Interaction Between Collagen Type I and Type III in Conditioning Bundles Organization

Lapière, Ch. M.; Nusgens, Betty; Pierard, Gérald

doi:10.3109/03008207709152608

Cited by 245 publications

(81 citation statements)

References 16 publications

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“…Also, the ratio of collagens to each other is important. The collagen I induction, normalized for changes in MMPs and TIMP expression, is much greater than that of type III, which would lead to the formation of larger fibrils compared with naive mice (45). Likewise, fiber size increases with higher collagen I:V ratios, yet the ratio of normalized I:V in both WT and 10/12 KO remains relatively unchanged or slightly increased throughout the time course (46).…”

Section: Discussionmentioning

confidence: 93%

Global Gene Expression Profiles During Acute Pathogen-Induced Pulmonary Inflammation Reveal Divergent Roles for Th1 and Th2 Responses in Tissue Repair

Sandler

Mentink‐Kane

Cheever

et al. 2003

The Journal of Immunology

226

203

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T helper 1 responses are typically proinflammatory, while Th2 responses have been considered regulatory. Interestingly, Th2 responses characterize a number of pulmonary diseases, many of which terminate in tissue remodeling and fibrosis. We developed a mouse model using Schistosoma mansoni eggs and cytokine-deficient mice to induce highly polarized Th1- or Th2-type inflammation in the lung. In this study, we examined the pathology and cytokine profiles in Th1- and Th2-polarized environments and used oligonucleotide microarray analysis to decipher the genes responsible for these effects. We further elaborated on the results using IL-10- and IL-13-deficient mice because these cytokines are believed to be the central regulators of Th2-associated pathology. We found that the Th1-polarized mice developed small granulomas with less fibrosis while expressing genes characteristic of tissue damage. Th2-polarized mice, in contrast, formed large granulomas with massive collagen deposition and up-regulated genes associated with wound healing, specifically, arginase, collagens, matrix metalloproteinases (MMPs), and tissue inhibitors of MMP. In addition, several members of the chitinase-like family were up-regulated in the lung following egg challenge. We also developed a method of defining the net collagen deposition using the expression profiles of several collagen, MMP, and tissue inhibitors of MMP genes. We found that Th1-polarized mice did not elaborate collagens or MMPs and therefore did not have a significant capacity for repair in this model. Thus, Th1-mediated inflammation is characterized by tissue damage, while Th2 directs wound healing and fibrosis.

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Section: Discussionmentioning

confidence: 93%

Global Gene Expression Profiles During Acute Pathogen-Induced Pulmonary Inflammation Reveal Divergent Roles for Th1 and Th2 Responses in Tissue Repair

Sandler

Mentink‐Kane

Cheever

et al. 2003

The Journal of Immunology

226

203

View full text Add to dashboard Cite

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“…Whereas collagen III forms an elastic network storing kinetic energy as elastic recoil, collagen I represents a stiff fibrillar protein providing tensile strength. 25,26 Only the collagen I and not the collagen III promoter is studded with SP-1-binding sites. Therefore, the differential increase of collagen I over collagen III in galectin-3-infused animals could be explained by the possible differences in the molecular makeup of their promoter sites.…”

Section: Significance Of Interstitial Fibrosis and Collagen I Productmentioning

confidence: 99%

Galectin-3 Marks Activated Macrophages in Failure-Prone Hypertrophied Hearts and Contributes to Cardiac Dysfunction

et al. 2004

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Background-Inflammatory mechanisms have been proposed to be important in heart failure (HF), and cytokines have been implicated to add to the progression of HF. However, it is unclear whether such mechanisms are already activated when hypertrophied hearts still appear well-compensated and whether such early mechanisms contribute to the development of HF. Methods and Results-In a comprehensive microarray study, galectin-3 emerged as the most robustly overexpressed gene in failing versus functionally compensated hearts from homozygous transgenic TGRmRen2-27 (Ren-2) rats. Myocardial biopsies obtained at an early stage of hypertrophy before apparent HF showed that expression of galectin-3 was increased specifically in the rats that later rapidly developed HF. Galectin-3 colocalized with activated myocardial macrophages. We found galectin-3-binding sites in rat cardiac fibroblasts and the extracellular matrix. Recombinant galectin-3 induced cardiac fibroblast proliferation, collagen production, and cyclin D1 expression. A 4-week continuous infusion of low-dose galectin-3 into the pericardial sac of healthy Sprague-Dawley rats led to left ventricular dysfunction, with a 3-fold differential increase of collagen I over collagen III. Myocardial galectin-3 expression was increased in aortic stenosis patients with depressed ejection fraction. Conclusions-This study shows that an early increase in galectin-3 expression identifies failure-prone hypertrophied hearts. Galectin-3, a macrophage-derived mediator, induces cardiac fibroblast proliferation, collagen deposition, and ventricular dysfunction. This implies that HF therapy aimed at inflammatory responses may need to be targeted at the early stages of HF and probably needs to antagonize multiple inflammatory mediators, including galectin-3.

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“…After 24 h, the culture mediums and the cell layers were collected separately. The collagen polypeptides were recovered from the cell layer by extraction at 4°C with 0.1 M acetic acid and from the culture medium by differential salt precipitation with ammonium sulfate as described earlier (16). The pattern of labeled collagen polypeptides was analyzed by 6.25% SDS-PAGE in nonreducing conditions and visualized after fluorography.…”

Section: Analysis Of Procollagen Processing In Vivo-for Evaluating Thmentioning

confidence: 99%

“…Collagen was purified from 1 M NaCl extracts by sequential steps of precipitation and solubilization as described earlier (16). The collagen preparation was then treated or not with pyroglutamate aminopeptidase before electrophoresis on a pre-run 7.5% acrylamide/piperazine diacrylamide gel in 50 mM Tris borate buffer (pH 8.3) containing 0.1% SDS and 0.1 mM thioglycolic acid.…”

Section: Analysis Of Procollagen Processing In Vivo-for Evaluating Thmentioning

confidence: 99%

Cloning and Characterization of ADAMTS-14, a Novel ADAMTS Displaying High Homology with ADAMTS-2 and ADAMTS-3

Colige¹,

Vandenberghe²,

Thiry³

et al. 2002

Journal of Biological Chemistry

184

129

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The processing of amino-and carboxyl-propeptides of fibrillar collagens is required to generate collagen monomers that correctly assemble into fibrils. Mutations in the ADAMTS2 gene, the aminopropeptidase of procollagen I and II, result in the accumulation of nonfully processed type I procollagen, causing human Ehlers-Danlos syndrome type VIIC and animal dermatosparaxis. In this study, we show that the aminopropeptide of type I procollagen can be cleaved in vivo in absence of ADAMTS-2 activity and that this processing is performed at the cleavage site for ADAMTS-2. In an attempt to identify the enzyme responsible for this alternative aminoprocollagen peptidase activity, we have cloned the cDNA and determined the primary structure of human and mouse ADAMTS-14, a novel ADAMTS displaying striking homologies with ADAMTS-2 and -3. The structure of the human gene, which maps to 10q21.3, and the mechanisms of generation of the various transcripts are described. The existence of two sites of initiation of transcription, in two different promoter contexts, suggests that transcripts resulting from these two sites can be differently regulated. The tissue distribution of AD-AMTS-14, the regulation of the gene expression by various cytokines and the activity of the recombinant enzyme are evaluated. The potential function of ADAMTS-14 as a physiological aminoprocollagen peptidase in vivo is discussed. ADAMTS1 (A Disintegrin and metalloprotease with thrombospondin type I repeats) is a novel family of metalloproteases found in vertebrates and invertebrates. These enzymes are related to ADAMs as judged from sequence homology and conserved domains such as a characteristic metalloprotease domain and a disintegrin-like module. However, they differ from ADAMs by their domain organization and the presence of distinct features. The most specific hallmark is the presence of a central thrombospondin type I repeat (TSPI) between the disintegrin-like module and the Cys-rich domain. All ADAMTS, except ADAMTS-4, contain also TSPI-like domains in varying numbers at the COOH terminus (1, 2). Currently, 12 ADAMTS from vertebrates and a few from invertebrates (Drosophila and Caenorhabditis elegans) have been described (1, 2). AD-AMTS-1, -4, and -5 are able to cleave proteoglycans and are probably involved in cartilage degradation during arthritis (3-5). ADAMTS-1 and -8 are potent anti-angiogenic molecules (6). Adamts1Ϫ/Ϫ mice display abnormal growth, defective fertility, and altered organ morphology and function (7). A C. elegans Adamts, gon-1, was found essential for gonadal morphogenesis (8). Both the metalloprotease domain and some TSPI-like repeats are required for the control of this process.The primarily described activity of ADAMTS-2 is to excise the aminopropeptide of type I and type II procollagens, explaining its former trivial name aminoprocollagen I/II peptidase (9, 10). Removal of the N-and C-propeptide of type I procollagen is required to generate collagen monomers able to assemble into elongated and cylindrical collagen fibers. H...

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Interaction Between Collagen Type I and Type III in Conditioning Bundles Organization

Cited by 245 publications

References 16 publications

Global Gene Expression Profiles During Acute Pathogen-Induced Pulmonary Inflammation Reveal Divergent Roles for Th1 and Th2 Responses in Tissue Repair

Global Gene Expression Profiles During Acute Pathogen-Induced Pulmonary Inflammation Reveal Divergent Roles for Th1 and Th2 Responses in Tissue Repair

Galectin-3 Marks Activated Macrophages in Failure-Prone Hypertrophied Hearts and Contributes to Cardiac Dysfunction

Cloning and Characterization of ADAMTS-14, a Novel ADAMTS Displaying High Homology with ADAMTS-2 and ADAMTS-3

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