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Identification of Candidate Interaction Partners of Human Calpain-5 in Neuroblastoma Cells with SWATH-MS Analysis

ABSTRACT: Few interaction partners of human calpain-5/CAPN5 have been identified or proposed. This project was designed to identify candidate interaction partners of CAPN5 in SH-SY5Y neuroblastoma cells. We utilized sequential window acquisition of all theoretical mass spectra (SWATH‐MS) for proteomic analysis of samples resulting from co-immunoprecipitation with full-length CAPN5-3×FLAG. The bait was catalytically inactive due to a C81A mutation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain, Neuroblastoma Cell Line

DISEASE(S): Neuroblastoma

SUBMITTER: Carlos Gartner

LAB HEAD: Calvin Vary

PROVIDER: PXD068008 | Pride | 2026-02-02

REPOSITORIES: Pride

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			Action	DRS
	DDA-87m-3F1.group	Other
	DDA-87m-C18A-5.group	Other
	DDA-87m-C18A-Pool2.group	Other
	DDA-GalJ-S1-730-F-035.wiff	Wiff
	DDA-GalJ-S1-730-F-035.wiff.scan	Wiff

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Publications

Candidate Interaction Partners of Calpain-5 Suggest Clues to Its Involvement in Neovascular Inflammatory Vitreoretinopathy.

Gal Jozsef J Bondada Vimala V Crasta Rachel R Croall Dorothy E DE Vary Calvin P CP Geddes James W JW

Cells 20260113 2

Although calpain-5/CAPN5 is widely expressed in mammals, little is known regarding its functions. Pathogenic mutations of CAPN5 are causal for a devastating autoimmune eye disease, neovascular inflammatory vitreoretinopathy (NIV). To provide insight into both the physiological and pathological roles of CAPN5, it is essential to identify candidate interaction partners and possible substrates. Human SH-SY5Y neuroblastoma cells, transfected with full-length catalytically dead (Cys81Ala) CAPN5-3×FLA ...[more]

PMID: 41597217

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Capture of candidate calpain5 interacting proteins from lysates of the human neuroblastoma SH-SY5Y cell line with analysis of LC-MSMS data using SWATH

Project description:Calpain5 (CAPN5) is a nonclassical calpain in that it lacks a pentaEF hand domain. Although widely expressed dominantly inherited mutations of CAPN5 display phenotypes primarily localized to the eye. These experiments aimed to identify proteins from the neuroblastoma cell line SH-SY5Y that may interact with the catalytic core domain of CAPN5 (phe2-leu348) and to complement co-immunoprecipitation studies using SH-SY5Y cell overexpressing full length CAPN5. Given that domains are independent folding units within the intact protein and interacting surfaces are in general localized some valid interacting proteins are expected to be captured. It is also clear that some interacting partners may be lost due to a decreased number of, or affinity of, interactions..

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Calpain Cleavage of Junctophilin-2 generates a Spectrum of Calcium-dependent Cleavage Products and DNA-rich NT1-Fragment Domains in Cardiomyocytes - PRM Dataset

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