Serum-dependent Secretion of Nondisulfide-bonded and Unfolded Type IV Collagen α Chains by Cultured Fetal Lung Fibroblasts

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概要

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• Human fetal lung fibroblasts, TIG-1, produced the type IV collagen that was immunoblotted as the band with Mr of 500 kDa(designated as NR500)either with a monoclonal antibody, JK132, recognizing the α1(IV)chain or with an antibody, H21 recognizing α2(IV)chain. However, the conditioned medium of the cultured cells with serum occasionally showed an additional band with Mr of 180kDa(designated as NR180)immunostained with JK132. ELISA with JK132 was high to the conditioned medium containing NR180, while it was lowest to the medium containing no NR180. The results suggested that NR180 might be an unfolded, nondisulfide-bonded α1(IV)chain, since JK132 recognizes only heat-denatured α1(IV)chain, but not the type IV collagen in a triple-helical conformation. NR180 was separated from other materials in the conditioned medium including NR500 as a bound fraction on JK132-coupled affinity column. One of the V8 proteolytic fragments from the isolated NR180 was sequenced. It contained hydroxyproline residues in an alignment with the amino acid sequence in α1(IV)chain. Nondisulfide-bonded α2(IV)chain was also detected in the conditioned medium containing NR180. The α2(IV)chain was not recovered in the bound fraction on the JK132-coupled column, suggesting that nondisulfide-bonded α1(IV)chain and α2(IV)chain are not associated through non-collagenous domain 1(NC1 domain)of type IV collagen α chains. We assume that production and secretion of nondisulfide-bonded type IV collagen α chains could be due to repressed trimerization of the chains required for triple-helical formation.

• 日本結合組織学会の論文
• 1999-09-25

著者

• TAKEDA Yasushi

  Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo

• SASAKI Tasuku

  Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo

• IMAMURA Yasutada

  Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo

• HAYASHI Toshihiko

  Department of Life Sciences-Chemistry, Graduate School of Arts and Sciences, The University of Tokyo

• SADO Yoshikazu

  Division of Immunology, Shigei Medical Research Institute

• Sasaki T

  National Inst. Res. Inorganic Materials Ibaraki Jpn

• Sado Y

  Shigei Medical Research Institute

• Sado Yoshikazu

  Division Of Immunology Shigei Medical Research Institute

• Sado Yoshikazu

  Divisions Of Immunology And Ultrastructure Research Shigei Medical Research Institute

• TAKAHASHI Seiichiro

  Department of Diabetes and Endocrinology, Saitama Medical University

• YOSHIKAWA Kiwamu

  Department of Cell Biology and Histology, Akita University School of Medicine

• Takeda Y

  Komazawa Univ. Tokyo

• Takemura Yukitoshi

  Department Of Life Sciences Graduate School Of Arts And Sciences The University Of Tokyo

• Imamura Yasutada

  Department Of Applied Chemistry Kogakuin University

• Hayashi Toshihiko

  Faculty Of Pharmaceutical Sciences Teikyo Heisei University

• Takahashi Seiichiro

  Department Of Life Sciences Graduate School Of Arts And Sciences The University Of Tokyo

• Takahashi Seiichiro

  Department Of Diabetes And Endocrinology Saitama Medical University

• Takeda Yasushi

  Department Of Cardiology Tokyo Teishin Hospital

• Sado Y

  Division Of Immunology Shigei Medical Research Institute

• Hayashi T

  Faculty Of Pharmaceutical Sciences Teikyo Heisei University

• Sasaki Tasuku

  Department Of Dermatology Yokohama City University School Of Medicine

• Hayashi Toshihiko

  Department Of Biology Faculty Of Science Shizuoka University

• Yoshikawa Kiwamu

  Department Of Life Sciences Graduate School Of Arts And Sciences The University Of Tokyo

• Yoshikawa Kiwamu

  Department Of Cell Biology And Histology Akita University School Of Medicine

• Hayashi Toshihiko

  Teikyo Heisei University

• YOSHIKAWA Kiwamu

  Department of Biochemistry, Akita University School of Medicine

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