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Mass spectrometry data supporting "Mass spectrometry imaging of SOD1 protein-metal complexes in SOD1G93A transgenic mice implicates demetalation with pathology"

ABSTRACT: Protein-metal complexes implicated in the pathogenesis of amyotrophic lateral sclerosis were mapped by mass spectrometry imaging. Metal-deficient hSOD1G93A complexes were revealed to be localised with disease pathology in the spinal cord and brain.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain, Spinal Cord

DISEASE(S): Amyotrophic Lateral Sclerosis

SUBMITTER: Oliver Hale

LAB HEAD: Helen Cooper

PROVIDER: PXD053247 | Pride | 2024-07-15

REPOSITORIES: Pride

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			Action	DRS
	1-12_s08_img.mat	Other
	2022_07_11_MB-TV_292061_s11.ibd	Other
	2022_07_11_MB-TV_292061_s11.ibh	Other
	2022_07_11_MB-TV_292061_s11.imzML	Other
	2022_07_11_MB-TV_292061_s11_img_01.raw	Raw

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Mass spectrometry imaging of SOD1 protein-metal complexes in SOD1G93A transgenic mice implicates demetalation with pathology.

Project description:Amyotrophic lateral sclerosis (ALS) is characterized by degeneration of motor neurons in the central nervous system (CNS). Mutations in the metalloenzyme SOD1 are associated with inherited forms of ALS and cause a toxic gain of function thought to be mediated by dimer destabilization and misfolding. SOD1 binds two Cu and two Zn ions in its homodimeric form. We have applied native ambient mass spectrometry imaging to visualize the spatial distributions of intact metal-bound SOD1G93A complexes in SOD1G93A transgenic mouse spinal cord and brain sections and evaluated them against disease pathology. The molecular specificity of our approach reveals that metal-deficient SOD1G93A species are abundant in CNS structures correlating with ALS pathology whereas fully metalated SOD1G93A species are homogenously distributed. Monomer abundance did not correlate with pathology. We also show that the dimer-destabilizing post-translational modification, glutathionylation, has limited influence on the spatial distribution of SOD1 dimers.

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