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Regulation of insulin-like growth factor (IGF)-I action by matrix metalloproteinase-3 involves selective disruption of IGF-I/IGF-binding protein-3 complexes.

Abstract:

IGF-I and IGF-II play important roles in growth and development via interactions with cell-surface receptors; however, in nature, IGFs are sequestered by at least six soluble, high-affinity IGF-binding proteins (IGFBPs), namely IGFBPs 1-6. Herein, we demonstrate that the stromal cell-derived extracellular matrix-degrading metalloproteinase stromelysin 1 (matrix metalloproteinase 3) disrupts IGF/IGFBP-3 complexes and liberates free, intact IGFs, leading to phosphorylation of cell surface type ...

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Publication status:
Published

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Publisher copy:
10.1210/en.2003-0636

Authors


Fowlkes, JL More by this author
Thrailkill, KM More by this author
Enghild, JJ More by this author
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Journal:
Endocrinology
Volume:
145
Issue:
2
Pages:
620-626
Publication date:
2004-02-05
DOI:
EISSN:
1945-7170
ISSN:
0013-7227
URN:
uuid:4a8c7e5d-2f6c-4b3a-883e-224494816cb4
Source identifiers:
227324
Local pid:
pubs:227324

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