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Biomedical subjects

S G Joshi

Publications and source records attributed to S G Joshi.

At least 37 records · Page 2Linked to original sources
PubMed1986

Serum and peritoneal fluid proteins in women with and without endometriosis.

We examined the proteins in serum and peritoneal fluid of women with endometriosis (and of healthy controls) for evidence of an autoimmune response that might account for their impaired fertility. No antibodies against endometrial glycoproteins or against "progestin dependent endometrial protein" (PEP) were found in any serum or peritoneal fluid sample. Levels of PEP were not different in serum from women with moderate to severe endometriosis (n = 6), with mild endometriosis (n = 21), or from disease-free cycling controls (n = 19). PEP levels in peritoneal fluid from mild endometriosis and from controls did not differ but were elevated ten times in fluid obtained in the secretory phase from women with moderate to severe disease. This suggests that PEP levels in peritoneal fluid reflect the extent of ectopic endometrial growth. The salient finding was a heretofore undescribed protein (mol wt 70,000) in secretory phase peritoneal fluid samples (18/20) and its absence during the proliferative phase (0/35).

Ascitic Fluid↗
PubMed1980

Progestogen-dependent endometrial protein in women: tissue concentration in relation to developmental stage and to serum hormone levels.

The presence of a progestogen-dependent endometrial protein (PEP) in women was previously described. The present study was undertaken to determine whether the occurrence or the concentration of PEP in endometria is related to the developmental stage of tissues and/or to the levels of endogenous progesterone (P) or 17 beta-estradiol (E) to which the tissues are exposed. Samples of serum and endometrial tissue in different developmental stages were obtained from pregnant women and women with normal menstrual cycles and were analyzed for PEP. In addition, the sera were analyzed for P and E. The occurrence of PEP in the endometrium of all of the women who were studied was found to be correlated with the heightened secretory activity and with the decidual change in the tissue. Furthermore, in women with normal cycles, the detection of PEP was associated with high serum levels of P. Comparison of serum levels of P with endometrial levels of PEP in pregnant women and in women in the mid-secretory phase of the menstrual cycle indicated that a 2.8-fold rise in serum levels of P during pregnancy was accompanied by a comparable (about threefold) rise in tissue levels of PEP. Therefore, we conclude that, in pregnant women and women with normal cycles, the levels of PEP in the endometrium reflect developmental changes within the endometrium, and that those levels are directly related to serum levels of P.

Adult↗
PubMed1980

Detection and synthesis of a progestagen-dependent protein in human endometrium.

Immunologiocal and biochemical methods were employed to demonstrate the presence of progestagen-dependent proteins in human endometrium. Cytosols were prepared from proliferative and secretory phase endometria of cycling women, from decidua and decidua-rich tissues of women in early pregnancy and from decidua of tubal pregnancy. Antisera were raised in rabbits against the antigens of decidua of tubal pregnancy and decidua-rich tissues. Immunoelectrophoresis, Ouchterlony's immunodiffusion test and polyacrylamide gel electrophoresis using native gels revealed 2 antigenic proteins, designated antigens A and B, in secretory endometria, decidua-rich tissues, decidua, and in decidua of tubal pregnancy. However, only 1 antigenic protein was detected by SDS-gel electrophoresis: antigens A and B may therefore be two different proteins or two forms of a single protein. The antigens could not be detected in non-pregnancy sera or in term placentae. Double isotopic labelling (incubation of tissues with [3H]- and [14C]leucine) followed by protein fractionation methods were used to compare the in-vitro synthesis rates of antigens in poroliferative tissues with those in decidua or secretory endometria. The rate of synthesis of antigens A and B was markedly higher in the decidua and secretory endometria than in the proliferative endometria. We conclude, therefore, that during progestagen-dependent transformation of proliferative phase endometria into secretory endometria and decidua in women, there is a selective stimulation of at least one species of pregnancy-associated protein.

Adult↗
PubMed1980

Properties of the progestagen-dependent protein of the human endometrium.

Antigens A and B, shown to be associated with the progestagen-dominated human endometrium, were partly purified and their properties studied. The antigens were recovered in the crude nuclei, the heavy particulate fraction and cytosol of decidua-rich tissue from early pregnancy. The antigens in cytosol were enriched by a combination of Concanavalin A-Sepharose chromatography and polyacrylamide gel electrophoresis. The immunological reactivity of the antigens after partial purification by Concanavalin A-Sepharose chromatography was retained after 30 min exposure to 4-85 degrees C at pH 7.4, or after 2 h to pH 2-12 at 22 degrees C. Trypsin, but not pepsin, RNase, DNase or neuraminidase, completely destroyed immunological reactivity of both antigens. The apparent molecular weight of both antigens determined by filtration on Sephadex G100 was 48 000. The isoelectric point of both antigens was approximately 4.9. The antigens were not immunologically related to transferrin, ceruloplasmin, alpha-1-antitrypsin, ferritin, uteroglobin, alpha-fetoprotein, human chorionic gonadotrophin, pregnancy-associated plasma proteins or pregnancy zone protein. Furthermore, the antisera to Antigens A and B did not react with the decidual cytosol of pregnant baboons or of pseudopregnant rats.

Antigens↗
PubMed1980

A progestagen-dependent endometrial protein in human amniotic fluid.

A protein was detected in human amniotic fluid that had properties identical to those of the progestagen-dependent endometrial protein. The concentration of the amniotic fluid protein was maximal during Weeks 15-18 of pregnancy and then declined rapidly. The protein was not detected in immature and mature placentae, ovary, Fallopian tube, myometrium and cervix. We conclude that a specific protein synthesized by the human uterine decidua is transported to the amniotic sac.

Adult↗
PubMed1976

Effects of progesterone on labeling of soluble proteins and glycoproteins in rabbit endometrium.

An in vitro test system was used to study in vivo effects of progesterone on synthesis and secretion of total proteins and glycoproteins in rabbit endometrium. Endometrial explants incubated in Eagle's minimal essential medium containing radioactive leucine and N-acetylglucosamine were found to synthesize soluble proteins readily, including glycoproteins. Furthermore, significant amounts of newly synthesized proteins, including blastokinin, were released by the tissues into the incubation medium. In addition, in vitro synthesis and release of labeled proteins by estrogen-primed endometrial tissue (E-primed tissue) was significantly enhanced by exposure of the tissues to progesterone in vivo. Double-labeling studies demonstrated qualitative as well as quantitative differences in peptide synthesis between E-primed tissues and E-primed, progesterone-treated tissues. Progesterone also stimulated both the synthesis and the release of glycoprotein by E-primed tissues. These studies, therefore, suggest that progesterone regulates qualitatively and quantitatively the synthesis and secretion of total proteins, including glyco-proteins, in rabbit endometrium.

Acetylglucosamine↗