Proteomics

Dataset Information

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Identification of mitochondrial Cyclophilins

ABSTRACT: We aimed at identify variants of the mitochondrial Cyclophilin D from total lysates of human skin fibroblasts and murine tissues. Total lysates were loaded onto SDS-PAGE stained with MS-compatible Coomassie and bands around 19 and 18 kDa were manually excised. In fact in Western blots analysis of CyPD, which is the sole known mitochondrial Cyclophilin, often show two distinct bands at that molecular weights.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Heart, Skin

SUBMITTER: Gabriele Coluccino  

LAB HEAD: Alessandra Corazza

PROVIDER: PXD057203 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

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Action DRS
20230310_Sample_S1.raw Raw
20230310_Sample_S2.raw Raw
20230425_Gel1_Sample_5.raw Raw
20230425_Gel1_Sample_6.raw Raw
20230427_Gel2_Sample_13.raw Raw
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Publications

Cyclophilin (CyP) D is a regulator of the mitochondrial F-ATP synthase. Here we report the discovery of a form of CyPD lacking the first 10 (mouse) or 13 (human) N-terminal residues (ΔN-CyPD), a protein region with species-specific features. NMR studies on recombinant human full-length CyPD (FL-CyPD) and ΔN-CyPD form revealed that the N-terminus is highly flexible, in contrast with the rigid globular part. We have studied the interactions of FL and ΔN-CyPD with F-ATP synthase at the OSCP subunit  ...[more]

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