Spatial and temporal alterations of phospholipids determined by mass spectrometry during mouse embryo implantation

Burnum, Kristin E.; Cornett, Dale S.; Puolitaival, Satu M.; Milne, Stephen; Myers, David S.; Tranguch, Susanne; Brown, H. Alex; Dey, Sudhansu K.; Caprioli, Richard M.

doi:10.1194/jlr.m900100-jlr200

Cited by 146 publications

(154 citation statements)

References 45 publications

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“…The main PE species detected in the samples (PE (38:4) and PE (38:3)) have arachidic and arachidonic acid units in their structures. PE species have been reported as important lipids during early mouse pregnancy and have been colocalized with cyclooxygenase-2, which uses PL as substrates for cellular signaling process [59]. Nonetheless, we have not observed ion abundance changes in PE species during mouse preimplantation development, probably because implantation processes are still not significantly activated.…”

Section: Discussioncontrasting

confidence: 36%

“…Usually, PI species are observed in small abundances in MS imaging of tissues [40,61] and we have also observed small abundances of PI species throughout mouse preimplantation development. Changes in this lipid class have been observed latter in mouse embryo development (uterine implantation) and were related to the presence of angiogenic regions [59]. The impact of in vitro culture conditions (source of protein supplementation in the culture medium and oxygen concentration in the incubator) is well recognized and a focus of active research in embryology [62].…”

Section: Discussionmentioning

confidence: 99%

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Developmental phases of individual mouse preimplantation embryos characterized by lipid signatures using desorption electrospray ionization mass spectrometry

et al. 2012

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Knowledge of the lipids present in individual preimplantation embryos is of interest in fundamental studies of embryology, in attempts to understand cellular pluripotency and in optimization of in vitro culture conditions necessary for the application and development of biotechnologies such as in vitro fertilization and transgenesis. In this work, the profiles of fatty acids and phospholipids (PL) in individual mouse preimplantation embryos and oocytes were acquired using an analytical strategy based on desorption electrospray ionization mass spectrometry (DESI-MS). The methodology avoids sample preparation and provides information on the lipids present in these microscopic structures. Differences in the lipid profiles observed for unfertilized oocytes, two-and four-cell embryos, and blastocysts were characterized. For a representative set of embryos (N= 114) using multivariate analysis (specifically principal component analysis) unfertilized oocytes showed a narrower range of PL species than did blastocysts. Two-and four-cell embryos showed a wide range of PLs compared with unfertilized oocytes and high abundances of fatty acids, indicating pronounced synthetic activity. The data suggest that the lipid changes observed in mouse preimplantation development reflect acquisition of a degree of cellular membrane functional and structural specialization by the blastocyst stage. It is also noteworthy that embryos cultured in vitro from the two-cell through the blastocyst stage have a more homogeneous lipid profile as compared with their in vivo-derived counterparts, which is ascribed to the restricted diversity of nutrients present in synthetic culture media. The DESI-MS data are interpreted from lipid biochemistry and previous reports on gene expression of diverse lipids known to be vital to early embryonic development.

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Section: Discussioncontrasting

confidence: 36%

Section: Discussionmentioning

confidence: 99%

Developmental phases of individual mouse preimplantation embryos characterized by lipid signatures using desorption electrospray ionization mass spectrometry

et al. 2012

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“…There has been increasing interest in the field of lipidomics, which has led to significant research into the analysis and imaging of lipids in tissue sections by MALDI-MS [16,20,24,25,31,34,[46][47][48][49][50][51][52][53][54][55][56][57][58][59]. There is now considerable evidence that lipids are differentially expressed in normal and diseased tissue, and that they may play a central role in the pathologic processes associated with numerous disease states, including diabetes, Alzheimer's and dementia, cancer, heart disease, and numerous metabolic diseases [25,50,52,58,[60][61][62][63][64][65][66][67][68][69].…”

Section: Introductionmentioning

confidence: 99%

Imaging of Phospholipids in Formalin Fixed Rat Brain Sections by Matrix Assisted Laser Desorption/Ionization Mass Spectrometry

Carter

McLeod

Bunch

2011

J. Am. Soc. Mass Spectrom.

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Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is a valuable tool for the analysis of molecules directly from tissue. Imaging of phospholipids is gaining widespread interest, particularly as these lipids have been implicated in a variety of pathologic processes. Formalin fixation (FF) is the standard protocol used in histology laboratories worldwide to preserve tissue for analysis, in order to aid in the diagnosis and prognosis of diseases. This study assesses MALDI imaging of phospholipids directly in formalin fixed tissue, with a view to future analysis of archival tissue. This investigation proves the viability of MALDI-MSI for studying the distribution of lipids directly in formalin fixed tissue, without any pretreatment protocols. High quality molecular images for several phosphatidylcholine (PC) and sphingomyelin (SM) species are presented. Images correspond well with previously published data for the analysis of lipids directly from freshly prepared tissue. Different ionization pathways are observed when analyzing fixed tissue compared with fresh, and this change was found to be associated with formalin buffers employed in fixation protocols. The ability to analyze lipids directly from formalin fixed tissue opens up new doors in the investigation of disease profiles. Pathologic specimens taken for histologic investigation can be analyzed by MALDI-MS to provide greater information on the involvement of lipids in diseased tissue.

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“…(J Am Soc Mass Spectrom 2010, 21, 1922-1929) © 2010 American Society for Mass Spectrometry S ince its inception ϳ10 y ago, MALDI imaging mass spectrometry (imaging MS) has developed into a powerful and versatile tool for biomedical research [1,2]. It is now routinely used for analyzing peptides and small proteins up to 25 kDa [3-6], administered drugs and their metabolites [7], and recently major improvements have been reported for lipids [8]. Despite this success, proteins exceeding 25 kDa are not routinely detected.…”

mentioning

confidence: 99%

“…It is now routinely used for analyzing peptides and small proteins up to 25 kDa [3][4][5][6], administered drugs and their metabolites [7], and recently major improvements have been reported for lipids [8]. Despite this success, proteins exceeding 25 kDa are not routinely detected.…”

mentioning

confidence: 99%

MALDI imaging and profiling MS of higher mass proteins from tissue

Remoortere

Zeijl

Oever

et al. 2010

J. Am. Soc. Mass Spectrom.

111

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MALDI imaging and profiling mass spectrometry of proteins typically leads to the detection of a large number of peptides and small proteins but is much less successful for larger proteins: most ion signals correspond to proteins of m/z Ͻ 25,000. This is a severe limitation as many proteins, including cytokines, growth factors, enzymes, and receptors have molecular weights exceeding 25 kDa. The detector technology typically used for protein imaging, a microchannel plate, is not well suited to the detection of high m/z ions and is prone to detector saturation when analyzing complex mixtures. Here we report increased sensitivity for higher mass proteins by using the CovalX high mass HM1 detector (Zurich, Switzerland), which has been specifically designed for the detection of high mass ions and which is much less prone to detector saturation. The results demonstrate that a range of different sample preparation strategies enable higher mass proteins to be analyzed if the detector technology maintains high detection efficiency throughout the mass range. The detector enables proteins up to 70 kDa to be imaged, and proteins up to 110 kDa to be detected, directly from tissue, and indicates new directions by which the mass range amenable to MALDI imaging MS and MALDI profiling MS may be extended. (J Am Soc Mass Spectrom 2010, 21, 1922-1929) © 2010 American Society for Mass Spectrometry S ince its inception ϳ10 y ago, MALDI imaging mass spectrometry (imaging MS) has developed into a powerful and versatile tool for biomedical research [1,2]. It is now routinely used for analyzing peptides and small proteins up to 25 kDa [3-6], administered drugs and their metabolites [7], and recently major improvements have been reported for lipids [8]. Despite this success, proteins exceeding 25 kDa are not routinely detected. Proteins larger than 25 kDa include many proteins with important biological activities, such as most cytokines, growth factors, enzymes, receptors, proproteins, and neuropeptide precursors. Increasing the mass range of proteins amenable to MALDI imaging MS might enable these biologically crucial proteins to be included in current applications, e.g., biomarker discovery.The most common technique currently used to access larger proteins in MALDI imaging MS analyses is based on proteolytic digestion of the tissue's proteins followed by MALDI imaging MS of their tryptic peptides. Note on-tissue digestion has the additional advantage that it can be applied to formalin fixed tissues as proteolytic peptides can be generated that are not bound within the cross-linked protein matrix. For example, Djidja et al. used on-tissue digestion to determine that the 78 kDa protein GRP78 may be a new candidate protein biomarker of pancreatic adenocarcinoma [9]. In principal, this 'bottom-up' strategy could enable proteins of any mass to be detected. In practice the large increase in complexity associated with proteolysing the entire tissue's protein content will cause many tryptic peptides to have identical nominal mass [1], thus under...

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Spatial and temporal alterations of phospholipids determined by mass spectrometry during mouse embryo implantation

Cited by 146 publications

References 45 publications

Developmental phases of individual mouse preimplantation embryos characterized by lipid signatures using desorption electrospray ionization mass spectrometry

Developmental phases of individual mouse preimplantation embryos characterized by lipid signatures using desorption electrospray ionization mass spectrometry

Imaging of Phospholipids in Formalin Fixed Rat Brain Sections by Matrix Assisted Laser Desorption/Ionization Mass Spectrometry

MALDI imaging and profiling MS of higher mass proteins from tissue

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