The role of proteomics in the assessment of premature rupture of fetal membranes

Thadikkaran, Lynne; Crettaz, David; Siegenthaler, Michèle A.; Gallot, Denis; Sapin, Vincent; Iozzo, Renato V.; Queloz, Pierre-Alain; Schneider, Philippe; Tissot, Jean‐Daniel

doi:10.1016/j.cccn.2005.04.018

Cited by 60 publications

(42 citation statements)

References 72 publications

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“…To identify potential AF markers (present only in AF but absent in maternal blood) for early detection of PROM, a 2-DE/MS approach was used to compare plasma and AF samples collected from women at terms. Two basement membrane-specific heparan sulfate proteoglycan proteins, perlecan and agrin, were found present in AF while they were absent from plasma samples of pregnant women [449,450]. Presence of intra-amniotic infection (IAI) is often associated with preterm birth and adverse neonatal sequelae.…”

Section: Amniotic Fluid (Af)mentioning

confidence: 99%

Human body fluid proteome analysis

2006

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The focus of this article is to review the recent advances in proteome analysis of human body fluids, including plasma/serum, urine, cerebrospinal fluid, saliva, bronchoalveolar lavage fluid, synovial fluid, nipple aspirate fluid, tear fluid, and amniotic fluid, as well as its applications to human disease biomarker discovery. We aim to summarize the proteomics technologies currently used for global identification and quantification of body fluid proteins, and elaborate the putative biomarkers discovered for a variety of human diseases through human body fluid proteome (HBFP) analysis. Some critical concerns and perspectives in this emerging field are also discussed. With the advances made in proteomics technologies, the impact of HBFP analysis in the search for clinically relevant disease biomarkers would be realized in the future.

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Section: Amniotic Fluid (Af)mentioning

confidence: 99%

Human body fluid proteome analysis

2006

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“…Consequently many putative markers for such anomalies as premature rupture of amnion, intra-amniotic infection, and Down syndrome have been reanalyzed or newly discovered (2)(3)(4). However, none of these biomarkers have a high enough individual detection rate to be used on their own.…”

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confidence: 99%

Proteomics Analysis of Human Amniotic Fluid

Cho

Shan

Winsor

et al. 2007

Molecular & Cellular Proteomics

158

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Amniotic fluid is a dynamic and complex mixture that reflects the physiological status of the developing fetus. In this study, the human amniotic fluid (AF) proteome of a 16 -18-week normal pregnancy was profiled and analyzed to investigate the composition and functions of this fluid. Due to the complexity of AF, we utilized three different fractionation strategies to provide greater coverage. Two types of two-dimensional LC/MS/MS as well as an LC-SDS-PAGE-LC-MS/MS platform were used. A total of 16 AF samples between gestational ages of 16 and 18 weeks from women carrying chromosomally normal fetuses were analyzed by one of the three fractionation methods followed by a common reverse phase LC-MS/MS step. Mascot and The Global Proteome Machine engines were used to search the International Protein Index human database for peptide sequence identification. The list of proteins was generated by combining the results of both engines through the PeptideProphet of Scaffold software. All identified proteins were combined to generate the AF proteome comprising 1,026 unique gene matches or 842 non-redundant proteins. This list includes most of the currently used biomarkers for pregnancy-associated pathologic conditions such as preterm delivery, intra-amniotic infection, and chromosomal anomalies of the fetus. The subcellular localization, tissue expression, functions, and networks of the AF proteome were analyzed by various bioinformatic tools. These data will contribute to the better understanding of amniotic fluid function and to the discovery of novel biomarkers for prenatal diagnosis of fetal abnormalities.

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“…6,12 The growing number of reports identifying LG3 in nearly all body fluids, including urine, blood, and amniotic fluid, further strengthen the concept of an endogenous role for endorepellin LG3 in regulating angiogenesis and perhaps other biologic processes. [13][14][15] Many cellular processes such as survival, proliferation, differentiation, and migration are governed by RTK signaling. On binding with their specific ligand, RTKs dimerize and become autophosphorylated on multiple sites.…”

Section: Introductionmentioning

confidence: 99%

Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin angiostatic activity

Nyström

Shaik

Gullberg

et al. 2009

Blood

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Endorepellin, the C-terminal domain of perlecan, is a powerful angiogenesis inhibitor. To dissect the mechanism of endorepellin-mediated endothelial silencing, we used an antibody array against multiple tyrosine kinase receptors. Endorepellin caused a widespread reduction in phosphorylation of key receptors involved in angiogenesis and a concurrent increase in phosphatase activity in endothelial cells and tumor xenografts. These effects were efficiently hampered by function-blocking antibodies against integrin ␣2␤1, the functional endorepellin receptor. The Src homology-2 protein phosphatase-1 (SHP-1) coprecipitated with integrin ␣2 and was phosphorylated in a dynamic fashion after endorepellin stimulation. Genetic evidence was provided by lack of an endorepellin-evoked phosphatase response in microvascular endothelial cells derived from integrin ␣2␤1 ؊/؊ mice and by response to endorepellin in cells genetically engineered to express the ␣2␤1 integrin, but not in cells either lacking this receptor or expressing a chimera harboring the integrin ␣2 ectodomain fused to the ␣1 intracellular domain. siRNA-mediated knockdown of integrin ␣2 caused a dose-dependent reduction of SHP-1. Finally, the levels of SHP-1 and its enzymatic activity were substantially reduced in multiple organs from ␣2␤1 ؊/؊ mice. Our results show that SHP-1 is an essential mediator of endorepellin activity and discover a novel functional interaction between the integrin ␣2 subunit and SHP-1. (Blood. 2009; 114:4897-4906) IntroductionThe development and maintenance of an efficient vascular system is vital for organ function and health in all higher organisms. Angiogenesis is abundant during fetal development but in the adult is a rare process mainly restricted to the female reproductive cycle and wound healing. However, deregulated angiogenesis is a prominent factor in many major diseases such as cancer, diabetes, and ischemia occurring after stroke. Controlled angiogenesis is achieved by interplay of proangiogenic and antiangiogenic factors. Proangiogenic growth factors, such as vascular endothelial growth factor (VEGF), signal by their respective receptor tyrosine kinase (RTK) to stimulate endothelial cell migration and proliferation, whereas angiogenic inhibitors counteract these actions. 1 The list of reported negative regulators of angiogenesis is long, ever growing, and truly versatile. Nevertheless, a common theme for many of them is that they are derived from limited proteolysis of extracellular matrix components and that they interact with integrin receptors. 2 The angiostatic protein endorepellin, located within the C-terminus of the heparan sulfate proteoglycan perlecan, consists of 3 laminin globular (LG1-3) domains separated by 4 epidermal growth factor-like repeats. 3 Endorepellin exerts its activity by a noncanonical cation-independent binding of the LG3 domain to the ␣2 I domain of the integrin ␣2␤1, 4-7 a key receptor regulating angiogenesis. [8][9][10] This triggers a signaling cascade that leads to endothelial cell immobilizatio...

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The role of proteomics in the assessment of premature rupture of fetal membranes

Cited by 60 publications

References 72 publications

Human body fluid proteome analysis

Human body fluid proteome analysis

Proteomics Analysis of Human Amniotic Fluid

Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin angiostatic activity

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