Journal article
Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3
American journal of physiology: endocrinology and metabolism, v 275(2), pp E321-E331
01 Aug 1998
PMID: 29585196
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Limited proteolysis lowers affinity of insulin-like growth factor (IGF)-binding protein (IGFBP)-3 for bound IGFs, resulting in greater IGF bioavailability. Plasmin is one of many proteases that cleave IGFBP-3, and the plasmin system may regulate IGFBP-3 proteolysis and IGF bioavailability in cultured cells in vitro. A role for the plasmin system in IGFBP-3 proteolysis in vivo is suggested by data presented here showing that IGFBP-3 binds plasminogen (Pg; Glu-Pg) with a dissociation constant ( K d ) ranging from 1.43 to 3.12 nM. IGF-I and Glu-Pg do not compete for IGFBP-3 binding; instead, the binary IGFBP-3/Glu-Pg complex binds IGF-I with high affinity ( K d = 0.47 nM) to form a ternary complex. Competitive binding studies suggest that the kringle 1, 4, and 5 domains of Glu-Pg and the heparin-binding domain of IGFBP-3 participate in forming the IGFBP-3/Glu-Pg complex, and other studies show that Glu-Pg in this complex is activated at a normal rate by tissue Pg activator. Importantly, IGFBP-3/Glu-Pg complexes were detected in both human citrate plasma and serum, indicating that these complexes exist in vivo. Binding of IGFBP-3 to Glu-Pg in vivo suggests how Glu-Pg activation can specifically lead to IGFBP-3 proteolysis with subsequent release of IGFs to local target tissues.
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Details
- Title
- Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3
- Creators
- Phil G. Campbell - Drexel University, Allegheny University of the Health Sciences (1996-1998)Susan K. Durham - Baylor College of MedicineAdisak Suwanichkul - Baylor College of MedicineJames D. Hayes - Drexel University, Allegheny University of the Health Sciences (1996-1998)David R. Powell - Baylor College of Medicine
- Publication Details
- American journal of physiology: endocrinology and metabolism, v 275(2), pp E321-E331
- Publisher
- American Physiological Society (APS)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Allegheny University of the Health Sciences (1996-1998)
- Web of Science ID
- WOS:000075180700019
- Scopus ID
- 2-s2.0-0031820995
- Other Identifier
- 991022199998504721
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InCites Highlights
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- Web of Science research areas
- Endocrinology & Metabolism
- Physiology