Proteomic identification of elevated saliva kallikrein levels in the mouse model of Duchenne muscular dystrophy.

Dystrophinopathies are multi-system disorders that affect the skeletal musculature, the cardio-respiratory system and the central nervous system. The systematic screening of suitable biofluids for released or altered proteins promises new insights into the highly complex pathophysiology of X-linked muscular dystrophy. However, standard detection approaches using antibody-based assays often fail to reproducibly detect low-abundance protein isoforms in dilute biological fluids.

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

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 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 saliva specimens.

Proteomic profiling of liver tissue from the - mouse model of Duchenne muscular dystrophy.

Background: Duchenne muscular dystrophy is a highly complex multi-system disease caused by primary abnormalities in the membrane cytoskeletal protein dystrophin. Besides progressive skeletal muscle degeneration, this neuromuscular disorder is also associated with pathophysiological perturbations in many other organs including the liver. To determine potential proteome-wide alterations in liver tissue, we have used a comparative and mass spectrometry-based approach to study the dystrophic - mouse model of dystrophinopathy.

Chemical crosslinking analysis of β-dystroglycan in dystrophin-deficient skeletal muscle.

: In Duchenne muscular dystrophy, primary abnormalities in the membrane cytoskeletal protein dystrophin trigger the loss of sarcolemmal linkage between the extracellular matrix component laminin-211 and the intracellular cortical actin membrane cytoskeleton. The disintegration of the dystrophin-associated glycoprotein complex renders the plasma membrane of contractile fibres more susceptible to micro-rupturing, which is associated with abnormal calcium handling and impaired cellular signalling in dystrophinopathy. : The oligomerisation pattern of β-dystroglycan, an integral membrane protein belonging to the core dystrophin complex, was studied using immunoprecipitation and chemical crosslinking analysis.

Subproteomic profiling of sarcolemma from dystrophic skeletal muscle.

The proteomic data presented in this article provide supporting information to the related research article "Proteomic analysis of the sarcolemma-enriched fraction from dystrophic skeletal muscle" (Murphy et al., 2018) [1]. In the associated research article, the sarcolemma from normal versus dystrophic skeletal muscle was analyzed by mass spectrometry-based proteomics.