed between positive and negative cases.

Adult↗
PubMed1987

The immunocytochemical localization of new soluble placental tissue proteins (PP14, 16, 17, 19, 20 and PP21) in human and cynomolgus monkey placentae.

Apparently Placenta-specific placental tissue proteins (PP14 and PP17) and solitary tissue proteins (PP16, 19, 20 and PP21) were investigated by avidin-biotin immunoperoxidase technique in the human and cynomolgus monkey placentae, membranes, decidua and umbilical cords. In human early placentae, PP14, 16, 17, 19 and PP21 were localized mainly in the cytoplasm of villous syncytiotrophoblast. PP20 was localized in the cytoplasm of basal chorionic trophoblasts. In human term placentae, positive stainings for PP16, 19 and PP21 were observed mainly in all kinds of trophoblastic cells, while positive stainings for PP14, 17 and PP20 were weakened in the trophoblastic cells. PP20 was clearly localized in the cytoplasm of Hofbauer-like cells in the villous stroma. The membrane of villous syncytiotrophoblast showed strongly positive stainings for PP21. PP21 was also localized in the membrane of amniotic and umbilical epithelium. The umbilical epithelium was cytoplasmically positive for PP14, 16 and PP20. Clear positive stainings for PP14 and PP21 were found in the cytoplasm of fetal polymorphonuclear neutrophils. All of the placental proteins were immunocytochemically positive in the decidual large cells. In the cynomolgus monkey placentae, similar immunostaining results were obtained. The monkey could, thus, serve as a model for the investigation of the placental proteins.

Amnion↗