Trophoblast calcyclin is elevated in placental tissue from patients with early pre-eclampsia

Schol, Pim B.B.; Güzel, Coşkun; Steegers, Eric A.P.; Krijger, Ronald R. de; Luider, Theo M.

doi:10.1016/j.preghy.2013.11.003

Cited by 5 publications

(7 citation statements)

References 12 publications

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“…The finding that a significant decrease was observed of S100A6 levels in the second trimester of PE patients was remarkable and suggests that S100A6 is involved in the pathophysiology of PE as was already observed previously in placental tissue . In placental tissue, we observed that S100A6 was higher abundant in patients with PE.…”

Section: Discussionsupporting

confidence: 87%

“…The numbers of placenta tissue analyzed in this study ( n = 5 in each group) were too small to report information whether HSP90 was upregulated in PE. In case of S100A6 , we reported previously that S100A6 was elevated in a larger cohort ( n = 138) …”

Section: Discussionmentioning

confidence: 69%

“…Previously, we reported significantly discriminating peptide patterns between trophoblast and stroma cells by laser capture microdissection (LCM) . We also demonstrated by immunohistochemistry that S100A6 was significantly more abundant in placentas of preeclamptic women as compared to controls . By multiple reaction monitoring (also known as SRM) we showed significantly elevated levels of S100A6 in formalin‐fixed paraffin‐embedded (FFPE) preeclamptic placentas compared to controls by LCM .…”

Section: Introductionmentioning

confidence: 71%

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Quantification of Calcyclin and Heat Shock Protein 90 in Sera from Women with and without Preeclampsia by Mass Spectrometry

Güzel

Berg

Duvekot

et al. 2018

Proteomics Clinical Apps

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Purpose The objective of present study is to determine serum levels and placental distribution of two interacting proteins calcyclin and heat shock protein 90 in preeclampsia. Experimental design Maternal serum levels of calcyclin and heat shock protein 90 are compared throughout pregnancy from the first trimester till term among women with preeclampsia (n = 43) and age‐matched normotensive pregnant controls (n = 46). A serum‐based 2D LC‐MS assay using Parallel Reaction Monitoring is applied to quantify both calcyclin and heat shock protein 90. Results Serum levels of calcyclin are significantly lower in patients with preeclampsia in the second trimester of pregnancy as compared to controls (p < 0.05). Serum levels of heat shock protein 90 are significantly higher in patients with preeclampsia in the third trimester as compared to controls (p < 0.001). Conclusion and clinical relevance Both interacting proteins calcyclin and heat shock protein 90 are notably changed in preeclamptic patients compared to controls. Calcyclin is already decreased before the onset of preeclampsia in the second trimester and HSP90 is strongly increased in the third trimester. This suggests that these proteins may play a role in the pathogenesis of preeclampsia and ought to be investigated in large cohort studies as molecular biomarkers.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 69%

Section: Introductionmentioning

confidence: 71%

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Quantification of Calcyclin and Heat Shock Protein 90 in Sera from Women with and without Preeclampsia by Mass Spectrometry

Güzel

Berg

Duvekot

et al. 2018

Proteomics Clinical Apps

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“…Schol et al investigated biomarker potential of calcyclin in formalin-fixed and paraffin-embedded placental tissue collected from 75 women with pre-eclampsia and the same number of healthy controls who delivered between 20 and 34 weeks of gestation. IHC analysis showed a significantly more intense staining of calcyclin in the trophoblasts from women with pre-eclampsia compared to healthy controls [ 73 ]. Determining expression of trophoblasts’ calcyclin early in pregnancy could be useful to investigate its role in the pathogenesis of pre-eclampsia.…”

Section: Introductionmentioning

confidence: 99%

Elucidating the Pathogenesis of Pre-eclampsia Using In Vitro Models of Spiral Uterine Artery Remodelling

et al. 2017

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Purpose of ReviewThe aim of the study is to perform a critical assessment of in vitro models of pre-eclampsia using complementary human and cell line-based studies. Molecular mechanisms involved in spiral uterine artery (SUA) remodelling and trophoblast functionality will also be discussed.Recent FindingsA number of proteins and microRNAs have been implicated as key in SUA remodelling, which could be explored as early biomarkers or therapeutic targets for prevention of pre-eclampsia.SummaryVarious 2D and 3D in vitro models involving trophoblast cells, endothelial cells, immune cells and placental tissue were discussed to elucidate the pathogenesis of pre-eclampsia. Nevertheless, pre-eclampsia is a multifactorial disease, and the mechanisms involved in its pathogenesis are complex and still largely unknown. Further studies are required to provide better understanding of the key processes leading to inappropriate placental development which is the root cause of pre-eclampsia. This new knowledge could identify novel biomarkers and treatment strategies.

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“…Calcyclin (S100-A6), a member of the S100 family of Ca 2ϩ -binding proteins that are highly homologous to acidic calcium-binding proteins containing two EF-hand motifs. Calcyclin is elevated in trophoblasts cells in pre-eclamptic placenta (21,22). Pre-eclampsia is a disease with high protein concentrations in urine and high blood pressure, resulting in a high mortality and morbidity in pregnant women.…”

Section: Discussionmentioning

confidence: 99%

Identifying Ca2+-Binding Sites in Proteins by Liquid Chromatography-Mass Spectrometry Using Ca2+-Directed Dissociations

Jamalian

Sneekes

Wienk

et al. 2014

Molecular & Cellular Proteomics

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Here we describe a new method to identify calcium-binding sites in proteins using high-resolution liquid chromatography-mass spectrometry in concert with calcium-directed collision-induced dissociations. Our method does not require any modifications to the liquid chromatography-mass spectrometry apparatus, uses standard digestion protocols, and can be applied to existing high-resolution MS data files. In contrast to NMR, our method is applicable to very small amounts of complex protein mixtures (femtomole level). Calcium-bound peptides can be identified using three criteria: (1) the calculated exact mass of the calcium containing peptide; (2) specific dissociations of the calcium-containing peptide from threonine and serine residues; and ( Calcium-dependent protein interactions mostly organized in protein networks are responsible for the regulation of cell cycle progression, cell growth, differentiation, secretion, and cytoskeletal organization (1-3). As many of these proteins are linked to various pathological conditions, they are clinically important. The speed at which calcium can have an interplay between various cellular components is impressive and comes notably detectable in neurological processes and in muscle contraction. Calcium binding sites in proteins can be determined by NMR spectroscopy (4, 5). For example, by such NMR measurements, the Ca 2ϩ -binding sites of the tellurite-resistance protein TerD from Klebsiella pneumoniae were found to be formed in part by a highly conserved motif of 13 residues specified by the sequence GDN(R/L)TG(E/A)GDGDDE (4).Although NMR is the gold standard to study calcium binding in proteins, this approach has several drawbacks. For instance, protein size is limited (Ͻ 30 kDa) and proteins should be pure and isotopically labeled. In addition, although the information content is high, NMR is relatively insensitive compared with other techniques such as MS and fluorescence spectroscopy, and relatively large quantities of material (typically 0.5 ml at 0.5-1.0 mM in biological samples) are needed, although efforts are devoted to improve sensitivity in NMR, such as stripline NMR (6).In bottom-up proteomics, proteolytic peptides, generated by enzymatic digestion of complex protein mixtures, are sequenced by MS-based methods (MS/MS (7, 8)) using collision-induced dissociations. Because of the even higher complexity of these peptide mixtures, liquid chromatography (LC) 1 is used to separate the peptides prior to sequencing. In such an LC-MS/MS procedure, many peptides can be identified belonging to the same protein. It has been stated (9) that by this procedure more peptides are analyzed than strictly necessary for identification purposes, but it can equally well be argued that such large coverages enable more reliable protein identifications; moreover, these larger coverages allow the detection of post-translational modifications, including specific calcium complexation as described here.Considering the need of identifying calcium-bound proteins in complex biological samples at...

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Trophoblast calcyclin is elevated in placental tissue from patients with early pre-eclampsia

Cited by 5 publications

References 12 publications

Quantification of Calcyclin and Heat Shock Protein 90 in Sera from Women with and without Preeclampsia by Mass Spectrometry

Quantification of Calcyclin and Heat Shock Protein 90 in Sera from Women with and without Preeclampsia by Mass Spectrometry

Elucidating the Pathogenesis of Pre-eclampsia Using In Vitro Models of Spiral Uterine Artery Remodelling

Identifying Ca2+-Binding Sites in Proteins by Liquid Chromatography-Mass Spectrometry Using Ca2+-Directed Dissociations

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