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

Author:

Boes Mary1,Dake Brian L.2,Booth Barbara A.2,Sandra Alexander34,Bateman Mathew3,Knudtson Kevin L.24,Bar Robert S.24

Affiliation:

1. Veterans Administration Medical Center and Departments of

2. Internal Medicine and

3. Anatomy and Cell Biology,

4. Diabetes and Endocrinology Research Center, The University of Iowa, Iowa City, Iowa 52246

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.

Publisher

American Physiological Society

Subject

Physiology (medical),Physiology,Endocrinology, Diabetes and Metabolism

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