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WFRF:(Mauch Cornelia)
 

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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003952naa a2200469 4500
001oai:lup.lub.lu.se:e273675e-01e0-418e-9572-d08e231fc379
003SwePub
008160401s2013 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/41032342 URI
024a https://doi.org/10.1016/j.matbio.2013.02.0102 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Agarwal, Pallavi4 aut
2451 0a Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies
264 1b Elsevier BV,c 2013
520 a 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.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Reumatologi och inflammation0 (SwePub)302102 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Rheumatology and Autoimmunity0 (SwePub)302102 hsv//eng
653 a COMP
653 a ECM organization
653 a Collagen fibrils
653 a Basal cell carcinoma
653 a Chronic
653 a wounds
653 a Fibroplastic stroma response
700a Schulz, Jan-Niklas4 aut
700a Blumbach, Katrin4 aut
700a Andréasson, Kristoferu Lund University,Lunds universitet,Reumatologi och molekylär skelettbiologi,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Rheumatology,Section III,Department of Clinical Sciences, Lund,Faculty of Medicine4 aut0 (Swepub:lu)med-kra
700a Heinegård, Dicku Lund University,Lunds universitet,Reumatologi och molekylär skelettbiologi,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Rheumatology,Section III,Department of Clinical Sciences, Lund,Faculty of Medicine4 aut0 (Swepub:lu)medk-dhe
700a Paulsson, Mats4 aut
700a Mauch, Cornelia4 aut
700a Eming, Sabine A.4 aut
700a Eckes, Beate4 aut
700a Krieg, Thomas4 aut
710a Reumatologi och molekylär skelettbiologib Sektion III4 org
773t Matrix Biologyd : Elsevier BVg 32:6, s. 325-331q 32:6<325-331x 1569-1802x 0945-053X
856u http://dx.doi.org/10.1016/j.matbio.2013.02.010y FULLTEXT
8564 8u https://lup.lub.lu.se/record/4103234
8564 8u https://doi.org/10.1016/j.matbio.2013.02.010

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