GSBS Student Publications

Title

Chicken and Xenopus mannose 6-phosphate receptors fail to bind insulin-like growth factor II

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Biochemistry; Program in Molecular Medicine

Date

10-5-1989

Document Type

Article

Medical Subject Headings

Animals; Chickens; Chromatography, Affinity; Female; Hexosephosphates; Humans; Insulin-Like Growth Factor II; Kinetics; Mannosephosphates; Microsomes; Microsomes, Liver; Molecular Weight; Placenta; Pregnancy; Protein Binding; Rats; Receptor, IGF Type 2; Receptors, Cell Surface; Somatomedins; Xenopus laevis

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The recent demonstration that a single mammalian receptor protein binds both mannose 6-phosphate (Man-6-P) and insulin-like growth factor II (IGF-II) with high affinity has suggested a multifunctional physiological role for this receptor, possibly including signal transduction. In order to better understand the functions of this receptor, we have investigated the properties of Man-6-P receptors from non-mammalian species. Receptors were affinity-purified from Triton X-100 extracts of total membranes from Xenopus and chicken liver as well as rat placenta using pentamannosyl 6-phosphate-Sepharose. The Man-6-P receptor was adsorbed to the pentamannosyl 6-phosphate-Sepharose and specifically eluted by Man-6-P in all three species, as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by silver staining. When the purified receptors from these three species were cross-linked to 125I-IGF-II with disuccinimidyl suberate, only receptors isolated from rat membranes were affinity-labeled. To further evaluate the properties of these Man-6-P receptors, binding of 125I-rat-IGF-II and 125I-chicken Tyr-Gly-Thr-Ala-IGF-II to purified receptors from Xenopus, chicken, and rat was evaluated by polyethylene glycol precipitation. Only the rat Man-6-P receptor exhibited detectable binding of 125I-IGF-II. These data suggest that the emergence of a high affinity IGF-II binding site on the Man-6-P receptor occurred in evolution after the divergence of mammals from other vertebrates. Thus, the biological actions of IGF-II in chickens and frogs appear to be initiated by the type I IGF receptor.

Rights and Permissions

Citation: J Biol Chem. 1989 Oct 5;264(28):16390-2.

Related Resources

Link to article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

2550441