Literature DB >> 19165811

Low molecular weight proteins in urines from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients: a MALDI study.

Annunziata Lapolla1, Roberta Seraglia, Laura Molin, Katherine Williams, Chiara Cosma, Rachele Reitano, Annalisa Sechi, Eugenio Ragazzi, Pietro Traldi.   

Abstract

Urine samples from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients were analyzed by matrix assisted laser desorption/ionization (MALDI) mass spectrometry in order to establish evidence of some possible differences in the peptide profile related to the pathological states. Multivariate analysis suggested the possibility of a distinction among the considered groups of patients. Some differences have been found, in particular, in the relative abundances of three ions at m/z 1912, 1219 and 2049. For these reasons, further investigation was carried out by MALDI/TOF/TOF to determine the sequence of these peptides and, consequently, to individuate their possible origin. By this approach, the peptide at m/z 1912 was found to originate from uromodulin, and its lower expression in the case of nephropathy can be well related to the pathological condition. Ions at m/z 2049 and 1219 originate from the collagen alpha-1(I) chain precursor and from the collagen alpha-5 (IV) chain precursor, respectively, and, also in this case, their different expressions can be related to the pathologies under investigation. The obtained data seem to indicate that urine is an interesting biological fluid to investigate on the peptide profile and to obtain, consequently, information on the dismetabolism activated by specific pathologies. Copyright (c) 2009 John Wiley & Sons, Ltd.

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Year:  2009        PMID: 19165811     DOI: 10.1002/jms.1520

Source DB:  PubMed          Journal:  J Mass Spectrom        ISSN: 1076-5174            Impact factor:   1.982


  14 in total

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Authors:  Matthew P Welberry Smith; Rosamonde E Banks; Steven L Wood; Andrew J P Lewington; Peter J Selby
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Review 3.  Urinary proteomics as a novel tool for biomarker discovery in kidney diseases.

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4.  Urinary collagen fragments are significantly altered in diabetes: a link to pathophysiology.

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Journal:  PLoS One       Date:  2010-09-28       Impact factor: 3.240

Review 5.  Urinary Proteomics for Diagnosis and Monitoring of Diabetic Nephropathy.

Authors:  G Currie; C Delles
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6.  A urinary peptide biomarker set predicts worsening of albuminuria in type 2 diabetes mellitus.

Authors:  S S Roscioni; D de Zeeuw; M E Hellemons; H Mischak; P Zürbig; S J L Bakker; R T Gansevoort; H Reinhard; F Persson; M Lajer; P Rossing; H J Lambers Heerspink
Journal:  Diabetologia       Date:  2012-10-20       Impact factor: 10.122

7.  Mass spectrometry for diabetic nephropathy monitoring: new effective tools for physicians.

Authors:  Annunziata Lapolla; Simona Porcu; Pietro Traldi
Journal:  ISRN Endocrinol       Date:  2012-05-20

8.  Urine proteome analysis may allow noninvasive differential diagnosis of diabetic nephropathy.

Authors:  Massimo Papale; Salvatore Di Paolo; Riccardo Magistroni; Olga Lamacchia; Anna Maria Di Palma; Angela De Mattia; Maria Teresa Rocchetti; Luciana Furci; Sonia Pasquali; Salvatore De Cosmo; Mauro Cignarelli; Loreto Gesualdo
Journal:  Diabetes Care       Date:  2010-07-29       Impact factor: 17.152

9.  Poor histological lesions in IgA nephropathy may be reflected in blood and urine peptide profiling.

Authors:  Fredzzia Graterol; Maribel Navarro-Muñoz; Meritxell Ibernon; Dolores López; Maria-Isabel Troya; Vanessa Pérez; Josep Bonet; Ramón Romero
Journal:  BMC Nephrol       Date:  2013-04-11       Impact factor: 2.388

10.  Protein glycation in diabetes as determined by mass spectrometry.

Authors:  Annunziata Lapolla; Laura Molin; Pietro Traldi
Journal:  Int J Endocrinol       Date:  2013-03-13       Impact factor: 3.257

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