Source:http://linkedlifedata.com/resource/pubmed/id/11292829
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
26
|
| pubmed:dateCreated |
2001-6-25
|
| pubmed:databankReference | |
| pubmed:abstractText |
We cloned a cDNA encoding a novel lysyl oxidase-related protein, named LOXC, by suppression subtractive hybridization between differentiated and calcified ATDC5 cells, a clonal mouse chondrogenic EC cell line. The deduced amino acid sequence of mouse LOXC consists of 757 amino acids and shows 50% identity with that of mouse lysyl oxidase. Northern blot analysis showed a distinct hybridization band of 5.4 kilobases, and Western blot analysis showed an immunoreactive band at 82 kilodaltons. Expression of LOXC mRNA was detected in osteoblastic MC3T3-E1 cells and embryonic fibroblast C3H10T1/2 cells, whereas none of NIH3T3 fibroblasts and myoblastic C2C12 cells expressed LOXC mRNA in vitro. Moreover, the LOXC mRNA and protein levels dramatically increased throughout a process of chondrogenic differentiation in ATDC5 cells. In vivo, LOXC gene expression was localized in hypertrophic and calcified chondrocytes of growth plates in adult mice. The conditioned media of COS-7 cells transfected with the full-length LOXC cDNA showed the lysyl oxidase activity in both type I and type II collagens derived from chick embryos, and these activities of LOXC were inhibited by beta-aminopropionitrile, a specific inhibitor of lysyl oxidase. Our data indicate that LOXC is expressed in cartilage in vivo and modulates the formation of a collagenous extracellular matrix.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
276
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
24023-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:11292829-Amino Acid Oxidoreductases,
pubmed-meshheading:11292829-Amino Acid Sequence,
pubmed-meshheading:11292829-Animals,
pubmed-meshheading:11292829-Animals, Newborn,
pubmed-meshheading:11292829-Base Sequence,
pubmed-meshheading:11292829-Blotting, Western,
pubmed-meshheading:11292829-COS Cells,
pubmed-meshheading:11292829-Cartilage,
pubmed-meshheading:11292829-Cell Line,
pubmed-meshheading:11292829-Cloning, Molecular,
pubmed-meshheading:11292829-Growth Plate,
pubmed-meshheading:11292829-Mice,
pubmed-meshheading:11292829-Molecular Sequence Data,
pubmed-meshheading:11292829-Protein-Lysine 6-Oxidase,
pubmed-meshheading:11292829-RNA, Messenger,
pubmed-meshheading:11292829-Sequence Homology, Amino Acid,
pubmed-meshheading:11292829-Tissue Distribution,
pubmed-meshheading:11292829-Transcription, Genetic,
pubmed-meshheading:11292829-Transfection
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage.
|
| pubmed:affiliation |
Department of Orthopaedic Surgery, Graduate School of Medicine, Kyoto University, Sakyo, Kyoto 606-8507, Japan.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|