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

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.

Rattus norvegicus Glutathione Transferase Omega 1 Localization in Oral Tissues and Interactions with Food Phytochemicals

“…Concerning human, salivary GST alpha 1 (GSTA1) and GST pi 1 (GSTP1) were recently shown to interact with and/or metabolize various bitter compounds, and decreased levels of salivary GSTA1 were observed in ageusic people . GSTO1 was previously identified in both human and murine saliva samples from proteomic studies. , The presence of GSTO1 in saliva could be due to its secretion by the salivary glands but could also result from the lysis of buccal and tongue cells, as we observed in the present study in the rat model. The presence of thiol-transferase activity in both oral and tongue extracts suggests that thiol–disulfide redox mechanisms exist in these tissues, although GSTO1 shows only weak activity in the buccal extract only.…”

“…Biochemical studies of nonanimal GSTOs have also evidenced a putative role for ligandin role. GSTOs have expanded through a multigenic family in saprotrophic fungi enabling them to scavenge plant polyphenols. − Based on proteomic studies, GSTO1 has been detected in the saliva from human, mouse, dog, and human oral epithelium samples . However, its immunolocalization in the oral epithelium and its role in the oral cavity have not yet been described.…”

How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?

“…These cellular changes in mdx-4cv hepatocytes agree with high levels of FABP5 and suggest the occurrence of altered patterns of fatty acid transportation and ectopic fat deposition in the liver in DMD [ 341 ]. In analogy to hepatic tissue, the proteomic analysis of serum from the same dystrophic mouse mutant was characterized by a high concentration of FABP5 [ 343 , 344 ], making it a potential serum biomarker candidate for the monitoring of hepatic alterations in association with dystrophinopathy [ 264 , 265 , 345 ].…”

“…Measurement of the serum carbonic anhydrase isoform CA3 alone versus the ratio of serum myoglobin to CA3 can be used to determine the loss of integrity of dystrophic skeletal muscles versus dystrophin-deficient heart muscle [ 423 ]. An interesting new source of non-invasive biomarkers is represented by the saliva proteome [ 412 ], whose analysis showed elevated levels of the kallikrein isoform Klk1 in the mdx-4cv model of DMD [ 344 , 433 ]. How future multi-omics research initiatives can build on these proteomic findings and establish a more comprehensive pathophysiological picture of dystrophinopathy is briefly outlined in the below section.…”

Extracellular Matrix Proteomics: The mdx-4cv Mouse Diaphragm as a Surrogate for Studying Myofibrosis in Dystrophinopathy

“…However, progressive myonecrosis, chronic inflammation, and reactive myofibrosis with increased levels of collagens, proteoglycans, matricellular proteins, and annexins are clearly observed in the mdx-4cv model with increasing severity during aging [55]. Table 3 lists major studies that have been carried out to characterize the mdx-4cv mouse model in the context of (i) chemical mutagenesis, genotyping, and phenotyping [41][42][43][44]231,237]; (ii) the testing of novel therapeutic strategies to treat X-linked Duchenne muscular dystrophy, including exon-skipping therapy [238], virus-or nanocarrier-mediated micro-dystrophin gene therapy [239][240][241][242][243], cell-based therapy [244][245][246], and gene editing [247,248]; (iii) the biochemical profiling of proteome-wide changes due to multi-systemic changes, including various skeletal muscles [55,146,229,230,[249][250][251][252], heart [253], liver [254], kidney [255,256], spleen [96,257], stomach wall and pancreas [258], and central nervous system [259]; and (iv) the biochemical profiling of proteome-wide changes in biofluids including serum [260,261], urine [262], and saliva [261,…”