期刊
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
卷 53, 期 -, 页码 51-54出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2014.04.020
关键词
Collagen XII; Collagen fiber; Osteogenesis; Ehlers-Danlos syndrome; Bethlem myopathy
资金
- Swiss NSF [3100A0-107515, 31003A_146825]
- NIH [NIAMS AR044745]
- NINDS/NIH
- DFG [SFB 829, A7]
- Koln Fortune Programme of the Medical Faculty
- Swiss National Science Foundation (SNF) [31003A_146825] Funding Source: Swiss National Science Foundation (SNF)
Collagen XII, largest member of the fibril-associated collagens with interrupted triple helix (FACIT) family, assembles from three identical alpha-chains encoded by the COL12A1 gene. The molecule consists of three threadlike N-terminal noncollagenous NC3 domains, joined by disulfide bonds and a short interrupted collagen triple helix toward the C-terminus. Splice variants differ considerably in size and properties: small collagen XIIB (220 kDa subunit) is similar to collagen XIV, whereas collagen XIIA (350 kDa) has a much larger NC3 domain carrying glycosaminoglycan chains. Collagen XII binds to collagen I-containing fibrils via its collagenous domain, whereas its large noncollagenous arms interact with other matrix proteins such as tenascin-X. In dense connective tissues and bone, collagen XII is thought to regulate organization and mechanical properties of collagen fibril bundles. Accordingly, recent findings show that collagen XII mutations cause Ehlers-Danlos/myopathy overlap syndrome associated with skeletal abnormalities and muscle weakness in mice and humans. (C) 2014 Elsevier Ltd. All rights reserved.
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