Source:http://linkedlifedata.com/resource/pubmed/id/17627542
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
|
pubmed:dateCreated |
2007-7-13
|
pubmed:abstractText |
The negative regulation of angiogenesis may provide a promising therapeutic target for a number of lifestyle-related diseases, as the switch to an angiogenic phenotype in many tissues represents a critical step during the progression of such disorders. Cartilage is avascular and shows resistance to vascular invasion from the surrounding well-vascularized mesenchyme. Using guanidine extracts of fetal bovine cartilage, we have identified and purified chondromodulin-I (ChM-I) as an angiogenesis inhibitor. The cDNA sequence of this factor has revealed that the ChM-I precursor protein is a type II transmembrane glycoprotein (334 amino acids) and that mature ChM-I is encoded in the C-terminal region of the precursor. After cleavage of the ChM-I precursor at its processing site, mature ChM-I (120 amino acids) is secreted from chondrocytes into the extracellular matrix. Following on from the identification of ChM-I as an angiogenesis inhibitor in cartilage, we have also cloned both mouse and human tenomodulin (TeM), which share significant homology with ChM-I at their C-termini. Moreover, exogenous expression experiments in COS cells suggests that TeM is a type II transmembrane glycoprotein (317 amino acids). When overexpressed in HUVECs, the C-terminal domain (116 amino acids) of the TeM protein shows both anti-angiogenic and anti-tumorigenic activities at equivalent levels to mature ChM-I. In our present review, we discuss the structure, biological activities and localization of these anti-angiogenic molecules.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Angiogenesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/LECT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lect1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TNMD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tnmd protein, mouse
|
pubmed:status |
MEDLINE
|
pubmed:issn |
1873-4286
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
13
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2101-12
|
pubmed:meshHeading |
pubmed-meshheading:17627542-Amino Acid Sequence,
pubmed-meshheading:17627542-Angiogenesis Inhibitors,
pubmed-meshheading:17627542-Animals,
pubmed-meshheading:17627542-Connective Tissue,
pubmed-meshheading:17627542-Gene Expression Regulation,
pubmed-meshheading:17627542-Humans,
pubmed-meshheading:17627542-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:17627542-Membrane Proteins,
pubmed-meshheading:17627542-Mesoderm,
pubmed-meshheading:17627542-Molecular Sequence Data,
pubmed-meshheading:17627542-Molecular Structure
|
pubmed:year |
2007
|
pubmed:articleTitle |
Chondromodulin-I and tenomodulin: the negative control of angiogenesis in connective tissue.
|
pubmed:affiliation |
Department of Cellular Differentiation, Institute for Frontier Medical Sciences, Kyoto University, Shogoin-Kawahara-cho, Kyoto, Japan.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|