Analysis of expression and comparative profile of normal placental tissue proteins and those in preeclampsia patients using proteomic approaches

Jin, Hong; Ma, Kaidong; Hu, Rong; Chen, Yan; Yang, Fengying; Yao, Jun; Li, Xiaotian; Yang, Pengyuan

doi:10.1016/j.aca.2008.09.015

Cited by 26 publications

(21 citation statements)

References 21 publications

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“…These differentially expressed proteins included signal transduction protein, cell skeleton protein and molecular chaperon protein, with Hsp27 upregulated among these differentially expressed proteins. Jin et al [4] identified an increased expression of Hsp27 by a proteomic technique in human preeclamptic tissue and said that further study on Hsp27 phosphorylation modification in the preeclampsia placenta is needed to reveal the function of cell apoptosis.…”

Section: Discussionmentioning

confidence: 99%

“…Two-dimensional electrophoresis (2-DE) and matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS) analysis can provide useful information for understanding the pattern of the peptide and protein profiles from extracted placental tissues. Recent proteomic studies have identified Hsp27 as a highly overexpressed protein in preeclamptic placental tissues [4]. …”

Section: Introductionmentioning

confidence: 99%

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Proteomic Analysis Reveals an Elevated Expression of Heat Shock Protein 27 in Preeclamptic Placentas

Shin¹,

Baek²,

Kang

et al. 2011

Gynecol Obstet Invest

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Aim: The purpose of this study was to identify the placental proteins that are associated with preeclampsia by performing proteomic analysis. Methods: To identify the proteins associated with preeclampsia, we performed two-dimensional electrophoresis (2-DE), followed by silver staining. The overexpressed proteins were identified by performing matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS), followed by peptide mass fingerprinting, a protein database search and Western blot analysis. Immunohistochemical staining was performed to determine the localization of the overexpressed Hsp27. Results: By use of 2-DE and MALDI-TOF-MS analysis, twelve differentially expressed proteins were identified, of which four proteins were upregulated and eight proteins were downregulated. One of the upregulated spots was identified as Hsp27. Immunohistochemical analysis showed that Hsp27 was mainly located in the trophoblasts. The Western blot analysis showed that the expression of Hsp27 in the tissues of the preeclampsia placenta was significantly increased. Conclusions: Our study confirmed that four proteins are upregulated and eight proteins are downregulated in preeclampsia. These differentially expressed proteins include signal transduction protein and molecular chaperon protein, in which Hsp27 is upregulated. We suggest that the increased expression level of Hsp27 might be correlated with the pathophysiology of preeclampsia.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis Reveals an Elevated Expression of Heat Shock Protein 27 in Preeclamptic Placentas

Shin¹,

Baek²,

Kang

et al. 2011

Gynecol Obstet Invest

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“…9 Up to now, only a few proteomic studies have been performed on the placental tissue or cell lines and the relationship between the placental proteome changes and pregnancy-related disorders, such as pregnancy loss and preeclampsia. 8,[10][11][12][13][14][15][16][17] Considering the scarcity of the published studies on the proteome changes during fetus development, the present study aimed to compare the total placental proteome differences between the normal first-and third-trimester human placentas. In order to fulfill this goal, placental proteins from normal first-and third-trimester human placentas were extracted and subjected to 2D-PAGE.…”

Section: Introductionmentioning

confidence: 99%

Proteome Differences in the First- and Third-Trimester Human Placentas

2015

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Placenta is a transient and unique pregnancy tissue that supports the fetus nutritionally and metabolically. Expression of the unique placental proteins in different stages may influence the development of the fetus as well as the pregnancy outcome. The present study aimed to compare the total placental proteome differences between the normal first-and third-trimester human placentas. In the current study, placental proteome was compared between normal first-and third-trimester placentas using 2-dimensional polyacrylamide gel electrophoresis method for separation and matrix-assisted laser desorption/ionization time-of flight mass spectrometry technique for identification of the proteins. Despite the overall similarities, comparison of the mean intensity of the protein spots between the first-and third-trimester placental proteomes revealed that 22 spots were differentially expressed (P < .05) among which 11 distinct spots were successfully identified. Of the 11 differentially expressed proteins, 4 were increased (protein disulfide isomerase, tropomyosin 4 isoform 2, enolase 1, and 78-kDa glucose-regulated protein), while the remaining 7 (actin g1 propeptide, heat shock protein gp96, a1-antitrypsin, EF-hand domain family member D1, tubulin a1, glutathione S-transferase, and vitamin D binding protein) showed decreased expression in the placentas from the first-trimester compared to the full-term ones. In summary, the results of the present study as the first research on the comparison of the first-and thirdtrimester human placental proteomes introduced a group of 11 proteins with altered expression. Interestingly, some of these proteins are reported to be altered in pregnancy-related disorders.

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“…This should be viewed in light of a loss of the major Mg-and Ca-binding proteins (60)(61)(62)(63)(64), which would result in elevation of the percent serum ionized Mg, as found in our study for normal late pregnancy (Table 1). Recently, several studies, using proteomics, have reported scores of other serum proteins, which were found to be up-regulated in preeclamptic women (70,71), thus potentially supplying additional ion-binding sites. Thus, the interesting finding, reported herein, of a reduced percentage of serum ionized Mg in Mg-treated preeclamptic women, that cannot be explained by a loss of serum albumin, transferrin, and hemopexin, but could be viewed in the light of a reported increase in other serum proteins (i.e., globulins, alpha 2 -glycoproteins, alpha 2 -macroglobulins, beta-lipoproteins, and various complement fractions in preeclamptic women) (64,66,67,72), which can potentially bind free Mg ions.…”

Section: Figurementioning

confidence: 98%

“…73). A host of placental proteins, which gain access to the serum of preeclamptic women, have been detected (71), which may bind Mg and Ca. Thus these proteins could be an additional source for the decreased ionized Mg in the blood of preeclamptic women over and above that of normal pregnancy.…”

Section: Figurementioning

confidence: 99%

Cerebral spinal fluid and serum ionized magnesium and calcium levels in preeclamptic women during administration of magnesium sulfate

Apostol

Apostol²,

Али

et al. 2010

Fertility and Sterility

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Analysis of expression and comparative profile of normal placental tissue proteins and those in preeclampsia patients using proteomic approaches

Cited by 26 publications

References 21 publications

Proteomic Analysis Reveals an Elevated Expression of Heat Shock Protein 27 in Preeclamptic Placentas

Proteomic Analysis Reveals an Elevated Expression of Heat Shock Protein 27 in Preeclamptic Placentas

Proteome Differences in the First- and Third-Trimester Human Placentas

Cerebral spinal fluid and serum ionized magnesium and calcium levels in preeclamptic women during administration of magnesium sulfate

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