Extracellular Matrix 22-KDa protein Interacts with Decorin Core Protein and Is Expressed in Cutaneous Fibrosis^1
-
- OKAMOTO Osamu
- Department of Dermatology, Oita Medical University
-
- SUZUKI Yutaka
- Department of Dermatology Chiba University School of Medicine
-
- KIMURA Sadao
- Center for Biomedical Science Chiba University School of Medicine
-
- SHINKAI Hiroshi
- Department of Dermatology Chiba University School of Medicine
この論文をさがす
抄録
A protein with an Mr of 22, 000 was purified from bovine dermis. The amino acid sequence of the protein was identical to 22-kDa protein [Neame, P. J. et al. (1989) J. Biol. Chem. 264, 5474-5479] and showed highly homologous sequences to TRAMP (tyrosine rich acidic matrix protein) [Cronshaw, A. D. et al. (1993) Matrix 13, 255-266] and dermatopontin [Superti-Furga, A. et al. (1993) Cenomics 17, 463-467]. The protein was proved to associate with decorin and a modified decorin with carboxymethylated cysteinyl residues, but not to assemble to hyaluronate or dermatan sulfate chains. The pyridylethylation of cysteinyl residues in the 22-kDa protein did not affect its binding activity to decorin or modified decorin. Immunohistochemical analyses revealed positive stains in endothelial cells and the periphery of collagen fibers in normal dermis but not in the fibroblasts in tissue. Collagen fibers in sclerotic regions of progressive systemic sclerosis were stained diffusely, suggesting that the 22-kDa protein increases in parallel to the accumulation of collagen in the disease. Western blotting analyses of extracts of cultured endothelial cells revealed a lower Mr protein than that from cultured fibroblasts, suggesting the presence of a molecule related to the 22-kDa protein.
収録刊行物
-
- The journal of biochemistry
-
The journal of biochemistry 119 (1), 106-114, 1996-01-01
社団法人 日本生化学会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1573105974191901440
-
- NII論文ID
- 10005185171
-
- NII書誌ID
- AA00694073
-
- ISSN
- 0021924X
-
- 本文言語コード
- en
-
- データソース種別
-
- CiNii Articles