Elongated dermatan sulphate in post-inflammatory healing skin distributes among collagen fibrils separated by enlarged interfibrillar gaps.

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.

[1]  A. Ghahary,et al.  Delayed appearance of decorin in healing burn scars , 2000, Histopathology.

[2]  H. Kitagawa,et al.  Purification and characterization of fetal bovine serum beta-N-acetyl-D-galactosaminyltransferase and beta-D-glucuronyltransferase involved in chondroitin sulfate biosynthesis. , 1999, European journal of biochemistry.

[3]  S. Irie,et al.  Temporal changes in disaccharide composition of dermatan sulfate in the skin after epicutaneous application of hapten. , 1999, Journal of dermatological science.

[4]  B. Pomahac,et al.  Dermatan Sulfate Released after Injury Is a Potent Promoter of Fibroblast Growth Factor-2 Function* , 1998, The Journal of Biological Chemistry.

[5]  Y. Nomura,et al.  Structural Property of Decorin from Small Intestine and its Effect of Type I Collagen Fibril Formation , 1998 .

[6]  John E. Scott,et al.  The structure of interfibrillar proteoglycan bridges (‘shape modules’) in extracellular matrix of fibrous connective tissues and their stability in various chemical environments , 1998, Journal of anatomy.

[7]  T. Nakamura,et al.  Hepatocyte Growth Factor/Scatter Factor Binds with High Affinity to Dermatan Sulfate* , 1998, The Journal of Biological Chemistry.

[8]  Renato V. Iozzo,et al.  Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility , 1997, Journal of Cell Biology.

[9]  I. Weber,et al.  Model Structure of Decorin and Implications for Collagen Fibrillogenesis* , 1996, The Journal of Biological Chemistry.

[10]  J. Scott Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. , 1996, Biochemistry.

[11]  J. Scott,et al.  Extracellular matrix, supramolecular organisation and shape. , 1995, Journal of anatomy.

[12]  A. Ghahary,et al.  Immunohistochemical localization of the proteoglycans decorin, biglycan and versican and transforming growth factor‐β in human post‐burn hypertrophic and mature scars , 1995, Histopathology.

[13]  E. Schönherr,et al.  Decorin-Type I Collagen Interaction , 1995, The Journal of Biological Chemistry.

[14]  J. Scott Morphometry of cupromeronic blue-stained proteoglycan molecules in animal corneas, versus that of purified proteoglycans stained in vitro, implies that tertiary structures contribute to corneal ultrastructure. , 1992, Journal of anatomy.

[15]  H. Dvorak,et al.  Alterations in proteoglycan synthesis common to healing wounds and tumors. , 1991, The American journal of pathology.

[16]  D. Tollefsen,et al.  Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity. , 1991, The Journal of biological chemistry.

[17]  D. Tollefsen,et al.  Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity. , 1990, The Journal of biological chemistry.

[18]  F. Barry Proteoglycans: structure and function. , 1990, Biochemical Society transactions.

[19]  L. Tang,et al.  Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography. , 1989, The Journal of biological chemistry.

[20]  A. Bassols,et al.  Transforming growth factor beta regulates the expression and structure of extracellular matrix chondroitin/dermatan sulfate proteoglycans. , 1988, The Journal of biological chemistry.

[21]  J. Trotter,et al.  The effect of proteoglycans on the morphology of collagen fibrils formed in vitro. , 1987, Collagen and related research.

[22]  J. Scott,et al.  Proteoglycan-type I collagen fibril interactions in bone and non-calcifying connective tissues , 1985, Bioscience reports.

[23]  D. Heinegård,et al.  Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. , 1984, The Biochemical journal.

[24]  J. Scott The periphery of the developing collagen fibril. Quantitative relationships with dermatan sulphate and other surface-associated species. , 1984, The Biochemical journal.

[25]  T. Hardingham,et al.  The control of chondroitin sulphate biosynthesis and its influence on the structure of cartilage proteoglycans. , 1982, The Biochemical journal.

[26]  M. Pacifici,et al.  Changes in the sulfated proteoglycans synthesized by "aging" chondrocytes. II. Organ-cultured vertebral columns. , 1981, The Journal of biological chemistry.

[27]  C. Kischer Collagen and dermal patterns in the hypertrophic scar , 1974, The Anatomical record.

[28]  C. Kischer,et al.  The histiotypic organization of the hypertrophic scar in humans. , 1972, The Journal of investigative dermatology.

[29]  Å. Wasteson A method for the determination of the molecular weight and molecular-weight distribution of chondroitin sulphate. , 1971, Journal of chromatography.

[30]  U. K. Laemmli,et al.  Cleavage of structural proteins during , 1970 .