Differential regulation of cell functions by CSD peptide subdomains

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• 作者：Charles Reese (1)
  Shanice Dyer (1)
  Beth Perry (1)
  Michael Bonner (1)
  James Oates (1)
  Ann Hofbauer (1)
  William Sessa (3)
  Pascal Bernatchez (4)
  Richard P Visconti (2)
  Jing Zhang (2)
  Corey M Hatfield (1)
  Richard M Silver (1)
  Stanley Hoffman (1) (2)
  Elena Tourkina (1) (5)
  
• 关键词：Caveolin ; 1 ; Monocytes ; Fibrocytes ; Fibroblasts ; Scleroderma (SSc) ; Migration ; TGFβ
• 刊名：Respiratory Research
• 出版年：2013
• 出版时间：December 2013
• 年：2013
• 卷：14
• 期：1
• 全文大小：1755KB
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• 作者单位：Charles Reese (1)
  Shanice Dyer (1)
  Beth Perry (1)
  Michael Bonner (1)
  James Oates (1)
  Ann Hofbauer (1)
  William Sessa (3)
  Pascal Bernatchez (4)
  Richard P Visconti (2)
  Jing Zhang (2)
  Corey M Hatfield (1)
  Richard M Silver (1)
  Stanley Hoffman (1) (2)
  Elena Tourkina (1) (5)
  
  1. Department of Medicine/Division of Rheumatology and Immunology, Medical University of South Carolina, 171 Ashley Avenue, Charleston, SC, 29425, USA
  3. Department of Pharmacology and Vascular Biology and Therapeutics Program, Yale University School of Medicine, New Haven, CT, 06520, USA
  4. Department of Anesthesiology, The James Hogg Research Centre, Heart and Lung Institute at St. Paul’s Hospital, Pharmacology and Therapeutics, University of British Columbia, St. Paul’s Hospital, Vancouver, British Columbia, Canada
  2. Department of Regenerative Medicine and Cell Biology, Medical University of South Carolina, 171 Ashley Avenue, Charleston, SC, 29425, USA
  5. Division of Rheumatology and Immunology, Department of Medicine, Medical University of South Carolina, 96 Jonathan Lucas Street, Suite 912 MSC 637, Charleston, SC, 29425, USA
  

文摘

Background In fibrotic lung diseases, expression of caveolin-1 is decreased in fibroblasts and monocytes. The effects of this deficiency are reversed by treating cells or animals with the caveolin-1 scaffolding domain peptide (CSD, amino acids 82-01 of caveolin-1) which compensates for the lack of caveolin-1. Here we compare the function of CSD subdomains (Cav-A, Cav-B, Cav-C, Cav-AB, and Cav-BC) and mutated versions of CSD (F92A and T90A/T91A/F92A). Methods Migration toward the chemokine CXCL12 and the associated expression of F-actin, CXCR4, and pSmad 2/3 were studied in monocytes from healthy donors and SSc patients. Fibrocyte differentiation was studied using PBMC from healthy donors and SSc patients. Collagen I secretion and signaling were studied in fibroblasts derived from the lung tissue of healthy subjects and SSc patients. Results Cav-BC and CSD at concentrations as low as 0.01?μM inhibited the hypermigration of SSc monocytes and TGFβ-activated Normal monocytes and the differentiation into fibrocytes of SSc and Normal monocytes. While CSD also inhibited the migration of poorly migrating Normal monocytes, Cav-A (and other subdomains to a lesser extent) promoted the migration of Normal monocytes while inhibiting the hypermigration of TGFβ-activated Normal monocytes. The effects of versions of CSD on migration may be mediated in part via their effects on CXCR4, F-actin, and pSmad 2/3 expression. Cav-BC was as effective as CSD in inhibiting fibroblast collagen I and ASMA expression and MEK/ERK signaling. Cav-C and Cav-AB also inhibited collagen I expression, but in many cases did not affect ASMA or MEK/ERK. Cav-A increased collagen I expression in scleroderma lung fibroblasts. Full effects on fibroblasts of versions of CSD required 5?μM peptide. Conclusions Cav-BC retains most of the anti-fibrotic functions of CSD; Cav-A exhibits certain pro-fibrotic functions. Results obtained with subdomains and mutated versions of CSD further suggest that the critical functional residues in CSD depend on the cell type and readout being studied. Monocytes may be more sensitive to versions of CSD than fibroblasts and endothelial cells because the baseline level of caveolin-1 in monocytes is much lower than in these other cell types.