Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-4-12
pubmed:abstractText
Insulin-like growth factor (IGF)-binding protein-3 (IGFBP-3) possesses both growth-inhibitory and -potentiating effects on cells that are independent of IGF action and are mediated through specific IGFBP-3 binding proteins/receptors located at the cell membrane, cytosol, or nuclear compartments and in the extracellular matrix. We have here characterized transferrin (Tf) as one of these IGFBP-3 binding proteins. Human serum was fractionated over an IGFBP-3 affinity column, and a 70-kDa protein was eluted, sequenced, and identified (through database searching and Western immunoblot) as human Tf. Tf bound IGFBP-3 but had negligible affinity to the other five IGFBPs, and iron-saturated holo-Tf bound IGFBP-3 more avidly than unsaturated Tf. Biosensor interaction analysis confirmed that this interaction is specific and sensitive, with a high association rate similar to IGF-I, and suggested that binding occurs in the vicinity of the IGFBP-3 nuclear localization site. As an independent confirmation of this interaction, using a yeast two-hybrid system, we cloned Tf from a human liver complementary DNA library as an IGFBP-3 protein partner. Tf treatment blocked IGFBP-3-induced cell proliferation in bladder smooth muscle cells, and IGFBP-3-induced apoptosis in prostate cancer cells. In summary, we have employed a combination of techniques to demonstrate that Tf specifically binds IGFBP-3, and we showed that this interaction has important physiological effects on cellular events.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1806-13
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11297622-Adult, pubmed-meshheading:11297622-Animals, pubmed-meshheading:11297622-Apoptosis, pubmed-meshheading:11297622-Carrier Proteins, pubmed-meshheading:11297622-Cell Division, pubmed-meshheading:11297622-Cells, Cultured, pubmed-meshheading:11297622-Dose-Response Relationship, Drug, pubmed-meshheading:11297622-Fluorescent Antibody Technique, pubmed-meshheading:11297622-Humans, pubmed-meshheading:11297622-Insulin-Like Growth Factor Binding Protein 3, pubmed-meshheading:11297622-Insulin-Like Growth Factor Binding Proteins, pubmed-meshheading:11297622-Iron, pubmed-meshheading:11297622-Kinetics, pubmed-meshheading:11297622-Male, pubmed-meshheading:11297622-Microscopy, Confocal, pubmed-meshheading:11297622-Muscle, Smooth, pubmed-meshheading:11297622-Prostatic Neoplasms, pubmed-meshheading:11297622-Sheep, pubmed-meshheading:11297622-Tissue Distribution, pubmed-meshheading:11297622-Transferrin, pubmed-meshheading:11297622-Urinary Bladder, pubmed-meshheading:11297622-Yeasts
pubmed:year
2001
pubmed:articleTitle
Transferrin is an insulin-like growth factor-binding protein-3 binding protein.
pubmed:affiliation
Children's Hospital of Philadelphia, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't