Open AccessComparative proteomic analysis of human lung telocytes with fibroblasts
Author(s) -
Zheng Yonghua,
Cretoiu Dragos,
Yan Guoquan,
Cretoiu Sanda Maria,
Popescu Laurentiu M.,
Wang Xiangdong
Publication year - 2014
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/jcmm.12290
Subject(s) - proteome , extracellular matrix , proteomics , cytoskeleton , extracellular , microbiology and biotechnology , chemistry , molecular mass , biology , tandem mass spectrometry , biochemistry , mass spectrometry , cell , gene , enzyme , chromatography
Abstract Telocytes ( TC s) were recently described as interstitial cells with very long prolongations named telopodes (Tps; www.telocytes.com ). Establishing the TC proteome is a priority to show that TC s are a distinct type of cells. Therefore, we examined the molecular aspects of lung TC s by comparison with fibroblasts ( FB s). Proteins extracted from primary cultures of these cells were analysed by automated 2‐dimensional nano‐electrospray ionization liquid chromatography tandem mass spectrometry (2D Nano‐ ESI LC ‐ MS / MS ). Differentially expressed proteins were screened by two‐sample t ‐test ( P < 0.05) and fold change (>2), based on the bioinformatics analysis. We identified hundreds of proteins up‐ or down‐regulated, respectively, in TC s as compared with FB s. TC proteins with known identities are localized in the cytoskeleton (87%) and plasma membrane (13%), while FB up‐regulated proteins are in the cytoskeleton (75%) and destined to extracellular matrix (25%). These identified proteins were classified into different categories based on their molecular functions and biological processes. While the proteins identified in TC s are mainly involved in catalytic activity (43%) and as structural molecular activity (25%), the proteins in FB s are involved in catalytic activity (24%) and in structural molecular activity, particularly synthesis of collagen and other extracellular matrix components (25%). Anyway, our data show that TC s are completely different from FB s. In conclusion, we report here the first extensive identification of proteins from TC s using a quantitative proteomics approach. Protein expression profile shows many up‐regulated proteins e.g . myosin‐14, periplakin, suggesting that TC s might play specific roles in mechanical sensing and mechanochemical conversion task, tissue homoeostasis and remodelling/renewal. Furthermore, up‐regulated proteins matching those found in extracellular vesicles emphasize TC s roles in intercellular signalling and stem cell niche modulation. The novel proteins identified in TC s will be an important resource for further proteomic research and it will possibly allow biomarker identification for TC s. It also creates the premises for understanding the pathogenesis of some lung diseases involving TC s.