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Comparative Proteomic Analysis of Rana Chensinensis Oviduct

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Comparative Proteomic Analysis of Rana Chensinensis Oviduct molecules Article Comparative Proteomic Analysis of Rana chensinensis Oviduct Hang Su 1, He Zhang 2,*, Xinghua Wei 3, Daian Pan 2, Li Jing 1, Daqing Zhao 4, Yu Zhao 4 and Bin Qi 5,* 1 Practice Innovations Center, Changchun University of Chinese Medicine, Changchun 130117, China; [email protected] (H.S.); [email protected] (L.J.) 2 School of Clinical Medicine, Changchun University of Chinese Medicine, Changchun 130117, China; [email protected] (D.P.) 3 Jilin Science Service Center, Changchun 130021, China; [email protected] 4 Jilin Ginseng Academy, Changchun University of Chinese Medicine, Changchun 130117, China; [email protected] (D.Z.); [email protected] (Y.Z.) 5 College of Pharmacy, Changchun University of Chinese Medicine, Changchun 130117, China * Correspondence: [email protected] (H.Z); [email protected] (B.Q.) Received: 8 March 2018; Accepted: 5 June 2018; Published: 8 June 2018 Abstract: As one of most important traditional Chinese medicine resources, the oviduct of female Rana chensinensis (Chinese brown frog) was widely used in the treatment of asthenia after sickness or delivery, deficiency in vigor, palpitation, and insomnia. Unlike other vertebrates, the oviduct of Rana chensinensis oviduct significantly expands during prehibernation, in contrast to the breeding period. To explain this phenomenon at the molecular level, the protein expression profiles of Rana chensinensis oviduct during the breeding period and prehibernation were observed using isobaric tags for relative and absolute quantitation (iTRAQ) technique. Then, all identified proteins were used to obtain gene ontology (GO) annotation. Ultimately, KEGG (Kyoto Encyclopedia of Genes and Genomes) enrichment analysis was performed to predict the pathway on differentially expressed proteins (DEPs). A total of 4479 proteins were identified, and 312 of them presented different expression profiling between prehibernation and breeding period. Compared with prehibernation group, 86 proteins were upregulated, and 226 proteins were downregulated in breeding period. After KEGG enrichment analysis, 163 DEPs were involved in 6 pathways, which were lysosome, RNA transport, glycosaminoglycan degradation, extracellular matrix (ECM)–receptor interaction, metabolic pathways and focal adhesion. This is the first report on the protein profiling of Rana chensinensis oviduct during the breeding period and prehibernation. Results show that this distinctive physiological phenomenon of Rana chensinensis oviduct was mainly involved in ECM–receptor interaction, metabolic pathways, and focal adhesion. Keywords: iTRAQ; proteomics; Rana chensinensis oviduct; regulation; differentially expressed proteins 1. Introduction The oviduct is a reproductive organ of females, which plays several important roles in the events related to fertilization and embryo development. The oviduct is not only a passive channel for sperm and eggs transport, but is also a highly active secretory organ, such as estrous cycle and ovulation [1]. It provides the most efficient environment for the success of fertilization and early embryo development [2,3]. The component of oviduct of Rana chensinensis is rich in glands, including glycoprotein (such as mucins, collagen, enzymes, and hormones, etc.) and lipoprotein [4]. The dry oviduct of female Rana chensinensis, which is recorded in the Chinese Pharmacopoeia, possesses the function of improving immune system and lung function [5]. Molecules 2018, 23, 1384; doi:10.3390/molecules23061384 www.mdpi.com/journal/molecules MoleculesMolecules2018 2018, 23, 23, 1384, x 22 of of 14 14 The hibernation for Rana chensinensis ranges from October to February next year, followed by the Thebreeding hibernation period from for Rana February chensinensis to June.ranges After fromthe breeding October period, to February Rana chensinensis next year, followed goes into bythe theprehibernation breeding period period from until February October to June.[6]. Distin Afterguishing the breeding from period,the oviducRanat chensinensisexpansion duringgoes into the thebreeding prehibernation period in period other species, until October a unique [6]. physiological Distinguishing phenomenon from the oviduct of Rana expansion chensinensis during is that the its breedingoviduct periodstarts to in expand other species, after breeding, a unique reaching physiological a peak phenomenon by October ofduringRana the chensinensis prehibernationis that its[7]. oviductFor this starts reason, to Rana expand chensinensis after breeding, oviduct, reaching as traditional a peak Chinese by October medicine, during was the collected prehibernation from frog [7 ].in Forthe this autumn reason, beforeRana hibernation. chensinensis Tooviduct, ascertain as traditional the signaling Chinese pathways medicine, involved was in collected the timing from of frogoviduct in theexpansion, autumn beforewe should hibernation. clarify the To ascertainchanges theof ma signalingcromolecular pathways components involved inbetween the timing prehibernation of oviduct expansion,and breeding we shouldperiod. clarifyProteomics the changes is an efficient of macromolecular methodology components to analyze prot betweenein expression, prehibernation and it andwill breeding disclose period.protein Proteomicsexpression isprofiles an efficient in different methodology physiological to analyze phases protein [8]. It expression, is widely used and itto willtackle disclose biological protein problems, expression whereb profilesy the in raw different data obtained physiological from pr phasesoteomics [8]. Itis isstudied widely further used toby tacklebioinformatic biological methodologies problems, whereby [8]. Isobaric the raw tags data for obtainedrelative and from absolute proteomics quantitation is studied (iTRAQ) further is by an bioinformaticisobaric labeling methodologies method applied [8]. Isobaricin quantitative tags for proteomics relative and by absolutetandem mass quantitation spectrometry (iTRAQ) to identify is an isobaricthe amount labeling of proteins method appliedfrom different in quantitative samples proteomics in a single byexperiment tandem mass [9]. spectrometryiTRAQ can separate to identify and theidentify amount a variety of proteins of proteins, from different including samples membrane in a single proteins, experiment proteins [9]. of iTRAQ high molecular can separate weight, and identifyinsoluble a varietyproteins, of acidic proteins, proteins, including and alkaline membrane proteins proteins, [10]. proteins of high molecular weight, insoluble proteins, acidic proteins, and alkaline proteins [10]. 2. Results 2. Results 2.1. Protein Identified through Itraq Technology 2.1. Protein Identified through Itraq Technology 13216 unique peptides and 4479 proteins were identified using the iTRAQ technology (see Tables13216 S1 and unique S2 in peptides Supplementary and 4479 Material). proteins Amon wereg identified these identified using proteins, the iTRAQ 2422 technology were 0–20 (seekDa, Tables1758 were S1 and 20–60 S2 in kDa, Supplementary and 299 were Material). over 60 kDa Among (Figure these 1A). identified Accordingly, proteins, we 2422found were that 0–20 identified kDa, 1758proteins were were 20–60 primarily kDa, and 299below were 20 overkDa. 60 To kDa further (Figure prove1A). the Accordingly, credibility we of foundprotein that identification, identified proteinspeptide were sequence primarily coverage below and 20 kDa.the unique To further peptide prove numbers the credibility of proteins of protein were identification, also regarded peptide as two sequenceimportant coverage quality andevaluation the unique parameters. peptide numbersFigure 1B of showed proteins that were peptide also regarded sequence as coverage two important of these qualityproteins evaluation was basically parameters. less than Figure 30%.1 BThe showed number that of peptide unique sequencepeptides coveragefor identified of these proteins proteins were wasmainly basically concentrated less than in 30%. 1 and The 2, which number makes of unique up approximately peptides for identified71% of the proteins total unique were peptides mainly concentrated(Figure 1C). in 1 and 2, which makes up approximately 71% of the total unique peptides (Figure1C). Figure 1. Cont. Molecules 2018, 23, 1384 3 of 14 Molecules 2018, 23, x 3 of 14 Figure 1. Summary for iTRAQ data: (A) The protein mass distribution shown as a histogram; (B) The Figure 1. A B peptideSummary sequence for coverage iTRAQ distribution data: ( ) The shown protein as a masshistogram; distribution (C) The number shown asof unique a histogram; peptides ( ) The peptidedistribution sequence shown coverage as a histogram. distribution shown as a histogram; (C) The number of unique peptides distribution shown as a histogram. 2.2. Differentially Expressed Proteins 2.2. DifferentiallyHereon, Expressed we defined Proteins proteins with expression level fold changes >2.0 or <0.5 with p-values < 0.05 Hereon,as differentially we defined expressed proteins proteins with expression(DEPs). Chan levelges in fold the changes protein profile >2.0 or were <0.5 analyzed, with p-values and 312 < 0.05 as proteins exhibited a difference. Compared with the prehibernation group, 86 proteins were increased differentially expressed proteins (DEPs). Changes in the protein profile were analyzed, and 312 proteins by more than 2-fold, and 226 proteins decreased to less than 0.5-fold during the breeding period. The exhibiteddetailed a difference. information Compared of differential with expressed the prehibernation
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