Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies

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Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies. / Agarwal, Pallavi; Schulz, Jan-Niklas; Blumbach, Katrin; Andréasson, Kristofer; Heinegård, Dick; Paulsson, Mats; Mauch, Cornelia; Eming, Sabine A.; Eckes, Beate; Krieg, Thomas.

In: Matrix Biology, Vol. 32, No. 6, 2013, p. 325-331.

Research output: Contribution to journalArticle

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Agarwal, P, Schulz, J-N, Blumbach, K, Andréasson, K, Heinegård, D, Paulsson, M, Mauch, C, Eming, SA, Eckes, B & Krieg, T 2013, 'Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies', Matrix Biology, vol. 32, no. 6, pp. 325-331. https://doi.org/10.1016/j.matbio.2013.02.010

APA

CBE

Agarwal P, Schulz J-N, Blumbach K, Andréasson K, Heinegård D, Paulsson M, Mauch C, Eming SA, Eckes B, Krieg T. 2013. Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies. Matrix Biology. 32(6):325-331. https://doi.org/10.1016/j.matbio.2013.02.010

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Agarwal, Pallavi ; Schulz, Jan-Niklas ; Blumbach, Katrin ; Andréasson, Kristofer ; Heinegård, Dick ; Paulsson, Mats ; Mauch, Cornelia ; Eming, Sabine A. ; Eckes, Beate ; Krieg, Thomas. / Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies. In: Matrix Biology. 2013 ; Vol. 32, No. 6. pp. 325-331.

RIS

TY - JOUR

T1 - Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies

AU - Agarwal, Pallavi

AU - Schulz, Jan-Niklas

AU - Blumbach, Katrin

AU - Andréasson, Kristofer

AU - Heinegård, Dick

AU - Paulsson, Mats

AU - Mauch, Cornelia

AU - Eming, Sabine A.

AU - Eckes, Beate

AU - Krieg, Thomas

PY - 2013

Y1 - 2013

N2 - Skin fibrosis is characterized by activated fibroblasts and an altered architecture of the extracellular matrix. Excessive deposition of extracellular matrix proteins and altered cytokine levels in the dermal collagen matrix are common to several pathological situations such as localized scleroderma and systemic sclerosis, keloids, dermatosclerosis associated with venous ulcers and the fibroproliferative tissue surrounding invasively growing tumors. Which factors contribute to altered organization of dermal collagen matrix in skin fibrosis is not well understood. We recently demonstrated that cartilage oligomeric matrix protein (COMP) functions as organizer of the dermal collagen I network in healthy human skin (Agarwal et al., 2012). Here we show that COMP deposition is enhanced in the dermis in various fibrotic conditions. COMP levels were significantly increased in fibrotic lesions derived from patients with localized scleroderma, in wound tissue and exudates of patients with venous leg ulcers and in the fibrotic stroma of biopsies from patients with basal cell carcinoma. We postulate enhanced deposition of COMP as one of the common factors altering the supramolecular architecture of collagen matrix in fibrotic skin pathologies. Interestingly, COMP remained nearly undetectable in normally healing wounds where myofibroblasts transiently accumulate in the granulation tissue. We conclude that COMP expression is restricted to a fibroblast differentiation state not identical to myofibroblasts which is induced by TGF beta and biomechanical forces. (C) 2013 Elsevier B.V. All rights reserved.

AB - Skin fibrosis is characterized by activated fibroblasts and an altered architecture of the extracellular matrix. Excessive deposition of extracellular matrix proteins and altered cytokine levels in the dermal collagen matrix are common to several pathological situations such as localized scleroderma and systemic sclerosis, keloids, dermatosclerosis associated with venous ulcers and the fibroproliferative tissue surrounding invasively growing tumors. Which factors contribute to altered organization of dermal collagen matrix in skin fibrosis is not well understood. We recently demonstrated that cartilage oligomeric matrix protein (COMP) functions as organizer of the dermal collagen I network in healthy human skin (Agarwal et al., 2012). Here we show that COMP deposition is enhanced in the dermis in various fibrotic conditions. COMP levels were significantly increased in fibrotic lesions derived from patients with localized scleroderma, in wound tissue and exudates of patients with venous leg ulcers and in the fibrotic stroma of biopsies from patients with basal cell carcinoma. We postulate enhanced deposition of COMP as one of the common factors altering the supramolecular architecture of collagen matrix in fibrotic skin pathologies. Interestingly, COMP remained nearly undetectable in normally healing wounds where myofibroblasts transiently accumulate in the granulation tissue. We conclude that COMP expression is restricted to a fibroblast differentiation state not identical to myofibroblasts which is induced by TGF beta and biomechanical forces. (C) 2013 Elsevier B.V. All rights reserved.

KW - COMP

KW - ECM organization

KW - Collagen fibrils

KW - Basal cell carcinoma

KW - Chronic

KW - wounds

KW - Fibroplastic stroma response

U2 - 10.1016/j.matbio.2013.02.010

DO - 10.1016/j.matbio.2013.02.010

M3 - Article

VL - 32

SP - 325

EP - 331

JO - Matrix (Stuttgart, Germany)

T2 - Matrix (Stuttgart, Germany)

JF - Matrix (Stuttgart, Germany)

SN - 1569-1802

IS - 6

ER -