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Updated: Jun 25, 2026
07:03
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
The collagen receptor uPARAP/Endo180
Lars H Engelholm1, Signe Ingvarsen, Henrik J Jürgensen
1The Finsen Laboratory, Rigshospitalet section 3735, Copenhagen Biocenter, Ole Maaloes Vej 5, DK-2200 Copenhagen N, Denmark. lars@engelholm.dk
Frontiers in Bioscience (Landmark Edition)
|March 11, 2009
Summary
The uPAR-associated protein (uPARAP/Endo180) is an endocytic receptor crucial for collagen turnover. Its role in collagen breakdown impacts bone development and invasive tumor growth.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- The uPAR-associated protein (uPARAP/Endo180) is a type-1 membrane protein in the mannose receptor family.
- It functions as an endocytic receptor for collagen, participating in collagen turnover.
Purpose of the Study:
- To elucidate the role of uPARAP/Endo180 in collagen turnover.
- To investigate its involvement in physiological processes and disease states.
Main Methods:
- The study likely involved biochemical assays to characterize collagen binding and internalization by uPARAP/Endo180.
- Cellular and potentially in vivo models were used to study its expression and function in different contexts.
Main Results:
- uPARAP/Endo180 internalizes both intact and degraded collagens.
- Its function involves interplay with matrix-degrading proteases and potentially redundant collagenolysis pathways.
- Expression is observed in mesenchymal cells, particularly during bone development and in breast tumors.
Conclusions:
- uPARAP/Endo180 plays a significant role in collagen turnover through endocytosis.
- Its collagenolytic function is a rate-limiting step in bone growth.
- The receptor's endocytic function contributes to invasive tumor growth.
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