Immunohistochemical location of placental proteins (PP8, 9, 10, 11, 12) in human term placentae

Inaba, Noriyuki; Renk, T.; Bohn, H.

doi:10.1007/bf02108266

Cited by 47 publications

(13 citation statements)

References 15 publications

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“…33 Transgelin, a 22 kDa protein constitutively expressed in the uterus 34 and previously described as a biomarker for arterial vessel remodeling in uterine tissue 34 and as a protein associated with endometriosis 35 was elevated in the EP profile in the present study. The EP luminal fluid also contained a substantial abundance of PP9, a trophoblast protein, 36 which was barely detectable in the NP profile. This result is in agreement with previous reports that PP9 is found in great abundance in uterine luminal fluid from early pregnant ewes (gestational day 17).…”

Section: Discussionmentioning

confidence: 99%

Proteomic Profile of Uterine Luminal Fluid from Early Pregnant Ewes

2010

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Embryonic development is a time-sensitive period that requires a synchronized uterine environment, which is created by the secretion of proteins from both the embryo and uterus. Numerous studies have identified uterine luminal proteins and related these to specific adaptations during early pregnancy (EP). However, no study has yet utilized LC-MS/MS to identify the signature profile of proteins in the uterine lumen during EP. In this study, uterine luminal fluid from nonpregnant (NP; n = 3) and EP (n = 3; gestational day 16) ewes were analyzed by LC-MS/MS and validated by Western immunoblotting. We identified a unique signature profile for EP luminal fluid; 15 proteins related to specific aspects of embryonic development including growth and remodeling, immune system regulation, oxidative stress balance, and nutrition were significantly altered (up to 65-fold of NP) in EP profile. Specific uterine remodeling proteins such as transgelin (P = 0.008) and placental proteins like PP9 (P = 0.02) were present in EP luminal fluid but were barely detectable in the NP flushings. Direct correlations (R2 = 0.84, P = 0.01) were observed between proteomics and immunoblotting. These data provide information on dynamic physiological processes associated with EP at the level of the uterus and conceptus and may potentially demonstrate a signature profile associated with embryonic well-being.

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Section: Discussionmentioning

confidence: 99%

Proteomic Profile of Uterine Luminal Fluid from Early Pregnant Ewes

2010

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“…Inaba et al have investigated the localization of PP5, PP10, PPll, and PP12 in trophoblastic tumors and ovarian adenocarcinomas by using immunohistochemical methods [9,11,13,14]. These proteins have been found to be associated with the carcinoma of the breast and digestive system [3,10,12,15].…”

Section: Introductionmentioning

confidence: 98%

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

Ota

Inaba

Shirotake

et al. 1990

Arch Gynecol Obstet

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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)

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“…Employing a colorimetric assay on purified placental protein and on periplasmic and cytoplasmic fractions of extracts prepared from E. coli, containing the 42-and 45-kDa proteins, respectively, a putative serine protease activity was assigned to the placental and to the recombinant 42-kDa proteins (6). Another piece of information, which may contribute to the understanding of PP11 biological role, derives from its subcellular localization; PP11 was exclusively localized in the cytoplasm of syncytiotrophoblast (7). Since then, PP11 has not been subjected to further characterization, validating its protease activity and investigating its natural substrates.…”

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confidence: 99%

The Tumor Marker Human Placental Protein 11 Is an Endoribonuclease

Laneve

Gioia

Ragno

et al. 2008

Journal of Biological Chemistry

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Human PP11 (placental protein 11) was previously described as a serine protease specifically expressed in the syncytiotrophoblast and in numerous tumor tissues. Several PP11-like proteins were annotated in distantly related organisms, such as worms and mammals, suggesting their involvement in evolutionarily conserved processes. Based on sequence similarity, human PP11 was included in a protein family whose characterized members are XendoU, a Xenopus laevis endoribonuclease involved in small nucleolar RNA processing, and Nsp15, an endoribonuclease essential for coronavirus replication. Here we show that the bacterially expressed human PP11 displays RNA binding capability and cleaves single stranded RNA in a Mn 2؉ -dependent manner at uridylates, to produce molecules with 2,3-cyclic phosphate ends. These features, together with structural and mutagenesis analyses, which identified the potential active site residues, reveal striking parallels to the amphibian XendoU and assign a ribonuclease function to PP11. This newly discovered enzymatic activity places PP11-like proteins in a completely new perspective. PP11 (placental protein 11) is one of the five glycoproteins (together with PP8, PP9, PP10, and PP12) that were first isolated from aqueous extracts of human term placentas in the 1980s. Unlike PP8 and PP9, which were found in relatively high concentrations in all tissues analyzed, PP10, PP11, and PP12 were supposed to be specific to the placentas, since they could not be detected in extracts of other human tissues (1, 2). Interestingly, it was shown that the placenta-specific proteins were also expressed in several tumor tissues; PP11 was detected in 66.7% of the analyzed mucinous cystadenocarcinomas and in 57.1% of serous cystadenocarcinomas tested, whereas it was not found in normal ovaries (3). Moreover, PP11 was also found in 47% of all breast cancers examined (4) and in 38% of all testicular and gastric cancers studied (5). These results suggested

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Immunohistochemical location of placental proteins (PP8, 9, 10, 11, 12) in human term placentae

Cited by 47 publications

References 15 publications

Proteomic Profile of Uterine Luminal Fluid from Early Pregnant Ewes

Proteomic Profile of Uterine Luminal Fluid from Early Pregnant Ewes

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

The Tumor Marker Human Placental Protein 11 Is an Endoribonuclease

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