The Proteoglycans in Hypertrophic Scar

Honda, Tomohito; Matsunaga, Etsuji; Katagiri, Kazumoto; Shinkai, Hiroshi

doi:10.1111/j.1346-8138.1986.tb02950.x

Cited by 10 publications

(3 citation statements)

References 22 publications

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“…Moreover, recent data show that highly sulfated chondroitin sulfate may protect fibroblasts of the HS from activation of alpha-smooth actin expression after stimulation by transforming growth factor-beta, the major regulator of fibrosis [52]. In this study, we did not identify the individual GAG types as this question has been addressed in several studies [6,43,[52][53][54][55][56][57][58][59][60][61][62][63][64][65][66]. However, our current findings clearly point to the role of GAGs in HS maturation, and therefore we expect that further, more targeted research in this area may help for better control of the scar tissue remodeling.…”

Section: Discussionmentioning

confidence: 93%

Modeling of Old Scars: Histopathological, Biochemical and Thermal Analysis of the Scar Tissue Maturation

Fayzullin

Ignatieva

Захаркина

et al. 2021

Biology

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Mature hypertrophic scars (HSs) remain a challenging clinical problem, particularly due to the absence of biologically relevant experimental models as a standard rabbit ear HS model only reflects an early stage of scarring. The current study aims to adapt this animal model for simulation of mature HS by validating the time of the scar stabilization using qualitative and quantitative criteria. The full-thickness skin and perichondrium excision wounds were created on the ventral side of the rabbit ears. The tissue samples were studied on post-operation days (PODs) 30, 60, 90 and 120. The histopathological examination and morphometry were applied in parallel with biochemical analysis of protein and glycosaminoglycans (GAGs) content and amino acid composition. The supramolecular organization of collagen was explored by differential scanning calorimetry. Four stages of the rabbit ear HS maturation were delineated and attributed with the histolomorphometrical and physicochemical parameters of the tissue. The experimental scars formed in 30 days but stabilized structurally and biochemically only on POD 90–120. This evidence-based model can be used for the studies and testing of new treatments of the mature HSs.

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Section: Discussionmentioning

confidence: 93%

Modeling of Old Scars: Histopathological, Biochemical and Thermal Analysis of the Scar Tissue Maturation

Fayzullin

Ignatieva

Захаркина

et al. 2021

Biology

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“…Truncated forms of decorin have been reported previously in human post-burn hypertrophic scar (28,29), calf skin (30), postnatal rat submandibular glad (31), and bovine cornea (32). However, the exact nature of these truncated forms of decorin was not ascertained.…”

Section: Discussionmentioning

confidence: 98%

Age-related Changes in the Proteoglycans of Human Skin

Carrino

Önnerfjord

Sandy

et al. 2003

Journal of Biological Chemistry

106

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Dramatic changes occur in skin as a function of age, including changes in morphology, physiology, and mechanical properties. Changes in extracellular matrix molecules also occur, and these changes likely contribute to the overall age-related changes in the physical properties of skin. The major proteoglycans detected in extracts of human skin are decorin and versican. In addition, adult human skin contains a truncated form of decorin, whereas fetal skin contains virtually undetectable levels of this truncated decorin. Analysis of this molecule, herein referred to as decorunt, indicates that it is a catabolic fragment of decorin rather than a splice variant. With antibody probes to the core protein, decorunt is found to lack the carboxyl-terminal portion of decorin. Further analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry shows that the carboxyl terminus of decorunt is at Phe 170 of decorin. This result indicates that decorunt represents the amino-terminal 43% of the mature decorin molecule. Such a structure is inconsistent with alternative splicing of decorin and suggests that decorunt is a catabolic fragment of decorin. A neoepitope antiserum, anti-VRKVTF, was generated against the carboxyl terminus of decorunt. This antiserum does not recognize intact decorin in any skin proteoglycan sample tested on immunoblots but recognizes every sample of decorunt tested. The results with anti-VRKVTF confirm the identification of the carboxyl terminus of decorunt. Analysis of collagen binding by surface plasmon resonance indicates that the affinity of decorunt for type I collagen is 100-fold less than that of decorin. This observation correlates with the structural analysis of decorunt, in that it lacks regions of decorin previously shown to be important for interaction with type I collagen. The detection of a catabolic fragment of decorin suggests the existence of a specific catabolic pathway for this proteoglycan. Because of the capacity of decorin to influence collagen fibrillogenesis, catabolism of decorin may have important functional implications with respect to the dermal collagen network.The mechanical properties of the dermis are determined primarily by the extracellular matrix. These mechanical properties change dramatically as a function of age (1, 2), perhaps as a direct result of the known age-related changes in the molecules of the dermal extracellular matrix. Age-related differences have been shown for fibrillar collagens (3-7), which are the major extracellular matrix components of the dermis (8). In addition to collagen, the dermal extracellular matrix also contains proteoglycans, which show age-related differences (9 -16). Perhaps related to these changes in proteoglycans are age-related increases in the water content of the dermis (11) and in the content of mobile water (17).Although dermal proteoglycans are present in much lower abundance than collagen, evidence indicates that these molecules are important in the physiology of skin. For example, the small proteogl...

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“…Therefore, we analysed glycosaminoglycans, including proteodermatan sulphate, in the patient's skin. Because dermatan sulphates were present in skin as dermatan sulphate proteoglycans, which were composed of mol, mass 55 kd core proteins and mol, mass 17.5 kd dermatan sulphate chains [17, 18], the defect in dermatan sulphate chains was thought to indicate a defect in the core protein of dermatan sulphate proteoglycans or in the enzymes involved in the synthesis by dermatan sulphate of, for example, C5 epimerase and sulphotransferase. Radioimmunoassay of DS‐proteoglycan core protein could not be done as purified core protein standard is not available.…”

Section: Discussionmentioning

confidence: 99%

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

Fushimi

Kameyama

Shinkai

1989

Journal of Internal Medicine

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A variant form of Ehlers-Danlos syndrome with single adrenocorticotrophic hormone (ACTH) deficiency and mild diabetes mellitus was studied by immunohistochemical and biochemical analyses of the connective tissue. The patient exhibited features characteristic of the Ehlers-Danlos syndrome, such as fragility, hyperextensibility, and bruisability of the skin and large veins were readily seen, but no hypermobility of any joint was detectable. Biochemical studies of the connective tissue confirmed that the apparent synthesis of collagens was within normal limits, but the deposition of the major proteoglycan in the skin of this patient was markedly reduced, mainly because the synthesis of core protein of dermatan sulphate proteoglycan was defective.

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The Proteoglycans in Hypertrophic Scar

Cited by 10 publications

References 22 publications

Modeling of Old Scars: Histopathological, Biochemical and Thermal Analysis of the Scar Tissue Maturation

Modeling of Old Scars: Histopathological, Biochemical and Thermal Analysis of the Scar Tissue Maturation

Age-related Changes in the Proteoglycans of Human Skin

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

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