Logo image
IGF-I and IGFBP-3 transport in the rat heart
Journal article   Peer reviewed

IGF-I and IGFBP-3 transport in the rat heart

Mary Boes, Brian L. Dake, Barbara A. Booth, Alexander Sandra, Mathew Bateman, Kevin L. Knudtson and Robert S. Bar
American journal of physiology: endocrinology and metabolism, Vol.284(1), pp.E237-E239
01/01/2003
DOI: 10.1152/ajpendo.00336.2002
PMID: 12485812

View Online

Abstract

Specific binding of IGF-binding protein (IGFBP)-3 was shown to be present in the isolated, beating rat heart. The uptake of perfused 125I-labeled IGF-I in the beating heart was decreased to 9% by blocking IGF-I binding sites with the IGF-I analog Long R3 (LR3) IGF-I. When LR3 was perfused with complexes of125I-IGF-I · IGFBP-3, uptake of125I-IGF-I was decreased to 41%, which was significantly greater than LR3 and 125I-IGF-I (41 vs. 9%). These data suggest that both microvessel IGF-I and IGFBP-3 binding sites contribute to the transport of IGF-I in the perfused rat heart. This also suggests a novel and plausible mechanism whereby circulating IGFs reach sites of IGF bioactivity.

Details

Metrics

Logo image