Literature DB >> 30456239

Dataset on the comparative proteomic profiling of mouse saliva and serum from wild type versus the dystrophic mdx-4cv mouse model of dystrophinopathy.

Sandra Murphy1, Margit Zweyer2, Rustam R Mundegar2, Dieter Swandulla2, Kay Ohlendieck1.   

Abstract

The comparative proteomic data presented in this article provide supporting information to the related research article "Proteomic identification of elevated saliva kallikrein levels in the mdx-4cv mouse model of Duchenne muscular dystrophy " (Murphy et al., 2018). Here we provide additional datasets on the comparative proteomic analysis of saliva and serum proteins and the mass spectrometric identification of kallikrein isoform Klk-1 in wild type versus mdx-4cv saliva specimens. The data article presents the systematic identification of the assessable saliva proteome and the differential presence of proteins in saliva versus serum samples. Representative mass spectrometric scans of unique peptides that were employed to identify the kallikrein isoform Klk-1 in wild type versus mdx-4cv saliva specimens are provided. The dataset contains typical saliva-associated marker proteins, including alpha-amylase and albumin, as well as distinct isoforms of cystatin, serpin, kallikrein, cathepsin, glutathione transferase, carbonic anhydrase, mucin, pyruvate kinase, and aldolase.

Entities:  

Year:  2018        PMID： 30456239      PMCID： PMC6231363          DOI： 10.1016/j.dib.2018.10.082

Source DB:  PubMed          Journal:  Data Brief        ISSN： 2352-3409


Specifications table Value of the data Proteomic data presented here provide an overview of biofluid changes in the mdx-4cv mouse model of X-linked muscular dystrophy. This data provide comparative listings of proteins in saliva versus serum specimens, as well as their mass spectrometric identification. The mass spectrometric data are valuable to serve as a pathobiochemical biofluid signature of the dystrophin-deficient mdx-4cv mouse.

Data

The data presented relate to the systematic survey of whole saliva using mass spectrometry-based proteomics of the mdx-4cv mouse model of Duchenne muscular dystrophy [1]. This accompanying article lists the proteomic identification of the total saliva protein population and the differential presence of protein species in saliva versus serum samples, as well as representative MS/MS scans of unique peptides that were used to identify the kallikrein isoform Klk-1 in wild type versus mdx-4cv saliva specimens. Table 1 lists the mass spectrometric profiling of the mouse saliva proteome. Listed are the protein name, gene name, the number of unique peptides, the number of total peptides, the relative molecular mass, and the estimated isoelectric point of the identified protein species. A set of typical marker proteins of whole saliva were identified, including alpha-amylase and albumin, as well as distinct isoforms of cystatin, serpin, kallikrein, cathepsin, glutathione transferase, carbonic anhydrase, mucin, pyruvate kinase, and aldolase [2], [3], [4], [5]. The identified protein species in saliva were compared with the previously established serum proteome [6]. Fig. 1 shows a Venn diagram of the distribution of proteins that are shared between saliva and serum, and protein species that are uniquely associated with saliva versus serum samples. Table 2, Table 3 list the mass spectrometric identification of proteins identified in saliva only or are shared between serum and saliva. In Table 2 are listed 59 proteins found in wild-type saliva, but not serum, including carbonic anhydrase 6, BPI fold-containing family A members 1 and 2, cystatin 10, cardiomyopathy-associated protein 5, mucin-19, and desmoplakin. Table 3 lists 78 proteins found in both serum and saliva, including alpha-amylase, cathepsin D, serum albumin, and fructose-bisphosphate aldolase A, as well as kallikrein-1 and Klk1-related peptidases b1, b3, b4, b5, b8, b9, b11, b16, b21, b22, b24, b26, and b27. In addition to the MS/MS scans of the unique peptide NNFLEDEPSAQHR shown in the accompanying research manuscript [1], Fig. 2 displays additional MS/MS scans of the unique peptides LGSTCLASGWGSITPVK and VLNFNTWIR that were used to identify the Klk-1 isoform in both wild type and mdx-4cv samples.
Table 1

Mass spectrometry-based proteomic identification of proteins in whole saliva from wild type mouse.

Protein nameGeneNumber of unique peptidesNumber of peptidesMolecular mass kDaIsoelectric point pI
Mucin-19Muc1944693.15.54
Cardiomyopathy-associated protein 5Cmya511412.84.75
DesmoplakinDsp11332.76.80
HornerinHrnr11247.410.33
OvostatinOvos66162.25.26
WD repeat-containing protein 7Wdr711160.27.01
Calcium-dependent secretion activator 2Cadps222143.86.14
Pro-epidermal growth factorEgf1010133.06.46
RepetinRptn11128.57.61
Collagen alpha-1(I) chainCol1a111117.75.72
Lysosomal alpha-mannosidaseMan2b11414114.68.13
Aminopeptidase NAnpep44109.65.90
Zinc finger CCHC domain-containing protein 14Zcchc141198.68.25
Dipeptidyl peptidase 4Dpp41187.46.42
NeprilysinMme2285.65.81
Heat shock protein 75 kDa, mitochondrialTrap11180.26.68
Cytosolic carboxypeptidase-like protein 5Agbl51180.18.24
Solute carrier family 15 member 1Slc15a11178.57.93
Amyloid beta A4 proteinApp1178.44.83
LactotransferrinLtf1177.88.53
Protein-glutamine gamma-glutamyltransferase ETgm32277.36.81
GalactocerebrosidaseGalc2277.26.74
Stress-70 protein, mitochondrialHspa91173.46.07
Keratin, type II cytoskeletal 2, epidermalKrt24570.98.06
Heat shock cognate 71 kDa proteinHspa81170.85.52
Serum albuminAlb3368.66.07
Keratin, type II cytoskeletal 1Krt15765.68.15
Sulfhydryl oxidase 1Qsox12263.37.93
Keratin, type II cytoskeletal 2, oralKrt7681162.88.43
VomeromodulinBpifb9a151562.45.68
Keratin, type II cytoskeletal 5Krt53961.77.75
ProsaposinPsap1161.45.19
Beta-hexosaminidase subunit betaHexb9961.18.12
Keratin, type II cytoskeletal 6BKrt6b11660.38.32
Keratin, type II cytoskeletal 6AKrt6a21759.37.94
Keratin, type II cytoskeletal 73Krt731358.98.09
BiotinidaseBtd1158.15.80
Pyruvate kinasePkm3357.87.47
N-acetylgalactosamine-6-sulfataseGalns1157.66.52
Alpha-amylase 1Amy1101057.66.96
Keratin, type II cytoskeletal 79Krt791357.57.69
Keratin, type I cytoskeletal 10Krt1091157.05.07
Keratin, type II cytoskeletal 4Krt4192156.28.15
PodocalyxinPodxl1153.44.97
Aldehyde dehydrogenase family 3 member B2Aldh3b22252.96.09
Keratin, type I cytoskeletal 14Krt143752.85.17
Acidic mammalian chitinaseChia3352.05.06
AngiotensinogenAgt1152.05.44
Keratin, type I cytoskeletal 16Krt164751.65.20
Carboxypeptidase QCpq4450.56.40
Aldehyde dehydrogenase, dimeric NADP-preferringAldh3a12250.46.95
Keratin, type I cytoskeletal 42Krt421550.15.16
Elongation factor 1-alpha 1Eef1a13350.19.01
Serpin B12Serpinb121147.85.17
Keratin, type I cytoskeletal 13Krt13141847.74.86
Transcobalamin-2Tcn21147.66.33
Alpha-N-acetyl-galactosaminidaseNaga1147.26.44
Alpha-enolaseEno12247.16.80
Rab GDP dissociation inhibitor betaGdi21146.66.90
Chitinase-like protein 4Chil44444.96.19
Cathepsin DCtsd4444.97.15
Phosphoglycerate kinase 2Pgk21144.86.80
MANSC domain-containing protein 1Mansc11144.89.11
Renin-1Ren12244.37.17
Prostatic acid phosphataseAcpp1143.76.24
Serpin B11Serpinb111143.58.94
Synaptic vesicle membrane protein VAT-1Vat11143.16.37
Serpin B6Serpinb64442.65.74
Actin, cytoplasmic 1Actb4441.75.48
Adenosine deaminaseAda3340.05.72
Fructose-bisphosphate aldolase AAldoa2239.38.09
Annexin A1Anxa11138.77.37
Protein LEG1Leg12238.34.36
Guanine nucleotide-binding protein subunit beta-4Gnb41137.46.16
Malate dehydrogenase, cytoplasmicMdh13336.56.58
L-lactate dehydrogenase A chainLdha2236.57.74
Carbonic anhydrase 6Ca67736.56.60
Gamma-glutamyl hydrolaseGgh3335.48.29
Polyubiquitin-BUbb1134.37.53
Triosephosphate isomeraseTpi12232.25.74
Deoxyribonuclease-1Dnase13332.04.92
Phospholipid phosphatase 1Plpp11131.97.02
Syntaxin-3Stx31130.95.63
Syntaxin-7Stx73329.85.78
Kallikrein 1-related peptidase b1Klk1b14829.08.10
Kallikrein 1-related peptidase b3Klk1b34729.06.84
Kallikrein 1-related peptidase b24Klk1b243928.98.16
Kallikrein 1-related peptidase b9Klk1b95928.97.64
Kallikrein-1Klk12628.85.12
Kallikrein 1-related peptidase b5Klk1b54728.75.59
Kallikrein 1-related peptidase b27Klk1b273928.78.56
Kallikrein 1-related peptidase b11Klk1b115928.77.14
Kallikrein 1-related peptidase b16Klk1b167928.75.64
Kallikrein 1-related peptidase b21Klk1b212828.77.37
BPI fold-containing family A member 1Bpifa11128.66.51
Kallikrein 1-related peptidase-like b4Klk1b46728.54.86
Kallikrein 1-related peptidase b8Klk1b871128.58.00
Kallikrein 1-related peptidase b26Klk1b263928.46.86
Kallikrein 1-related peptidase b22Klk1b225628.46.65
14-3-3 protein zeta/deltaYwhaz1127.84.79
Cysteine-rich secretory protein 1Crisp13427.76.87
Glutathione S-transferase omega-1Gsto12227.57.36
Cysteine-rich secretory protein 3Crisp31227.38.37
Beta-nerve growth factorNgf3327.19.47
Ras-related protein Rab-27ARab27a1125.05.36
BPI fold-containing family A member 2Bpifa24424.75.01
Ras-related protein Rab-2ARab2a1123.56.54
Rho GDP-dissociation inhibitor 1Arhgdia1123.45.20
Synaptosomal-associated protein 23Snap231123.24.98
Ras-related protein Rab-10Rab101322.58.38
Ras-related protein Rab-1BRab1b1322.25.73
Peroxiredoxin-1Prdx11122.28.12
Major urinary protein 3Mup31121.54.81
Vomeronasal secretory protein 2Lcn41121.45.73
Ras-related protein Rap-1ARap1a1121.06.67
Major urinary protein 5Mup53320.94.86
Placenta-expressed transcript 1 proteinPlet11120.86.14
Vomeronasal secretory protein 1Lcn31120.64.60
Major urinary protein 4Mup44420.55.80
Tumor protein D52Tpd521120.04.88
Odorant-binding protein 2aObp2a2220.06.42
Odorant-binding protein 1bObp1b3319.46.29
Protein MAL2Mal21119.16.49
DestrinDstn1118.57.97
Odorant-binding protein 1aObp1a4418.55.67
Peptidyl-prolyl cis-trans isomerase APpia1118.07.90
Nucleoside diphosphate kinase BNme23317.47.50
Prolactin-inducible proteinPip4416.84.78
Calmodulin-4Calm41116.84.89
Cystatin 10Cst102216.47.72
Superoxide dismutase [Cu-Zn]Sod13315.96.51
Submaxillary gland androgen-regulated protein 3ASmr3a1115.59.09
Profilin-1Pfn11114.98.28
Protein S100-A9S100a91113.07.17
Secretoglobin family 2B member 2Scgb2b21112.85.95
Vesicle-associated membrane protein 8Vamp82211.48.19
Protein S100-A1S100a11110.54.50
Fig. 1

Overview of the comparative proteomic profiling of mouse saliva and serum. Shown is the flow chart of the preparation of saliva and serum protein populations for the mass spectrometry-based proteomic identification of biofluid markers. The Venn diagram illustrates the distribution of protein species between saliva and serum.

Table 2

Mass spectrometry-based proteomic identification of proteins present in whole saliva from wild type mouse, but not serum.

Accession NumberProtein nameGene name
P07744Keratin, type II cytoskeletal 4Krt4
Q80XI7VomeromodulinBpifb9a
P08730Keratin, type I cytoskeletal 13Krt13
P18761Carbonic anhydrase 6Ca6
Q9Z331Keratin, type II cytoskeletal 6BKrt6b
P07743BPI fold-containing family A member 2Bpifa2
Q9D3H2Odorant-binding protein 1aObp1a
P11590Major urinary protein 4Mup4
P11591Major urinary protein 5Mup5
P02535-2Isoform 2 of Keratin, type I cytoskeletal 10Krt10
A2AEP0Odorant-binding protein 1bObp1b
P61027Ras-related protein Rab-10Rab10
Q9JM84Cystatin 10Cst10
Q6UGQ3Secretoglobin family 2B member 2Scgb2b2
Q91Z98Chitinase-like protein 4Chil4
Q8C6C9Protein LEG1 homologLeg1
Q91XA9Acidic mammalian chitinaseChia
P06281Renin-1Ren1
Q9JM83Calmodulin-4Calm4
P49183Deoxyribonuclease-1Dnase1
Q61900Submaxillary gland androgen-regulated protein 3ASmr3a
O09044Synaptosomal-associated protein 23Snap23
Q62472Vomeronasal secretory protein 2Lcn4
P38647Stress-70 protein, mitochondrialHspa9
Q62471Vomeronasal secretory protein 1Lcn3
Q62465Synaptic vesicle membrane protein VAT-1 homologVat1
Q8BI08Protein MAL2Mal2
P53994Ras-related protein Rab-2ARab2a
Q9ERI2Ras-related protein Rab-27ARab27a
P97361BPI fold-containing family A member 1Bpifa1
Q61469Phospholipid phosphatase 1Plpp1
Q09M02–6Isoform 6 of Cytosolic carboxypeptidase-like protein 5Agbl5
Q62393-2Isoform 2 of Tumor protein D52Tpd52
Q3UU35Ovostatin homologOvos
Q8BND5-3Isoform 3 of Sulfhydryl oxidase 1Qsox1
Q8VIG0–2Isoform 2 of Zinc finger CCHC domain-containing protein 14Zcchc14
P47739Aldehyde dehydrogenase, dimeric NADP-preferringAldh3a1
P10107Annexin A1Anxa1
E9Q3E1Aldehyde dehydrogenase family 3 member B2Aldh3b2
Q9R0M4PodocalyxinPodxl
P09041Phosphoglycerate kinase 2Pgk2
Q08189Protein-glutamine gamma-glutamyltransferase ETgm3
P54818GalactocerebrosidaseGalc
Q9CR33MANSC domain-containing protein 1Mansc1
Q9D7P9Serpin B12Serpinb12
Q64704-3Isoform 3C of Syntaxin-3Stx3
Q8CE08Prostatic acid phosphataseAcpp
Q920I9-2Isoform 2 of WD repeat-containing protein 7Wdr7
P29387Guanine nucleotide-binding protein subunit beta-4Gnb4
Q9QWR8Alpha-N-acetylgalactosaminidaseNaga
Q8VHD8HornerinHrnr
Q9CQN1Heat shock protein 75 kDa, mitochondrialTrap1
Q8BYR5-5Isoform 5 of Calcium-dependent secretion activator 2Cadps2
Q9JIP7Solute carrier family 15 member 1Slc15a1
P12023-2Isoform APP695 of Amyloid beta A4 proteinApp
P97347RepetinRptn
Q70KF4Cardiomyopathy-associated protein 5Cmya5
Q6PZE0Mucin-19Muc19
E9Q557DesmoplakinDsp
Table 3

Mass spectrometry-based proteomic identification of proteins that are present in both saliva and serum from wild type mouse.

Accession numberProtein nameGene name
P05064Fructose-bisphosphate aldolase AAldoa
P00756Kallikrein 1-related peptidase b3Klk1b3
P07724Serum albuminAlb
Q01768Nucleoside diphosphate kinase BNme2
P15946Kallikrein 1-related peptidase b11Klk1b11
P00755Kallikrein 1-related peptidase b1Klk1b1
P35700Peroxiredoxin-1Prdx1
P06151L-lactate dehydrogenase A chainLdha
P15948Kallikrein 1-related peptidase b22Klk1b22
P07628Kallikrein 1-related peptidase b8Klk1b8
P15949Kallikrein 1-related peptidase b9Klk1b9
P17751Triosephosphate isomeraseTpi1
P60710Actin, cytoplasmic 1Actb
P52480Pyruvate kinase PKMPkm
P04071Kallikrein 1-related peptidase b16Klk1b16
P62962Profilin-1Pfn1
Q9JM71Kallikrein 1-related peptidase b27Klk1b27
P17182Alpha-enolaseEno1
P36369Kallikrein 1-related peptidase b26Klk1b26
P08228Superoxide dismutase [Cu-Zn]Sod1
P14152Malate dehydrogenase, cytoplasmicMdh1
P0CG49Polyubiquitin-BUbb
Q61759Kallikrein 1-related peptidase b21Klk1b21
P17742Peptidyl-prolyl cis-trans isomerase APpia
P63017Heat shock cognate 71 kDa proteinHspa8
P15945Kallikrein 1-related peptidase b5Klk1b5
P6310114-3-3 protein zeta/deltaYwhaz
O88968Transcobalamin-2Tcn2
P00757Kallikrein 1-related peptidase-like b4Klk1b4
Q61754Kallikrein 1-related peptidase b24Klk1b24
P00687Alpha-amylase 1Amy1
P15947Kallikrein-1Klk1
Q61598-2Isoform 2 of Rab GDP dissociation inhibitor betaGdi2
Q8CIF4BiotinidaseBtd
Q99PT1Rho GDP-dissociation inhibitor 1Arhgdia
Q03401Cysteine-rich secretory protein 1Crisp1
O09131Glutathione S-transferase omega-1Gsto1
P04939Major urinary protein 3Mup3
O09159Lysosomal alpha-mannosidaseMan2b1
P20060Beta-hexosaminidase subunit betaHexb
P11859AngiotensinogenAgt
Q9WVJ3-2Isoform 2 of Carboxypeptidase QCpq
P10126Elongation factor 1-alpha 1Eef1a1
P56565Protein S100-A1S100a1
Q9R0P5DestrinDstn
Q922U2Keratin, type II cytoskeletal 5Krt5
Q6IFX2Keratin, type I cytoskeletal 42Krt42
Q61781Keratin, type I cytoskeletal 14Krt14
P50446Keratin, type II cytoskeletal 6AKrt6a
P08071LactotransferrinLtf
P01132Pro-epidermal growth factorEgf
Q9Z2K1Keratin, type I cytoskeletal 16Krt16
Q03402Cysteine-rich secretory protein 3Crisp3
P01139Beta-nerve growth factorNgf
Q9D1G1Ras-related protein Rab-1BRab1b
P97449Aminopeptidase NAnpep
Q3TTY5Keratin, type II cytoskeletal 2 epidermalKrt2
P31725Protein S100-A9S100a9
Q60854Serpin B6Serpinb6
Q8VEN2-2Isoform 2 of Placenta-expressed transcript 1 proteinPlet1
O70404Vesicle-associated membrane protein 8Vamp8
P18242Cathepsin DCtsd
Q61207ProsaposinPsap
Q9CQV3Serpin B11Serpinb11
P11087-2Isoform 2 of Collagen alpha-1(I) chainCol1a1
P28843Dipeptidyl peptidase 4Dpp4
Q6NXH9Keratin, type II cytoskeletal 73Krt73
Q3UV17Keratin, type II cytoskeletal 2 oralKrt76
Q8VED5Keratin, type II cytoskeletal 79Krt79
P62835Ras-related protein Rap-1ARap1a
P04104Keratin, type II cytoskeletal 1Krt1
P02816Prolactin-inducible protein homologPip
Q8K1H9Odorant-binding protein 2aObp2a
Q571E4N-acetylgalactosamine-6-sulfataseGalns
Q9Z0L8-2Isoform II of Gamma-glutamyl hydrolaseGgh
P03958Adenosine deaminaseAda
Q61391NeprilysinMme
O70439Syntaxin-7Stx7
Fig. 2

Proteomic identification of kallikrein isoform Klk1 in saliva from the wild type versus the mdx-4cv mouse model of Duchenne muscular dystrophy. Shown are representative MS/MS scans of the unique Klk-1 peptides LGSTCLASGWGSITPVK and VLNFNTWIR, which were identified and compared in wild type versus mdx-4cv saliva, respectively.

Mass spectrometry-based proteomic identification of proteins in whole saliva from wild type mouse. Overview of the comparative proteomic profiling of mouse saliva and serum. Shown is the flow chart of the preparation of saliva and serum protein populations for the mass spectrometry-based proteomic identification of biofluid markers. The Venn diagram illustrates the distribution of protein species between saliva and serum. Mass spectrometry-based proteomic identification of proteins present in whole saliva from wild type mouse, but not serum. Mass spectrometry-based proteomic identification of proteins that are present in both saliva and serum from wild type mouse. Proteomic identification of kallikrein isoform Klk1 in saliva from the wild type versus the mdx-4cv mouse model of Duchenne muscular dystrophy. Shown are representative MS/MS scans of the unique Klk-1 peptides LGSTCLASGWGSITPVK and VLNFNTWIR, which were identified and compared in wild type versus mdx-4cv saliva, respectively.

Experimental design, materials, and methods

Details of the methodological approach used in this study are available in [1], [6].

Sample collection and processing

For the proteomic profiling of easily assessable biofluids, saliva and serum specimens were obtained from 6-month-old dystrophic mdx-4cv and age-matched wild type C57BL/6 mice through the Bioresource Unit of the University of Bonn [6], where mice were kept under standard conditions according to German legislation on the use of animals in experimental research. Sample collection and preparation of protein extracts were carried out as previously described in detail [1], [6]. The collected saliva and serum specimens were transported to Maynooth University on dry ice in accordance with the Department of Agriculture (animal by-product register number 2016/16 to the Department of Biology, National University of Ireland, Maynooth).

Mass spectrometric analysis of saliva and serum proteins

Serum samples were processed as previously described [6]. For the proteomic analysis of saliva samples, 30 µg of protein was processed by the filter-aided sample preparation (FASP) method, as described in detail by Wiśniewski et al. [7], using a trypsin to protein ratio of 1:25 (protease:protein). Following overnight digestion and elution of peptides from the spin filter, 2% trifluoroacetic acid (TFA) in 20% acetonitrile (ACN) was added to the filtrates (3:1 (v/v) dilution). Peptides were analyzed by label-free liquid chromatography mass spectrometry (LC-MS/MS) by a standardized method using an Ultimate 3000 NanoLC system (Dionex Corporation, Sunnyvale, CA, USA) coupled to a Q-Exactive mass spectrometer (Thermo Fisher Scientific) as previously described in detail [1], [6], [8], [9].

Protein identification and quantification

Proteins present in the wild type and the mdx-4cv salivary and serum proteomes were initially identified using Proteome Discoverer 1.4 against Sequest HT (SEQUEST HT algorithm, licence Thermo Scientific, registered trademark University of Washington, USA) using the UniProtKB/Swiss-Prot database, with 25,041 sequences for Mus musculus [1], [6]. Identified saliva peptides were then filtered using a minimum XCorr score of 1.5 for 1, 2.0 for 2, 2.25 for 3, and 2.5 for 4 charge states, with peptide probability set to high confidence. For quantitative analysis, samples were evaluated with MaxQuant software (version 1.6.1.0) and the Andromeda search engine used to explore the detected features against the UniProtKB/SwissProt database for Mus musculus. The following search parameters were used: (i) first search peptide tolerance of 20 ppm, (ii) main search peptide tolerance of 4.5 ppm, (iii) cysteine carbamidomethylation set as a fixed modification, (iv) methionine oxidation set as a variable modification, (v) a maximum of two missed cleavage sites, and (vi) a minimum peptide length of seven amino acids. The false discovery rate (FDR) was set to 1% for both peptides and proteins using a target-decoy approach. Relative quantification was performed using the MaxLFQ algorithm [10]. The “proteinGroups.txt” file produced by MaxQuant was further analysed in Perseus (version 1.5.1.6). Proteins that matched to the reverse database or a contaminants database or that were only identified by site were removed. The LFQ intensities were log2 transformed, and only proteins found in all eight replicates in at least one group were used for further analysis. Data imputation was performed to replace missing values with values that simulate signals from peptides with low abundance chosen from a normal distribution specified by a downshift of 1.8 times the mean standard deviation of all measured values and a width of 0.3 times this standard deviation [11]. A two-sample t-test was performed using p<0.05 on the post imputated data to identify statistically significant differentially abundant proteins.
Subject areaBiology
More specific subject areaBiomedicine
Type of dataTables, MS/MS scans, Venn diagram
How data was acquiredLC-MS/MS analysis, using an Ultimate 3000 NanoLC system (Dionex Corporation, Sunnyvale, CA, USA) coupled to a Q-Exactive mass spectrometer (Thermo Fisher Scientific)
Data formatAnalyzed
Experimental factorsProtein was extracted from whole saliva and pre-fractionated serum specimens from wild type versus dystrophic mdx-4cv mice.
Experimental featuresComparative mass spectrometry-based proteomic profiling of the saliva and serum fraction.
Data source locationMaynooth, Ireland
Data accessibilityThe data are available with this article
Related research articleMurphy S, Zweyer M, Mundegar RR, Swandulla D, Ohlendieck K. Proteomic identification of elevated saliva kallikrein levels in the mdx-4cv mouse model of Duchenne muscular dystrophy. Biochem Biophys Rep. (2018) In press [1]
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Authors:  Gwendoline Deslyper; Thomas J Colgan; Andrew J R Cooper; Celia V Holland; James C Carolan
Journal:  PLoS Negl Trop Dis       Date:  2016-08-04

10.  Mass spectrometric identification of dystrophin, the protein product of the Duchenne muscular dystrophy gene, in distinct muscle surface membranes.

Authors:  Sandra Murphy; Kay Ohlendieck
Journal:  Int J Mol Med       Date:  2017-07-27       Impact factor: 4.101
  10 in total
  1 in total

1.  Proteomic identification of elevated saliva kallikrein levels in the mdx-4cv mouse model of Duchenne muscular dystrophy.

Authors:  Sandra Murphy; Margit Zweyer; Rustam R Mundegar; Dieter Swandulla; Kay Ohlendieck
Journal:  Biochem Biophys Rep       Date:  2018-05-30
  1 in total

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