Abstract
Cartilage oligomeric matrix protein (COMP), the fifth member of the thrombospondin gene family, is an extracellular matrix calcium-binding protein. The importance of COMP is underscored by the finding that mutations in COMP cause the human dwarfing condition, pseudoachondroplasia (PSACH). Here, we report the results of human tissue distribution and cell secretion studies of human COMP. COMP is expressed and secreted by cultured monolayer chondrocyte, tendon and ligament cells, and COMP secretion is not restricted to a differentiated chondrocyte phenotype. Whereas COMP is retained in the endoplasmic reticulum that accumulates within PSACH chondrocytes in vivo, COMP is not retained intracellularly in the dedifferentiated PSACH chondrocytes in cultures. These results lend further support to the hypothesis that retention of COMP is related to the terminal PSACH chondrocyte phenotype, processing of proteins related to extracellular matrix formation, and maintenance in cartilage.
| Original language | English |
|---|---|
| Pages (from-to) | 269-278 |
| Number of pages | 10 |
| Journal | Matrix Biology |
| Volume | 17 |
| Issue number | 4 |
| DOIs | |
| State | Published - Aug 1998 |
Funding
We would like to thank Mark Duquette and Xiao-Hua Yuan for excellent technical assistance and Carol Foss for preparing the manuscript. We also thank Paul Bornstein for sharing the phenotype of thrombospondin-2-deficient mice before publication. This work was supported by NIH Grant HL 49081 from the National Heart, Lung and Blood Institute to J.L. and by Shriners Hospital grant 15955 to J.T.H.
| Funder number |
|---|
| 15955 |
| R01HL049081 |
Keywords
- Cartilage
- Cartilage oligomeric matrix protein (COMP)
- Ligament
- Pseudoachondroplasia (PSACH)
- Tendon
- Thrombospondin-4 (TSP-4)