The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Elongated dermatan sulphate in post-inflammatory healing skin distributes among collagen fibrils separated by enlarged interfibrillar gaps
Open accessAbstract
It has been reported that the disaccharide composition of dermatan sulphate shows transient changes after epicutaneous application of the hapten 2,4-dinitrofluorobenzene to mouse skin, and that these changes are most conspicuous in healing skin on day 15 after chemical insult [Kuwaba, Nomura, Irie and Koyama (1999) J. Dermatol. Sci. 19, 23–30]. In the present study it was found that the molecular size of dermatan sulphate was increased on day 15 after hapten application. The molecular size of decorin increased in healing skin, whereas the size of dermatan-sulphate-depleted core protein did not increase. The length and localization of decorin dermatan sulphate were investigated by electron microscopy. Dermatan sulphate filaments oriented orthogonally to collagen fibrils were longer in healing skin than in control skin. In control skin, dermatan sulphate filaments were found among tightly packed collagen fibrils. In contrast, the interfibrillar gaps between each collagen fibril were enlarged in healing skin; elongated dermatan sulphate filaments extended from the surface of collagen fibrils across the enlarged gap. These results suggest that the increase in molecular size of decorin dermatan sulphate is important in organizing collagen fibrils separated by enlarged interfibrillar gaps in healing skin.
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“The initial scar tissue, characterized by delicate, accidentally organized collagen fibers, typical for proliferation phase, is replaced by a matrix which resembles the dermis in which mature, cross-linked collagen fibers, of the proper diameter, construct a framework of the newly formed tissue”
From The role of the extracellular matrix components in cutaneous wound healing (2014) · cites this paper as [88]
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The role of the extracellular matrix components in cutaneous wound healing
Olczyk, P., Mencner, Ł., & Komosinska-Vassev, K. (2014) · BioMed Research International · doi:10.1155/2014/747584 · Cited by 387
Metadata
- Authors
- KUWABA, K., KOBAYASHI, M., NOMURA, Y., IRIE, S., & KOYAMA, Y.-I.
- Affiliations
- Nippi Research Institute of Biomatrix, Nippi Inc., 1-1 Senju-Midoricho, Adachi-ku, Tokyo 120-8601, Japan
- Nagoya University (JP)
- Tokyo University of Agriculture and Technology (JP)
- Corresponding author
- KUWABA, Kumiko
- IRIE, Shinkichi
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2001-08-08
- Volume
- 358
- Issue
- 1
- Pages
- 157-163
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1222043
- OpenAlex
- W1990521708
- Cited by
- 30
- References
- 35
- Citations by year
- 2022: 1 · 2018: 1 · 2017: 2 · 2015: 1 · 2014: 3 · 2013: 3 · 2012: 2
- FWCI
- 0.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Keywords
- dermatan sulfate, decorin, collagen fibrils, molecular size, 2,4-dinitrofluorobenzene, extracellular matrix
- MeSH terms
- Animals, Anticoagulants, Chondroitin Sulfates, Chromatography, High Pressure Liquid, Collagen, Dermatan Sulfate, Electrophoresis, Polyacrylamide Gel, Female, Inflammation, Mice, Inbred BALB C, Microscopy, Electron, Proteoglycans, Skin, Time Factors, Ultrasonography, Wound Healing, Blotting, Western, Extracellular Matrix Proteins, Mice, Decorin
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