Literature DB >> 23702329

Protein glycation during aging and in cardiovascular disease.

Andreas Simm1.   

Abstract

Advanced glycation endproducts (AGEs), pathophysiological important posttranslational modifications, are formed in vivo by a non-enzymatic reaction of proteins with reactive carbohydrates and accumulate during aging. They are discussed to be responsible for degenerative diseases. Glycation modifies the structure and function of proteins, induces tissue stiffening via crosslinking and a long-lasting inflammatory response after binding to AGE-receptors. Beside the extracellular matrix, a couple of intracellular proteins are known to be glycated leading to molecular and cellular dysfunction. In the cardiovascular system, AGEs are a major cause of cardiac and vascular dysfunction. Whereas AGEs are discussed to be potential biomarkers for diseases as well as for aging, the molecular analysis of AGEs in body fluids and tissue has still to be further improved. This article is part of a Special Issue entitled: Posttranslational Protein modifications in biology and Medicine.
Copyright © 2013 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Aging; Cardiovascular disease; Diabetes mellitus; Posttranscriptional modification; Protein glycation

Mesh:

Substances:

Year:  2013        PMID: 23702329     DOI: 10.1016/j.jprot.2013.05.012

Source DB:  PubMed          Journal:  J Proteomics        ISSN: 1874-3919            Impact factor:   4.044


  20 in total

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2.  Protein carbamylation is a hallmark of aging.

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3.  Hydrodynamic size-based separation and characterization of protein aggregates from total cell lysates.

Authors:  Maya Tanase; Valerio Zolla; Cristina C Clement; Francesco Borghi; Aleksandra M Urbanska; Jose Antonio Rodriguez-Navarro; Barbara Roda; Andrea Zattoni; Pierluigi Reschiglian; Ana Maria Cuervo; Laura Santambrogio
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4.  Reduced endosomal microautophagy activity in aging associates with enhanced exocyst-mediated protein secretion.

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Journal:  Aging Cell       Date:  2022-09-18       Impact factor: 11.005

Review 5.  Avenues for post-translational protein modification prevention and therapy.

Authors:  Mengyao Tang; Sahir Kalim
Journal:  Mol Aspects Med       Date:  2022-02-25

6.  Increased serotransferrin and ceruloplasmin turnover in diet-controlled patients with type 2 diabetes.

Authors:  Makan Golizeh; Kwangwon Lee; Serguei Ilchenko; Abdullah Ösme; James Bena; Rovshan G Sadygov; Sangeeta R Kashyap; Takhar Kasumov
Journal:  Free Radic Biol Med       Date:  2017-10-25       Impact factor: 7.376

7.  Enhanced Approaches for Identifying Amadori Products: Application to Peanut Allergens.

Authors:  Katina L Johnson; Jason G Williams; Soheila J Maleki; Barry K Hurlburt; Robert E London; Geoffrey A Mueller
Journal:  J Agric Food Chem       Date:  2016-02-05       Impact factor: 5.279

Review 8.  Role of advanced glycation end products in cellular signaling.

Authors:  Christiane Ott; Kathleen Jacobs; Elisa Haucke; Anne Navarrete Santos; Tilman Grune; Andreas Simm
Journal:  Redox Biol       Date:  2014-01-09       Impact factor: 11.799

9.  Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.

Authors:  Fernanda L Sirota; Sebastian Maurer-Stroh; Birgit Eisenhaber; Frank Eisenhaber
Journal:  Proteomics       Date:  2015-07       Impact factor: 3.984

10.  Role of Carbonyl Modifications on Aging-Associated Protein Aggregation.

Authors:  Maya Tanase; Aleksandra M Urbanska; Valerio Zolla; Cristina C Clement; Liling Huang; Kateryna Morozova; Carlo Follo; Michael Goldberg; Barbara Roda; Pierluigi Reschiglian; Laura Santambrogio
Journal:  Sci Rep       Date:  2016-01-18       Impact factor: 4.379

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