Processing of chromogranins/secretogranin in patients with diabetic retinopathy

Isabelle Fournier, David Gaucher, Jean F. Chich, Charlotte Bach, Peiman Shooshtarizadeh, Serge Picaud, Tristan Bourcier, Claude Speeg-Schatz, Jean M. Strub, Alain Van Dorsselaer, Angelo Corti, Dominique Aunis, Marie H. Metz-Boutigue

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Aims: Inflammation has been linked to the development of diabetic retinopathy (DR). Chromogranins A, B (CgA, CgB) and secretogranin II (SgII), are prohormones overexpressed in inflammatory diseases. The present study was conducted to evaluate the presence and processing of these prohormones in the vitreous of patients with DR (DV), compared with nondiabetic vitreous (NDV). Methods: Thirteen DV and 14 NDV samples were collected during vitreoretinal surgery. ELISA, Western blot, RP-HPLC, dot blot, protein sequencing and mass spectrometry were used to study the quantitative expression and the processing of CgA, CgB and SgII. Results: CgA, CgB and SgII presence was higher in DV than in NDV. Mean concentration of CgA evaluated by ELISA was 90.8 (±90.1) n L±1 in DV vs. 29.7 (±20.9) in NDV (p=0.039). In NDV, Western blot indicated that only short CgB-derived peptides were identified. In DV, proteomic analyses showed that long CgA-, CgB- and SgII-derived fragments and ±1-antitrypsin were overexpressed, suggesting possible inhibition of the proteolytic process. Conclusions: This study shows differences in the presence and endogenous processing of CgA, CgB and SgII from DV vs. NDV. In DV, the increase of complete granins and the attenuation of their endogenous proteolytic processing could participate in DR progression by reducing the presence of regulatory peptides, important for the pro-/anti-angiogenic balance in the eye.

Original languageEnglish
JournalRegulatory Peptides
Volume167
Issue number1
DOIs
Publication statusPublished - Feb 25 2011

Fingerprint

Secretogranin II
Chromogranins
Diabetic Retinopathy
Processing
Chromogranin B
Western Blotting
Enzyme-Linked Immunosorbent Assay
Vitreoretinal Surgery
Chromogranin A
Peptides
Protein Sequence Analysis
Proteomics
Surgery
Mass spectrometry
Mass Spectrometry
High Pressure Liquid Chromatography
Inflammation
Proteins

Keywords

  • Chromogranin
  • Diabetic retinopathy
  • Neuropeptides
  • Physiopathology
  • Proteomics
  • Secretogranin

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Fournier, I., Gaucher, D., Chich, J. F., Bach, C., Shooshtarizadeh, P., Picaud, S., ... Metz-Boutigue, M. H. (2011). Processing of chromogranins/secretogranin in patients with diabetic retinopathy. Regulatory Peptides, 167(1). https://doi.org/10.1016/j.regpep.2010.12.004

Processing of chromogranins/secretogranin in patients with diabetic retinopathy. / Fournier, Isabelle; Gaucher, David; Chich, Jean F.; Bach, Charlotte; Shooshtarizadeh, Peiman; Picaud, Serge; Bourcier, Tristan; Speeg-Schatz, Claude; Strub, Jean M.; Van Dorsselaer, Alain; Corti, Angelo; Aunis, Dominique; Metz-Boutigue, Marie H.

In: Regulatory Peptides, Vol. 167, No. 1, 25.02.2011.

Research output: Contribution to journalArticle

Fournier, I, Gaucher, D, Chich, JF, Bach, C, Shooshtarizadeh, P, Picaud, S, Bourcier, T, Speeg-Schatz, C, Strub, JM, Van Dorsselaer, A, Corti, A, Aunis, D & Metz-Boutigue, MH 2011, 'Processing of chromogranins/secretogranin in patients with diabetic retinopathy', Regulatory Peptides, vol. 167, no. 1. https://doi.org/10.1016/j.regpep.2010.12.004
Fournier I, Gaucher D, Chich JF, Bach C, Shooshtarizadeh P, Picaud S et al. Processing of chromogranins/secretogranin in patients with diabetic retinopathy. Regulatory Peptides. 2011 Feb 25;167(1). https://doi.org/10.1016/j.regpep.2010.12.004
Fournier, Isabelle ; Gaucher, David ; Chich, Jean F. ; Bach, Charlotte ; Shooshtarizadeh, Peiman ; Picaud, Serge ; Bourcier, Tristan ; Speeg-Schatz, Claude ; Strub, Jean M. ; Van Dorsselaer, Alain ; Corti, Angelo ; Aunis, Dominique ; Metz-Boutigue, Marie H. / Processing of chromogranins/secretogranin in patients with diabetic retinopathy. In: Regulatory Peptides. 2011 ; Vol. 167, No. 1.
@article{c68dbb42f81147a7a3e555f0bf0e6494,
title = "Processing of chromogranins/secretogranin in patients with diabetic retinopathy",
abstract = "Aims: Inflammation has been linked to the development of diabetic retinopathy (DR). Chromogranins A, B (CgA, CgB) and secretogranin II (SgII), are prohormones overexpressed in inflammatory diseases. The present study was conducted to evaluate the presence and processing of these prohormones in the vitreous of patients with DR (DV), compared with nondiabetic vitreous (NDV). Methods: Thirteen DV and 14 NDV samples were collected during vitreoretinal surgery. ELISA, Western blot, RP-HPLC, dot blot, protein sequencing and mass spectrometry were used to study the quantitative expression and the processing of CgA, CgB and SgII. Results: CgA, CgB and SgII presence was higher in DV than in NDV. Mean concentration of CgA evaluated by ELISA was 90.8 (±90.1) n L±1 in DV vs. 29.7 (±20.9) in NDV (p=0.039). In NDV, Western blot indicated that only short CgB-derived peptides were identified. In DV, proteomic analyses showed that long CgA-, CgB- and SgII-derived fragments and ±1-antitrypsin were overexpressed, suggesting possible inhibition of the proteolytic process. Conclusions: This study shows differences in the presence and endogenous processing of CgA, CgB and SgII from DV vs. NDV. In DV, the increase of complete granins and the attenuation of their endogenous proteolytic processing could participate in DR progression by reducing the presence of regulatory peptides, important for the pro-/anti-angiogenic balance in the eye.",
keywords = "Chromogranin, Diabetic retinopathy, Neuropeptides, Physiopathology, Proteomics, Secretogranin",
author = "Isabelle Fournier and David Gaucher and Chich, {Jean F.} and Charlotte Bach and Peiman Shooshtarizadeh and Serge Picaud and Tristan Bourcier and Claude Speeg-Schatz and Strub, {Jean M.} and {Van Dorsselaer}, Alain and Angelo Corti and Dominique Aunis and Metz-Boutigue, {Marie H.}",
year = "2011",
month = "2",
day = "25",
doi = "10.1016/j.regpep.2010.12.004",
language = "English",
volume = "167",
journal = "Regulatory Peptides",
issn = "0167-0115",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Processing of chromogranins/secretogranin in patients with diabetic retinopathy

AU - Fournier, Isabelle

AU - Gaucher, David

AU - Chich, Jean F.

AU - Bach, Charlotte

AU - Shooshtarizadeh, Peiman

AU - Picaud, Serge

AU - Bourcier, Tristan

AU - Speeg-Schatz, Claude

AU - Strub, Jean M.

AU - Van Dorsselaer, Alain

AU - Corti, Angelo

AU - Aunis, Dominique

AU - Metz-Boutigue, Marie H.

PY - 2011/2/25

Y1 - 2011/2/25

N2 - Aims: Inflammation has been linked to the development of diabetic retinopathy (DR). Chromogranins A, B (CgA, CgB) and secretogranin II (SgII), are prohormones overexpressed in inflammatory diseases. The present study was conducted to evaluate the presence and processing of these prohormones in the vitreous of patients with DR (DV), compared with nondiabetic vitreous (NDV). Methods: Thirteen DV and 14 NDV samples were collected during vitreoretinal surgery. ELISA, Western blot, RP-HPLC, dot blot, protein sequencing and mass spectrometry were used to study the quantitative expression and the processing of CgA, CgB and SgII. Results: CgA, CgB and SgII presence was higher in DV than in NDV. Mean concentration of CgA evaluated by ELISA was 90.8 (±90.1) n L±1 in DV vs. 29.7 (±20.9) in NDV (p=0.039). In NDV, Western blot indicated that only short CgB-derived peptides were identified. In DV, proteomic analyses showed that long CgA-, CgB- and SgII-derived fragments and ±1-antitrypsin were overexpressed, suggesting possible inhibition of the proteolytic process. Conclusions: This study shows differences in the presence and endogenous processing of CgA, CgB and SgII from DV vs. NDV. In DV, the increase of complete granins and the attenuation of their endogenous proteolytic processing could participate in DR progression by reducing the presence of regulatory peptides, important for the pro-/anti-angiogenic balance in the eye.

AB - Aims: Inflammation has been linked to the development of diabetic retinopathy (DR). Chromogranins A, B (CgA, CgB) and secretogranin II (SgII), are prohormones overexpressed in inflammatory diseases. The present study was conducted to evaluate the presence and processing of these prohormones in the vitreous of patients with DR (DV), compared with nondiabetic vitreous (NDV). Methods: Thirteen DV and 14 NDV samples were collected during vitreoretinal surgery. ELISA, Western blot, RP-HPLC, dot blot, protein sequencing and mass spectrometry were used to study the quantitative expression and the processing of CgA, CgB and SgII. Results: CgA, CgB and SgII presence was higher in DV than in NDV. Mean concentration of CgA evaluated by ELISA was 90.8 (±90.1) n L±1 in DV vs. 29.7 (±20.9) in NDV (p=0.039). In NDV, Western blot indicated that only short CgB-derived peptides were identified. In DV, proteomic analyses showed that long CgA-, CgB- and SgII-derived fragments and ±1-antitrypsin were overexpressed, suggesting possible inhibition of the proteolytic process. Conclusions: This study shows differences in the presence and endogenous processing of CgA, CgB and SgII from DV vs. NDV. In DV, the increase of complete granins and the attenuation of their endogenous proteolytic processing could participate in DR progression by reducing the presence of regulatory peptides, important for the pro-/anti-angiogenic balance in the eye.

KW - Chromogranin

KW - Diabetic retinopathy

KW - Neuropeptides

KW - Physiopathology

KW - Proteomics

KW - Secretogranin

UR - http://www.scopus.com/inward/record.url?scp=79951683117&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79951683117&partnerID=8YFLogxK

U2 - 10.1016/j.regpep.2010.12.004

DO - 10.1016/j.regpep.2010.12.004

M3 - Article

C2 - 21185877

AN - SCOPUS:79951683117

VL - 167

JO - Regulatory Peptides

JF - Regulatory Peptides

SN - 0167-0115

IS - 1

ER -