In:
American Journal of Physiology-Endocrinology and Metabolism, American Physiological Society, Vol. 284, No. 1 ( 2003-01-01), p. E237-E239
Abstract:
Specific binding of IGF-binding protein (IGFBP)-3 was shown to be present in the isolated, beating rat heart. The uptake of perfused 125 I-labeled IGF-I in the beating heart was decreased to 9% by blocking IGF-I binding sites with the IGF-I analog Long R 3 (LR 3 ) IGF-I. When LR 3 was perfused with complexes of 125 I-IGF-I · IGFBP-3, uptake of 125 I-IGF-I was decreased to 41%, which was significantly greater than LR 3 and 125 I-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.
Type of Medium:
Online Resource
ISSN:
0193-1849
,
1522-1555
DOI:
10.1152/ajpendo.00336.2002
Language:
English
Publisher:
American Physiological Society
Publication Date:
2003
detail.hit.zdb_id:
1477331-4
SSG:
12