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LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Questions
  9. Schema
  10. External Links
  11. Analytics And Tracking
  12. Libraries

We are analyzing https://link.springer.com/article/10.1007/s00441-012-1390-z.

Title:
Proteases and the gut barrier | Cell and Tissue Research
Description:
Serine proteases, cysteine proteases, aspartic proteases and matrix metalloproteinases play an essential role in extracellular matrix remodeling and turnover through their proteolytic action on collagens, proteoglycans, fibronectin, elastin and laminin. Proteases can also act on chemokines, receptors and anti-microbial peptides, often potentiating their activity. The intestinal mucosa is the largest interface between the external environment and the tissues of the human body and is constantly exposed to proteolytic enzymes from many sources, including bacteria in the intestinal lumen, fibroblasts and immune cells in the lamina propria and enterocytes. Controlled proteolytic activity is crucial for the maintenance of gut immune homeostasis, for normal tissue turnover and for the integrity of the gut barrier. However, in intestinal immune-mediated disorders, pro-inflammatory cytokines induce the up-regulation of proteases, which become the end-stage effectors of mucosal damage by destroying the epithelium and basement membrane integrity and degrading the extracellular matrix of the lamina propria to produce ulcers. Protease-mediated barrier disruption in turn results in increased amounts of antigen crossing into the lamina propria, driving further immune responses and sustaining the inflammatory process.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {๐Ÿ“š}

  • Education
  • Science
  • Health & Fitness

Content Management System {๐Ÿ“}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {๐Ÿ“ˆ}

What is the average monthly size of link.springer.com audience?

๐ŸŒ  Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

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How Does Link.springer.com Make Money? {๐Ÿ’ธ}

The income method remains a mystery to us.

Not every website is profit-driven; some are created to spread information or serve as an online presence. Websites can be made for many reasons. This could be one of them. Link.springer.com might be earning cash quietly, but we haven't detected the monetization method.

Keywords {๐Ÿ”}

google, scholar, article, pubmed, cas, intestinal, matrix, disease, macdonald, gut, cell, bowel, inflammatory, epithelial, immunol, metalloproteinases, mucosal, metalloproteinase, mmp, expression, pender, barrier, cells, tissue, sabatino, proteases, colitis, biancheri, corazza, mucosa, bacterial, nat, gastroenterology, inflammation, interleukin, monteleone, role, extracellular, human, access, rev, patients, saarialhokere, stromelysin, matrilysin, immune, homeostasis, necrosis, adam, med,

Topics {โœ’๏ธ}

gamma-secretase-dependent e-cadherin cleavage month download article/chapter il-1beta-induced increase vibrio cholera haemagglutinin/protease intestinal alpha-defensin activation protease-mediated barrier disruption gram-negative bacterial pneumonia intestinal immune-mediated disorders pro-inflammatory cytokines induce laminin-5 gamma2-chain expression lipopolysaccharide-induced disruption antonio di sabatinoย &ย gino related subjects transforming growth factor lรณpez-boado ys full article pdf mucosal epithelial cells tnf-alpha convertase intestinal epithelial barrier matrix metalloproteinase-3 secretion bacterial protease perturbs colonic epithelial barrier privacy choices/manage cookies tissue research aims paracellular barrier function transporting epithelial monolayers european economic area t-cell activation antonio di sabatino extracellular matrix remodeling extracellular matrix remodelling extracellular matrix components colonic epithelial cells gut mucosal barrier intraepithelial gamma delta inflammatory bowel diseases inflammatory bowel disease human intestinal fibroblasts walker-smith ja intestinal bacterial infection stromal/epithelial interactions check access salmela mt instant access small intestinal mucosa article cell bowel disease linked intestinal biopsy specimens intestinal wound healing effects epithelial regeneration

Questions {โ“}

  • Ravi A, Garg P, Sitaraman SV (2007) Matrix metalloproteinases in inflammatory bowel disease: boon or a bane?

Schema {๐Ÿ—บ๏ธ}

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         headline:Proteases and the gut barrier
         description:Serine proteases, cysteine proteases, aspartic proteases and matrix metalloproteinases play an essential role in extracellular matrix remodeling and turnover through their proteolytic action on collagens, proteoglycans, fibronectin, elastin and laminin. Proteases can also act on chemokines, receptors and anti-microbial peptides, often potentiating their activity. The intestinal mucosa is the largest interface between the external environment and the tissues of the human body and is constantly exposed to proteolytic enzymes from many sources, including bacteria in the intestinal lumen, fibroblasts and immune cells in the lamina propria and enterocytes. Controlled proteolytic activity is crucial for the maintenance of gut immune homeostasis, for normal tissue turnover and for the integrity of the gut barrier. However, in intestinal immune-mediated disorders, pro-inflammatory cytokines induce the up-regulation of proteases, which become the end-stage effectors of mucosal damage by destroying the epithelium and basement membrane integrity and degrading the extracellular matrix of the lamina propria to produce ulcers. Protease-mediated barrier disruption in turn results in increased amounts of antigen crossing into the lamina propria, driving further immune responses and sustaining the inflammatory process.
         datePublished:2012-03-20T00:00:00Z
         dateModified:2012-03-20T00:00:00Z
         pageStart:269
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            Extracellular matrix
            Inflammatory bowel disease
            Mucosal immunology
            Tumor necrosis factor-alpha
            Human Genetics
            Proteomics
            Molecular Medicine
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      headline:Proteases and the gut barrier
      description:Serine proteases, cysteine proteases, aspartic proteases and matrix metalloproteinases play an essential role in extracellular matrix remodeling and turnover through their proteolytic action on collagens, proteoglycans, fibronectin, elastin and laminin. Proteases can also act on chemokines, receptors and anti-microbial peptides, often potentiating their activity. The intestinal mucosa is the largest interface between the external environment and the tissues of the human body and is constantly exposed to proteolytic enzymes from many sources, including bacteria in the intestinal lumen, fibroblasts and immune cells in the lamina propria and enterocytes. Controlled proteolytic activity is crucial for the maintenance of gut immune homeostasis, for normal tissue turnover and for the integrity of the gut barrier. However, in intestinal immune-mediated disorders, pro-inflammatory cytokines induce the up-regulation of proteases, which become the end-stage effectors of mucosal damage by destroying the epithelium and basement membrane integrity and degrading the extracellular matrix of the lamina propria to produce ulcers. Protease-mediated barrier disruption in turn results in increased amounts of antigen crossing into the lamina propria, driving further immune responses and sustaining the inflammatory process.
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         Mucosal immunology
         Tumor necrosis factor-alpha
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         Proteomics
         Molecular Medicine
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External Links {๐Ÿ”—}(284)

Analytics and Tracking {๐Ÿ“Š}

  • Google Tag Manager

Libraries {๐Ÿ“š}

  • Clipboard.js
  • Prism.js

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