Measurement of Pregnancy-Associated Plasma Proteins during Human Gestation

Lin, Tsue-Ming; Halbert, Seymour P.; Spellacy, William N.

doi:10.1172/jci107794

Cited by 175 publications

(102 citation statements)

References 33 publications

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“…PAPPA, originally isolated as one of the proteins synthesized in the placenta, circulating at high concentrations in pregnant women, is commonly used as biochemical marker in the screening of Down's syndrome during first-trimester of pregnancy (Lin et al, 1974;Van Heesch et al, 2010;Wald et al, 1999). PAPPA seems to be a critical determinant of growth and development through the proteolysis of insulin-growth-factor-binding proteins (IGFBPs), which bind IGFI and IGFII, thus preventing their interaction with IGF receptors (Oxvig, 2001).…”

Section: M43 Familymentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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Section: M43 Familymentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

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“…This protein is secreted into the maternal blood like human PSG and the presumed murine PSG homologue PAMP-2 (Lin et al, 1974;Hau and Skovgaard Jensen, 1987). Its smaller size (116 kDa) in the blood may be caused by proteolytic cleavage or other modifications.…”

Section: Discussionmentioning

confidence: 99%

Spatiotemporal expression of pregnancy‐specific glycoprotein gene rnCGM1 in rat placenta

Rebstock

Lucas

Weiß

et al. 1993

Developmental Dynamics

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As a basis towards a better understanding of the role of the pregnancy-specific glycoprotein (PSG) family in the maintenance of pregnancy, detailed investigations are described on the expression of a recently identified rat PSG gene (rnCGMl) at the mRNA and protein levels. Using specific oligonucleotide primers, rnCGMl transcripts were identified after reverse transcription, polymerase chain reaction, and hybridization with a radiolabelled, internal oligonucleotide. Transcripts were only found in significant amounts in placenta. In situ hybridization visualized rnCGM1 transcripts at day 14 post coitum (P.c.), in secondary trophoblast giant cells and in the spongiotrophoblast. Only those secondary giant cells lining the maternal decidua were positive. In contrast, primary giant cells did not contain rnCGMl mRNA. At day 18 P.c., rnCGMl transcripts were almost exclusively detectable in the spongiotrophoblast. No rnCGMl transcripts were found in rat embryos of these two developmental stages. Rabbit antisera were generated against the amino-terminal immunoglobulin variable-like domain and against a synthetic peptide containing the last 13 carboxy-terminal amino acids of rnCGMI. Both antisera recognized a 124 kDa protein in day 18 rat placental extracts as identified by Western blot analysis. The anti-peptide antiserum recognized a 116 kDa protein in the serum of a 14 day p.c. pregnant rat that is absent from the sera of non-pregnant females. Taken together, these results confirm exclusive expression of rnCGMl in the rat trophoblast, but unlike human PSG, negligible or no expression is found in other organs, such as fetal liver or salivary glands, indicating a more specialized function of rnCGM1. Its spatiotemporal expression pattern is conducive with a potential role of PSG in protecting the fetus against the maternal immune system andlor in regulating the invasive growth of trophoblast cells. 0 1993 Wiley-Liss, Inc.

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“…Restriction endonuclease sites on lorist B cosmids were mapped by partial digestion after conversion into phosmids, as described previously (Hohn 1983;Little and Cross 1985). Exon positions were determined by sequencing and PCR (as above), using primers from different exons of Cea-2.…”

Section: Mapping Of Cosmid Clonesmentioning

confidence: 99%

“…In contrast to the CEA-related proteins, which are membrane-bound, they appear to be secreted because most of them lack hydrophobic C-terminal domains suitable for membrane anchorage. PSGs are produced in large amounts by the syncytiotrophoblast and represent the major group of placental proteins in the serum of women at term pregnancy (Lin et al 1974). As tumors of trophoblastic origin also produce PSGs, these proteins have been used as markers to monitor the treatment of choriocarcinoma patients (Sakuragi 1982).…”

Section: Introductionmentioning

confidence: 99%

Characterization of murine carcinoembryonic antigen gene family members

et al. 1992

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Abstract. The carcinoembryonic antigen (CEA) is a human tumor marker whose gene belongs to a family with more than 20 members. This gene family codes for a group of proteins with in vitro cell adhesion properties and for a group of abundantly expressed pregnancy-specific glycoproteins (PSG) with unknown functions. As a basis for in vivo functional studies, we have started to analyze the murine CEA gene family and have identified five new members (Cea-2 to Cea-6). eDNA clones were isolated for Cea-2, Cea-3, and Cea-6. The deduced amino acid sequences of Cea-2 and Cea-6 indicate three IgV-like (N), followed by one IgC-like (A) domain (N1-N2-N3-A). We have also partially characterized the Cea-2 gene and two additional ones, Cea-4 and Cea-5. Cea-2 and Cea-4 are separated by only 16 kb, suggesting a close linkage of murine CEA-related genes, as found for the human CEA gene family. Cea-5 was located to the proximal region of mouse Chromosome (Chr) 7, which is syntenic to part of human Chr 19, containing the human CEA gene family cluster. Cea-2, Cea-3, and a Cea-4-1ike gene are differentially transcribed in the placenta during pregnancy, but not in other organs tested. This expression pattern strongly suggests that they represent counterparts of the human PSG subgroup members, despite the presence of multiple IgV-like domains, a feature not found for human PSGs. The more distantly related Cea-5 seems to be ubiquitously expressed. The putative promoter region of Cea-2 lacks typical TATA-or CAAT-boxes, but contains other conserved motifs that could play a role in the initiation of transcription.

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Measurement of Pregnancy-Associated Plasma Proteins during Human Gestation

Abstract: A B S T R AIn the two instances studied, mothers of twins showed abnormally high PAPP levels.

Cited by 175 publications

References 33 publications

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Spatiotemporal expression of pregnancy‐specific glycoprotein gene rnCGM1 in rat placenta

Characterization of murine carcinoembryonic antigen gene family members

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