Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P39060 (endostatin)
 2,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Skin-derived precursors (SKPs) can differentiate into fibroblasts. However, little is known about the molecular mechanism of the differentiation process. Our previous study has compared the transcriptomes of mouse SKPs and SKP-derived fibroblasts (SFBs) by RNA-Seq analysis and found some genes and signal pathways that might play important roles in the transition from SKPs to SFBs. Here, to further investigate the process by which SKPs differentiate into fibroblasts, we compared the proteomes between SKPs and SFBs using iTRAQ. Our results showed that 243 differentially expressed proteins (DEPs) were identified. Among the 28 DEPs which were related to the functional group of cell differentiation, Down-regulated DEPs collagen XVIII, keratin 10, keratin 5, keratin 14, and TIFIbeta, up-regulated DEPs Thy-1, ANXA1, alpha-catenin, and calreticulin might play important roles in the transition of SKPs to fibroblasts. Further study is needed to clarify the roles of these proteins in the differentiation process of SKPs into fibroblasts, which could facilitate investigations of the detailed molecular mechanisms in the process and make it possible to take advantage of the potential therapeutic applications of SKPs in skin regeneration in the future.
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PMID:Comparison of the proteomes of mouse Skin Derived Precursors (SKPs) and SKP-derived fibroblasts (SFBs) by iTRAQ. 2874 44

Epithelial keratinization involves complex cellular modifications that provide protection against pathogens and chemical and mechanical injuries. In the oral cavity, keratinized mucosa is also crucial to maintain healthy periodontal or peri-implant tissues. In this study, we investigated the roles of type XVIII collagen, a collagen-glycosaminoglycan featuring an extracellular matrix component present in the basement membrane, in oral mucosal keratinization. Histological analysis of keratinized and non-keratinized oral mucosa showed that type XVIII collagen was highly expressed in keratinized mucosa. Additionally, a 3D culture system using human squamous carcinoma cells (TR146) was used to evaluate and correlate the changes in the expression of type XVIII collagen gene, COL18A1, and epithelial keratinization-related markers, e.g., keratin 1 (KRT1) and 10 (KRT10). The results showed that the increase in COL18A1 expression followed the increase in KRT1 and KRT10 mRNA levels. Additionally, loss-of-function analyses using silencing RNA targeting COL18A1 mRNA and a Col18-knockout (KO) mouse revealed that the absence of type XVIII collagen induces a dramatic decrease in KRT10 expression as well as in the number and size of keratohyalin granules. Together, the results of this study demonstrate the importance of type XVIII collagen in oral mucosal keratinization.
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PMID:Type XVIII Collagen Modulates Keratohyalin Granule Formation and Keratinization in Oral Mucosa. 3155 64