scholarly journals Alkaline phosphatases contribute to uterine receptivity, implantation, decidualization, and defense against bacterial endotoxin in hamsters

Reproduction ◽  
2013 ◽  
Vol 146 (5) ◽  
pp. 419-432 ◽  
Author(s):  
Wei Lei ◽  
Heidi Nguyen ◽  
Naoko Brown ◽  
Hua Ni ◽  
Tina Kiffer-Moreira ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Epithelial Cells ◽  
Hormonal Regulation ◽  
Cell Type ◽  
Uterine Receptivity ◽  
Rt Pcr ◽  
Alkaline Phosphatases ◽  
Specific Expression ◽  
Luminal Epithelial Cells

Alkaline phosphatase (AP) activity has been demonstrated in the uterus of several species, but its importance in the uterus, in general and during pregnancy, is yet to be revealed. In this study, we focused on identifying AP isozyme types and their hormonal regulation, cell type, and event-specific expression and possible functions in the hamster uterus during the cycle and early pregnancy. Our RT-PCR and in situ hybridization studies demonstrated that among the known Akp2, Akp3, Akp5, and Akp6 murine AP isozyme genes, hamster uteri express only Akp2 and Akp6; both genes are co-expressed in luminal epithelial cells. Studies in cyclic and ovariectomized hamsters established that while progesterone (P4) is the major uterine Akp2 inducer, both P4 and estrogen are strong Akp6 regulators. Studies in preimplantation uteri showed induction of both genes and the activity of their encoded isozymes in luminal epithelial cells during uterine receptivity. However, at the beginning of implantation, Akp2 showed reduced expression in luminal epithelial cells surrounding the implanted embryo. By contrast, expression of Akp6 and its isozyme was maintained in luminal epithelial cells adjacent to, but not away from, the implanted embryo. Following implantation, stromal transformation to decidua was associated with induced expressions of only Akp2 and its isozyme. We next demonstrated that uterine APs dephosphorylate and detoxify endotoxin lipopolysaccharide at their sites of production and activity. Taken together, our findings suggest that uterine APs contribute to uterine receptivity, implantation, and decidualization in addition to their role in protection of the uterus and pregnancy against bacterial infection.

scholarly journals Pig Conceptuses Secrete Estrogen and Interferons to Differentially Regulate Uterine STAT1 in a Temporal and Cell Type-Specific Manner

Endocrinology ◽  
2007 ◽  
Vol 148 (9) ◽  
pp. 4420-4431 ◽  
Author(s):  
Margaret M. Joyce ◽  
Robert C. Burghardt ◽  
Rodney D. Geisert ◽  
James R. Burghardt ◽  
R. Neil Hooper ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Secretory Proteins ◽  
Cell Type ◽  
Specific Expression ◽  
Interferon Stimulated Genes ◽  
Close Proximity ◽  
Cell Type Specific Expression ◽  
Cell Type Specific ◽  
Pregnancy Recognition ◽  
Luminal Epithelial Cells

Conceptus trophectoderm and uterine luminal epithelial cells interact via endocrine, paracrine, and autocrine modulators to mediate pregnancy recognition and implantation. Pig conceptuses not only release estrogens for pregnancy recognition but also secrete interferons during implantation. Because interferon-stimulated genes are increased by interferons secreted for pregnancy recognition in ruminants, we asked whether the interferon-stimulated gene, STAT1, is up-regulated in pig endometrium by conceptus estrogens and/or interferons. STAT1 expression in response to day of pregnancy, estrogen injection, and intrauterine infusion of conceptus secretory proteins in pigs indicated 1) estrogen increases STAT1 in luminal epithelial cells, 2) conceptus secretory proteins that contain interferons increase STAT1 in stroma, 3) STAT1 increases in close proximity to the conceptus, and 4) early estrogen results in conceptus death and no STAT1 in stroma. The interactions of estrogen and interferons to regulate cell-type-specific expression of STAT1 highlight the complex interplay between endometrium and conceptus for pregnancy recognition and implantation.

Expression of the ammonia transporter proteins Rh B glycoprotein and Rh C glycoprotein in the intestinal tract

2005 ◽  
Vol 288 (5) ◽  
pp. G1036-G1047 ◽  
Author(s):  
Mary E. Handlogten ◽  
Seong-Pyo Hong ◽  
Li Zhang ◽  
Allen W. Vander ◽  
Marshall L. Steinbaum ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Epithelial Cells ◽  
Intestinal Tract ◽  
Pcr Amplification ◽  
Immunoblot Analysis ◽  
Rt Pcr ◽  
Specific Expression ◽  
Ammonia Metabolism ◽  
Transporter Family ◽  
Ammonia Transport

Ammonia metabolism is important in multiple aspects of gastrointestinal physiology, but the mechanisms of ammonia transport in the gastrointestinal tract remain incompletely defined. The present study examines expression of the ammonia transporter family members Rh B glycoprotein (RhBG) and Rh C glycoprotein (RhCG) in the mouse gastrointestinal tract. Real-time RT-PCR amplification and immunoblot analysis identified mRNA and protein for both RhBG and RhCG were expressed in stomach, duodenum, jejunum, ileum, and colon. Immunohistochemistry showed organ and cell-specific expression of both RhBG and RhCG. In the stomach, both RhBG and RhCG were expressed in the fundus and forestomach, but not in the antrum. In the forestomach, RhBG was expressed by all nucleated squamous epithelial cells, whereas RhCG was expressed only in the stratum germinativum. In the fundus, RhBG and RhCG immunoreactivity was present in zymogenic cells but not in parietal or mucous cells. Furthermore, zymogenic cell RhBG and RhCG expression was polarized, with apical RhCG and basolateral RhBG immunoreactivity. In the duodenum, jejunum, ileum, and colon, RhBG and RhCG immunoreactivity was present in villous, but not in mucous or crypt cells. Similar to the fundic zymogenic cell, RhBG and RhCG expression in villous epithelial cells was polarized when apical RhCG and basolateral RhBG immunoreactivity was present. Thus the ammonia transporting proteins RhBG and RhCG exhibit cell-specific, axially heterogeneous, and polarized expression in the intestinal tract suggesting they function cooperatively to mediate gastrointestinal tract ammonia transport.

scholarly journals Characterization of breast carcinomas by two monoclonal antibodies distinguishing myoepithelial from luminal epithelial cells.

1986 ◽  
Vol 34 (7) ◽  
pp. 869-881 ◽  
Author(s):  
R B Nagle ◽  
W Böcker ◽  
J R Davis ◽  
H W Heid ◽  
M Kaufmann ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Epithelial Cells ◽  
Tumor Cells ◽  
Mammary Tissue ◽  
Cytokeratin 19 ◽  
Proliferating Cells ◽  
Cytokeratin 5 ◽  
Homogeneous Pattern ◽  
Luminal Epithelial Cells

Two monoclonal antibodies, KA 1 and KA 4, raised against human epidermis, were biochemically and immunologically characterized and were shown to react with specific cytokeratin polypeptides. On frozen sections of human mammary gland, these antibodies distinguish between myoepithelial and luminal epithelial cells. We present evidence that in these cells KA 1 antibody recognized cytokeratin 5 and KA 4 antibody cytokeratin 19. In normal mammary tissue, KA 4 antibody invariably reacted with the epithelial cells lining the lumina of acini, ductules, ducts, and sinus. In contrast, KA 1 antibody decorated only the myoepithelial and basal epithelial cells of acini, ducts, and sinus. In ductules, however, KA 1 also stained the luminal cells. All 73 invasive lobular and ductal carcinomas studied reacted with KA 4 antibody; five of these were also positive, apparently in the same tumor cells, with KA 1. The tumor cells of in situ carcinomas were also stained in a homogeneous pattern with KA 4 antibody; KA 1 antibody reacted only with the surrounding myoepithelium. In epithelial hyperplasias, the proliferating cells were decorated by KA 1 and KA 4 antibodies in a heterogeneous pattern. Other antibodies were used for comparison. The results are discussed with respect to epithelial differentiation and pathogenesis and to the application of such antibodies for immunohistodiagnosis of mammary lesions.

Influence of Light on the Alkaline Phosphatase Activity of Selenastrum capricornutum (Chlorophyceae) in Streams

1985 ◽  
Vol 42 (2) ◽  
pp. 384-388 ◽  
Author(s):  
R. L. Klotz
Keyword(s):  
New York ◽  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
New York State ◽  
Selenastrum Capricornutum ◽  
Alkaline Phosphatases ◽  
Reactive Phosphorus ◽  
First Time

The alkaline phosphatase activity (APA) of Selenastrum capricomutum Printz incubated in situ in four streams in New York State was inversely related to total insolation. APA was not correlated with stream molybdate reactive phosphorus over the range of concentrations encountered. Selenastrum showed no diel cycle of APA. The phosphorus fraction made available by the activity of alkaline phosphatases, enzyme hydrolyzable phosphorus (measured for the first time in streams), increased the phosphorus supply to organisms with high APA.

scholarly journals Expression of Prolactin mRNA in Rat Mammary Gland During Pregnancy and Lactation

2000 ◽  
Vol 48 (3) ◽  
pp. 389-395 ◽  
Author(s):  
Toshiki Iwasaka ◽  
Shinobu Umemura ◽  
Kochi Kakimoto ◽  
Haruko Koizumi ◽  
Yoshiyuki R. Osamura
Keyword(s):  
Mammary Gland ◽  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Late Pregnancy ◽  
Mammary Epithelial ◽  
Rt Pcr ◽  
Pregnancy And Lactation ◽  
Rat Mammary Gland ◽  
Pcr Method

We studied the expression of prolactin (PRL) mRNA in the mammary gland of resting, pregnant, lactating, and weanling rats using in situ and solution reverse transcriptase-polymerase chain reaction (RT-PCR). In mid- to late pregnancy and throughout lactation, PRL mRNA was detected in both in situ and solution RT-PCR. These PRL mRNA signals were clearly identified in the cytoplasm of alveolar and ductal mammary epithelial cells by the in situ RT-PCR method. In mid- to late pregnancy, such as at the initiating point of PRL mRNA expression, we confirmed in some cases a lack of PRL mRNA by solution RT-PCR. In addition, in the early weaning phase, no signals were detected by solution RT-PCR. However, slight focal signals were detected in some poorly vacuolated cytoplasm of regressing acinar cells by in situ RT-PCR. These findings suggest that PRL mRNA in rat mammary gland begins in mid- to late pregnancy in parallel with the development of the mammary gland, continues throughout lactation, and declines in the early phase of weaning, with regression of mammary epithelial cells.

Tandem duplication of the fabp1b gene and subsequent divergence of the tissue-specific distribution of fabp1b.1 and fabp1b.2 transcripts in zebrafish (Danio rerio)

Genome ◽  
2009 ◽  
Vol 52 (12) ◽  
pp. 985-992 ◽  
Author(s):  
Santhosh Karanth ◽  
Eileen M. Denovan-Wright ◽  
Christine Thisse ◽  
Bernard Thisse ◽  
Jonathan M. Wright
Keyword(s):  
In Situ Hybridization ◽  
Linkage Group ◽  
Tandem Duplication ◽  
Duplication Event ◽  
Rt Pcr ◽  
Specific Expression ◽  
Fatty Acid Binding ◽  
Tissue Specific ◽  
Specific Distribution

We describe a fatty acid-binding protein 1 (fabp1b.2) gene and its tissue-specific expression in zebrafish embryos and adults. The 3.5 kb zebrafish fabp1b.2 gene is the paralog of the previously described zebrafish fabp1a and fabp1b genes. Using the LN54 radiation hybrid mapping panel, we assigned the zebrafish fabp1b.2 gene to linkage group 8, the same linkage group to which fabp1b.1 was mapped. fabp1b.1 and fabp1b.2 appear to have arisen by a tandem duplication event. Whole-mount in situ hybridization of a riboprobe to embryos and larvae detected fabp1b.2 transcripts in the diencephalon and as spots in the periphery of the yolk sac. In adult zebrafish, in situ hybridization revealed fabp1b.2 transcripts in the anterior intestine and skin, and reverse transcription PCR (RT-PCR) detected fabp1b.2 transcripts in the intestine, brain, heart, ovary, skin, and eye. By contrast, fabp1b.1 transcripts were detected by RT-PCR in the liver, intestine, heart, testis, ovary, and gills. The tissue-specific distribution of transcripts for the tandemly duplicated fabp1b.1 and fabp1b.2 genes in adult tissues and during development suggests that the duplicated fabp1b genes of zebrafish have acquired additional functions compared with the ancestral fabp1 gene, i.e., by neofunctionalization. Furthermore, these functions were subsequently divided between fabp1b.1 and fabp1b.2 owing to subfunctionalization.

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