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Unconventional Protein Secretion

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Cover of 'Unconventional Protein Secretion'

Table of Contents

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    Book Overview
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    Chapter 1 ER to Golgi-Dependent Protein Secretion: The Conventional Pathway
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    Chapter 2 Unconventional Protein Secretion
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    Chapter 3 Unconventional Protein Secretion
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    Chapter 4 Chemical Secretory Pathway Modulation in Plant Protoplasts
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    Chapter 5 From Cytosol to the Apoplast: The Hygromycin Phosphotransferase (HYGR) Model in Arabidopsis
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    Chapter 6 Unconventional Protein Secretion
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    Chapter 7 Unconventional Protein Secretion
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    Chapter 8 Quantification of a Non-conventional Protein Secretion: The Low-Molecular-Weight FGF-2 Example
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    Chapter 9 Human Primary Keratinocytes as a Tool for the Analysis of Caspase-1-Dependent Unconventional Protein Secretion
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    Chapter 10 A Reporter System to Study Unconventional Secretion of Proteins Avoiding N-Glycosylation in Ustilago maydis
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    Chapter 11 Stress-Inducible Protein 1 (STI1): Extracellular Vesicle Analysis and Quantification
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    Chapter 12 Unconventional Protein Secretion
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    Chapter 13 Unconventional Protein Secretion
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    Chapter 14 Characterization of the Unconventional Secretion of the Ebola Matrix Protein VP40
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    Chapter 15 Role and Characterization of Synuclein-γ Unconventional Protein Secretion in Cancer Cells
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    Chapter 16 Unconventional Protein Secretion
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    Chapter 17 Unconventional Protein Secretion
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    Chapter 18 Isolation of Exosome-Like Vesicles from Plants by Ultracentrifugation on Sucrose/Deuterium Oxide (D2O) Density Cushions
Attention for Chapter 8: Quantification of a Non-conventional Protein Secretion: The Low-Molecular-Weight FGF-2 Example
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Chapter title
Quantification of a Non-conventional Protein Secretion: The Low-Molecular-Weight FGF-2 Example
Chapter number 8
Book title
Unconventional Protein Secretion
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3804-9_8
Pubmed ID
Book ISBNs
978-1-4939-3802-5, 978-1-4939-3804-9
Authors

Tania Arcondéguy, Christian Touriol, Eric Lacazette

Editors

Andrea Pompa, Francesca De Marchis

Abstract

Quantification of secreted factors is most often measured with enzyme-linked immunosorbent assay (ELISA), Western Blot, or more recently with antibody arrays. However, some of these, like low-molecular-weight fibroblast growth factor-2 (LMW FGF-2; the 18 kDa form), exemplify a set of secreted but almost non-diffusible molecular actors. It has been proposed that phosphorylated FGF-2 is secreted via a non-vesicular mechanism and that heparan sulfate proteoglycans function as extracellular reservoir but also as actors for its secretion. Heparan sulfate is a linear sulfated polysaccharide present on proteoglycans found in the extracellular matrix or anchored in the plasma membrane (syndecan). Moreover the LMW FGF-2 secretion appears to be activated upon FGF-1 treatment. In order to estimate quantification of such factor export across the plasma membrane, technical approaches are presented (evaluation of LMW FGF-2: (1) secretion, (2) extracellular matrix reservoir, and (3) secretion modulation by surrounding factors) and the importance of such procedures in the comprehension of the biology of these growth factors is underlined.

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The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 6 100%

Demographic breakdown

Readers by professional status Count As %
Lecturer > Senior Lecturer 1 17%
Student > Doctoral Student 1 17%
Student > Bachelor 1 17%
Researcher 1 17%
Professor > Associate Professor 1 17%
Other 0 0%
Unknown 1 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 33%
Agricultural and Biological Sciences 1 17%
Chemistry 1 17%
Engineering 1 17%
Unknown 1 17%