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We are analyzing https://link.springer.com/article/10.1007/s00418-006-0184-3.

Title:
Immunohistochemical study of NG2 chondroitin sulfate proteoglycan expression in the small and large intestines | Histochemistry and Cell Biology
Description:
The intestinal subepithelial myofibroblasts (ISEMFs) are located in the lamina propria under the epithelial cells. ISEMFs are thought to have an important role in protecting and maintaining the integrity of the epithelial cell layer and also in the process of wound healing. In this study, we report that the membrane-bound proteoglycan NG2 is abundantly distributed in the ISEMF layer of the mouse and human intestines. NG2 immunostaining in this layer is distributed with similar intensity from the crypt to villi. NG2 is also immunolocalized along the membranes of smooth muscle cells in the intestinal muscle layer. However, skeletal and cardiac muscles are not immunostained for NG2, demonstrating selective expression of the proteoglycan by smooth muscle cells. Using electron microscopy, NG2 immunoreactivity was strongly observed along the cell membranes of ISEMF, with weak diffusion into the neighboring matrix, indicative of the presence of some β€œshed” NG2. This first report of NG2 proteoglycan expression by ISEMF provides insights into the nature of the interaction of these cells with extracellular matrix and/or intestinal epithelial cells.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {πŸ“š}

  • Education
  • Telecommunications
  • Science

Content Management System {πŸ“}

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 {πŸ“ˆ}

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

🌠 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.
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How Does Link.springer.com Make Money? {πŸ’Έ}

We don't see any clear sign of profit-making.

Not all websites are made for profit; some exist to inform or educate users. Or any other reason why people make websites. And this might be the case. Link.springer.com might have a hidden revenue stream, but it's not something we can detect.

Keywords {πŸ”}

google, scholar, article, pubmed, cas, cell, proteoglycan, stallcup, cells, biol, expression, myofibroblasts, human, intestinal, nishiyama, terada, ohno, physiol, chondroitin, sulfate, matrix, access, privacy, cookies, content, study, epithelial, mol, protein, growth, development, publish, research, search, immunohistochemical, shinichi, subepithelial, layer, muscle, brain, normal, colonic, neurosci, factor, dahlinhuppe, differentiation, trapp, expressed, yamanashi, data,

Topics {βœ’οΈ}

platelet-derived growth factor-aa month download article/chapter membrane-bound proteoglycan ng2 membrane-spanning proteoglycan ng2 adegboyega pa extracellular matrix related subjects type vi collagen cell surface proteolysis full article pdf glial cell population beta iv tubulin ng2 proteoglycan expression powell dw ng2+ glial cells privacy choices/manage cookies ng2 proteoglycan leads cell biology aims membrane skeletal molecule normal colonic mucosa chondroitin sulfate intestinal subepithelial myofibroblasts schwann cells ryohei katoh demonstrating selective expression article terada mesenchymal cell system normal human tissues developing rodent brain article histochemistry ng2 knockout mouse smooth muscle cells european economic area adenomatous colorectal polyps ulcerative colitis patients cytoskeletal reorganization induced high-affinity binding putative instructive properties fine structural aspects inflammatory bowel differentiation acetic acid treatment duchenne muscular dystrophies interdisciplinary graduate school shinichi murata epithelial cell layer developing rat brain conditions privacy policy o2a progenitor cells progenitor cells committed check access

Schema {πŸ—ΊοΈ}

WebPage:
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         headline:Immunohistochemical study of NG2 chondroitin sulfate proteoglycan expression in the small and large intestines
         description:The intestinal subepithelial myofibroblasts (ISEMFs) are located in the lamina propria under the epithelial cells. ISEMFs are thought to have an important role in protecting and maintaining the integrity of the epithelial cell layer and also in the process of wound healing. In this study, we report that the membrane-bound proteoglycan NG2 is abundantly distributed in the ISEMF layer of the mouse and human intestines. NG2 immunostaining in this layer is distributed with similar intensity from the crypt to villi. NG2 is also immunolocalized along the membranes of smooth muscle cells in the intestinal muscle layer. However, skeletal and cardiac muscles are not immunostained for NG2, demonstrating selective expression of the proteoglycan by smooth muscle cells. Using electron microscopy, NG2 immunoreactivity was strongly observed along the cell membranes of ISEMF, with weak diffusion into the neighboring matrix, indicative of the presence of some β€œshed” NG2. This first report of NG2 proteoglycan expression by ISEMF provides insights into the nature of the interaction of these cells with extracellular matrix and/or intestinal epithelial cells.
         datePublished:2006-04-20T00:00:00Z
         dateModified:2006-04-20T00:00:00Z
         pageStart:483
         pageEnd:490
         sameAs:https://doi.org/10.1007/s00418-006-0184-3
         keywords:
            NG2 proteoglycan
            Myofibroblast
            Intestine
            Immunohistochemistry
            Biomedicine
            general
            Cell Biology
            Biochemistry
            Developmental Biology
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                        type:PostalAddress
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      headline:Immunohistochemical study of NG2 chondroitin sulfate proteoglycan expression in the small and large intestines
      description:The intestinal subepithelial myofibroblasts (ISEMFs) are located in the lamina propria under the epithelial cells. ISEMFs are thought to have an important role in protecting and maintaining the integrity of the epithelial cell layer and also in the process of wound healing. In this study, we report that the membrane-bound proteoglycan NG2 is abundantly distributed in the ISEMF layer of the mouse and human intestines. NG2 immunostaining in this layer is distributed with similar intensity from the crypt to villi. NG2 is also immunolocalized along the membranes of smooth muscle cells in the intestinal muscle layer. However, skeletal and cardiac muscles are not immunostained for NG2, demonstrating selective expression of the proteoglycan by smooth muscle cells. Using electron microscopy, NG2 immunoreactivity was strongly observed along the cell membranes of ISEMF, with weak diffusion into the neighboring matrix, indicative of the presence of some β€œshed” NG2. This first report of NG2 proteoglycan expression by ISEMF provides insights into the nature of the interaction of these cells with extracellular matrix and/or intestinal epithelial cells.
      datePublished:2006-04-20T00:00:00Z
      dateModified:2006-04-20T00:00:00Z
      pageStart:483
      pageEnd:490
      sameAs:https://doi.org/10.1007/s00418-006-0184-3
      keywords:
         NG2 proteoglycan
         Myofibroblast
         Intestine
         Immunohistochemistry
         Biomedicine
         general
         Cell Biology
         Biochemistry
         Developmental Biology
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            name:Nobuo Terada
            affiliation:
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                  address:
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                     type:PostalAddress
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            email:[email protected]
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            name:Nobuhiko Ohno
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                  address:
                     name:Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
                     type:PostalAddress
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            name:Shinichi Murata
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                     name:Cancer Research Center, The Burnham Institute, La Jolla, USA
                     type:PostalAddress
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            name:Shinichi Ohno
            affiliation:
                  name:University of Yamanashi
                  address:
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      name:University of Yamanashi
      address:
         name:Department of Human Pathology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
         type:PostalAddress
      name:The Burnham Institute
      address:
         name:Cancer Research Center, The Burnham Institute, La Jolla, USA
         type:PostalAddress
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      address:
         name:Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
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            address:
               name:Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
               type:PostalAddress
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      email:[email protected]
      name:Nobuhiko Ohno
      affiliation:
            name:University of Yamanashi
            address:
               name:Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
               type:PostalAddress
            type:Organization
      name:Shinichi Murata
      affiliation:
            name:University of Yamanashi
            address:
               name:Department of Human Pathology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
               type:PostalAddress
            type:Organization
      name:Ryohei Katoh
      affiliation:
            name:University of Yamanashi
            address:
               name:Department of Human Pathology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
               type:PostalAddress
            type:Organization
      name:William B. Stallcup
      affiliation:
            name:The Burnham Institute
            address:
               name:Cancer Research Center, The Burnham Institute, La Jolla, USA
               type:PostalAddress
            type:Organization
      name:Shinichi Ohno
      affiliation:
            name:University of Yamanashi
            address:
               name:Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
               type:PostalAddress
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      name:Department of Human Pathology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
      name:Department of Human Pathology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
      name:Cancer Research Center, The Burnham Institute, La Jolla, USA
      name:Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan
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External Links {πŸ”—}(140)

Analytics and Tracking {πŸ“Š}

  • Google Tag Manager

Libraries {πŸ“š}

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