Analysis of Differential Expression Proteins from Different Parts of Pistillate Flower in Mulberry (Morus alba)

2013 ◽  
Vol 796 ◽  
pp. 62-66
Author(s):  
Rui He Niu ◽  
Yuan Yuan Chen ◽  
Chi Chen ◽  
Bi Ping Zheng ◽  
Jian Zhong Tan
Keyword(s):  
Mass Spectrometry ◽  
Differential Expression ◽  
Pistillate Flower ◽  
Membrane Lipid ◽  
Mass Spectrometry Analysis ◽  
Specific Expression ◽  
Spectrometry Analysis ◽  
Software Analysis ◽  
Regulated Expression ◽  
Protein Components

Fruit mulberry cultivation has become a new field of modern sericulture, and quite a number of studies were focused on the growth and development of mulberry flowers and fruits. In order to explore the molecular mechanism of development and regulation of mulberry pistillate flower, the total protein were extracted from the flowering style (with the stigma) and ovary with fruit mulberry variety "Da 10" as materials, separated by two-dimensional electrophoresis and identified by mass spectrometry. The results showed that there were significant differential expressions in different tissues, and 20 proteins with specific expression were detected in the style of pistillate flower. By mass spectrometry analysis, database retrieval and bioinformatics software analysis, these protein components were given functional annotation, mainly related to the biosynthetic metabolism of protein and flavonoid, stress response and redox reaction. Additionally, glucan endo-1,3-beta-glucosidase involved in cell wall metabolism was detected to be up-regulated expression and lipoxygenase participating in membrane lipid oxidation reaction was detected to be down-regulated expression in the style compared with that in the ovary. It illustrated that the differential expression of these proteins in style were closely related to pollen germination, pollen tube growth or intrusion of other xenobiotics.

Calculation of Membrane Lipid Ratios Using Single-Pixel Time-of-Flight Secondary Ion Mass Spectrometry Analysis

2015 ◽  
Vol 87 (15) ◽  
pp. 7795-7802 ◽  
Author(s):  
Rainer Kassenböhmer ◽  
Felix Draude ◽  
Martin Körsgen ◽  
Andreas Pelster ◽  
Heinrich F. Arlinghaus
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Time Of Flight ◽  
Membrane Lipid ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Lipid Ratios ◽  
Ion Mass Spectrometry ◽  
Secondary Ion ◽  
Single Pixel

scholarly journals Mass spectrometry analysis of mouse hematopoietic stem cells and their progenitors reveals differential expression within and between proteome and transcriptome throughout adult and aged hematopoiesis

2019 ◽  
Author(s):  
Balyn W. Zaro ◽  
Joseph J. Noh ◽  
Victoria L. Mascetti ◽  
Janos Demeter ◽  
Benson M. George ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stem Cells ◽  
Protein Expression ◽  
Hematopoietic Stem Cells ◽  
Differential Expression ◽  
Cell Types ◽  
Mass Spectrometry Analysis ◽  
Hematopoietic Stem ◽  
Spectrometry Analysis ◽  
Mass Spectrometry Technology

SummaryHematopoietic stem cells (HSCs) are responsible for the generation of blood and immune cells throughout life. They have the unique ability to self-renew and generate more HSCs or differentiate into a progenitor cell in response to cell-intrinsic and -extrinsic stimuli. The balance of HSC fate commitment is critical for a healthy blood supply. Imbalances during hematopoiesis, which are frequent in aging, can result in hematological malignancies and pre-malignancies as well as increase risk of atherosclerosis. Given the importance of HSCs and their progenitors, they have been extensively characterized in genomic and transcriptomic studies. However, an understanding of protein expression within the HSC compartment and more broadly throughout hematopoiesis remains poorly understood, and it has been widely reported that the correlation between mRNA and proteins is more complicated than previously thought. Previous mouse mass spectrometry studies have focused either specifically on stem and the first early progenitor or broadly across mixed populations of stem and progenitor cells, which do not allow for cell-type specific protein resolution across stages of differentiation. Mass cytometry has been employed to characterize transcription factor expression in human HSCs and progenitors but does not apply an unbiased discovery approach. New mass spectrometry technology now allows for deep proteomic coverage with no more than 200 ng of sample input. We report here a proteomics resource characterizing protein expression in mouse adult and aged HSCs, multipotent progenitors and oligopotent progenitors, 12 cell types in total. We validated differential expression by flow cytometry analysis and immunofluorescence staining. Additionally, we investigated the relationship between mRNA and protein levels of individual genes in HSCs compared to progenitors through RNA sequencing studies and identified two proteins that appear to be uniquely regulated in the HSC compartment, Cpin1 and Adnp. In summary, this resource provides proteomic coverage of adult and aged hematopoietic stem cells and their progenitors and reveals changes in protein abundance between cell types, with potential future implications in understanding mechanisms for stem-cell maintenance, niche interactions and fate determination.

scholarly journals Effect of Ocular Hypertension on D-β-Aspartic Acid-Containing Proteins in the Retinas of Rats

2019 ◽  
Vol 2019 ◽  
pp. 1-8 ◽  
Author(s):  
Takashi Kanamoto ◽  
Takashi Tachibana ◽  
Yasushi Kitaoka ◽  
Toshio Hisatomi ◽  
Yasuhiro Ikeda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ocular Hypertension ◽  
Aspartic Acid ◽  
Atp Synthase ◽  
Wistar Rats ◽  
Protein Band ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Spectrometry Analysis ◽  
Sds Page

Purpose. To investigate the effect of ocular hypertension-induced isomerization of aspartic acid in retinal proteins. Methods. Adult Wistar rats with ocular hypertension were used as an experimental model. D-β-aspartic acid-containing proteins were isolated by SDS-PAGE and western blot with an anti-D-β-aspartic acid antibody and identified by liquid chromatography-mass spectrometry analysis. The concentration of ATP was measured by ELISA. Results. D-β-aspartic acid was expressed in a protein band at around 44.5 kDa at much higher quantities in the retinas of rats with ocular hypertension than in those of normotensive rats. The 44.5 kDa protein band was mainly composed of α-enolase, S-arrestin, and ATP synthase subunits α and β, in both the ocular hypertensive and normotensive retinas. Moreover, increasing intraocular pressure was correlated with increasing ATP concentrations in the retinas of rats. Conclusion. Ocular hypertension affected the expression of proteins containing D-β-aspartic acid, including ATP synthase subunits, and up-regulation of ATP in the retinas of rats.

scholarly journals N-Terminomics Strategies for Protease Substrates Profiling

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4699
Author(s):  
Mubashir Mintoo ◽  
Amritangshu Chakravarty ◽  
Ronak Tilvawala
Keyword(s):  
Mass Spectrometry ◽  
Protease Activity ◽  
Viral Infections ◽  
Mass Spectrometry Analysis ◽  
Post Translational Modification ◽  
Spectrometry Analysis ◽  
Physiological Conditions ◽  
Inflammatory Conditions ◽  
Biological Mixtures

Proteases play a central role in various biochemical pathways catalyzing and regulating key biological events. Proteases catalyze an irreversible post-translational modification called proteolysis by hydrolyzing peptide bonds in proteins. Given the destructive potential of proteolysis, protease activity is tightly regulated. Dysregulation of protease activity has been reported in numerous disease conditions, including cancers, neurodegenerative diseases, inflammatory conditions, cardiovascular diseases, and viral infections. The proteolytic profile of a cell, tissue, or organ is governed by protease activation, activity, and substrate specificity. Thus, identifying protease substrates and proteolytic events under physiological conditions can provide crucial information about how the change in protease regulation can alter the cellular proteolytic landscape. In recent years, mass spectrometry-based techniques called N-terminomics have become instrumental in identifying protease substrates from complex biological mixtures. N-terminomics employs the labeling and enrichment of native and neo-N-termini peptides, generated upon proteolysis followed by mass spectrometry analysis allowing protease substrate profiling directly from biological samples. In this review, we provide a brief overview of N-terminomics techniques, focusing on their strengths, weaknesses, limitations, and providing specific examples where they were successfully employed to identify protease substrates in vivo and under physiological conditions. In addition, we explore the current trends in the protease field and the potential for future developments.

Sign in / Sign up

Export Citation Format

Share Document