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Rapid and Efficient Generation of Neurons from Human Pluripotent Stem Cells in a Multititre Plate Format

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Published on: March 5, 2013

A Deep Quantitative Proteome Turnover Platform for Human iPSC-derived Neurons.

Ashley M Frankenfield¹, Jamison Shih², Tao Zhang^3,4

¹Department of Chemistry, George Washington University, Washington, DC, USA.

Biorxiv : the Preprint Server for Biology

|March 27, 2026

Summary

Researchers developed a new method to measure protein half-lives in human neurons, revealing conserved dynamics and subtype-specific differences. This platform aids neurological disease research and drug development.

Keywords:

NeuronProfile dynamic SILAC iPSC-derived neuron protein half-life protein turnover proteostasis

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Three-dimensional Quantification of Dendritic Spines from Pyramidal Neurons Derived from Human Induced Pluripotent Stem Cells

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Published on: October 10, 2015

Area of Science:

Neuroscience
Proteomics
Systems Biology

Background:

Quantifying protein turnover in human neurons is vital for understanding neurological diseases and homeostasis.
Existing methods like Stable Isotope Labeling by Amino acids in Cell culture (SILAC) face challenges in human neurons, including limited proteome coverage and a wide range of protein half-lives.

Purpose of the Study:

To establish a comprehensive platform for quantifying protein half-lives in human induced pluripotent stem cell (iPSC)-derived neurons.
To compare protein turnover and abundance between different human neuronal subtypes.
To create a publicly accessible resource for exploring neuronal protein dynamics.

Main Methods:

Optimized dynamic SILAC labeling in human neuron cultures.
Extensive peptide fractionation and advanced LC-MS/MS acquisition (data-dependent and data-independent).
Streamlined computational pipeline for deep and accurate proteome-wide half-life measurements.

Main Results:

Successfully quantified 10,792 protein half-lives from 162,854 unique peptides in human iPSC-derived neurons.
Revealed globally conserved proteome dynamics between glutamatergic cortical neurons and spinal motor neurons.
Identified subtype-specific differences in protein turnover and abundance consistent with specialized neuronal functions.

Conclusions:

The developed platform provides a robust method for assessing human neuronal proteostasis.
The findings offer a foundational resource for neurological disease research and therapeutic development.
The interactive web platform NeuronProfile enhances accessibility to neuronal proteomic data.