A matricellular protein fibulin-4 is essential for the activation of lysyl oxidase

Author:

Noda Kazuo12ORCID,Kitagawa Kaori1ORCID,Miki Takao1,Horiguchi Masahito3ORCID,Akama Tomoya O.1,Taniguchi Takako4,Taniguchi Hisaaki4,Takahashi Kazuaki5ORCID,Ogra Yasumitsu5ORCID,Mecham Robert P.6ORCID,Terajima Masahiko7ORCID,Yamauchi Mitsuo7,Nakamura Tomoyuki1ORCID

Affiliation:

1. Department of Pharmacology, Kansai Medical University, Hirakata, Osaka 573-1010, Japan.

2. Department of Plastic and Reconstructive Surgery, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.

3. Department of Emergency Medicine, Japanese Red Cross Society Kyoto Daiichi Hospital, Kyoto 605-0981, Japan.

4. Division of Disease Proteomics, Institute for Enzyme Research, Tokushima University, Tokushima 770-8503, Japan.

5. Laboratory of Toxicology and Environmental Health, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba 260-8675, Japan.

6. Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO 63110, USA.

7. Division of Oral and Craniofacial Health Sciences, Adams School of Dentistry, University of North Carolina, Chapel Hill, NC 27599, USA.

Abstract

A secreted protein activates a major extracellular matrix cross-linking enzyme by promoting copper ion transfer in the Golgi.

Funder

NIH Office of the Director

Takeda Science Foundation

Japan Society for the Promotion of Science

Funding Program for Next Generation World-Leading Researchers in Japan

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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