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. 1990 Mar;1(4):327–335. doi: 10.1091/mbc.1.4.327

Identification and cellular distribution of distinct proteins forming human GM-CSF receptor.

S Chiba 1, K Shibuya 1, Y F Piao 1, A Tojo 1, N Sasaki 1, S Matsuki 1, K Miyagawa 1, K Miyazono 1, F Takaku 1
PMCID: PMC361485  PMID: 2151610

Abstract

Two proteins forming the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF)1 were identified and characterized. One with apparent Mr of about 80,000 was defined as alpha-chain and has Kd of 0.7-2.8 nM. The other binding molecule with apparent Mr of about 135,000 was defined as beta-chain and is related to the high-affinity binding with Kd of 10-40 pM. The binding kinetic studies confirmed that the 125I-GM-CSF associated slower to and dissociated more rapidly from the alpha-chain than the beta-chain. The alpha-chain is expressed not only on hemopoietic cells but also on full-term placental tissues, choriocarcinoma cells, and other solid tumor cells. In contrast, the distribution of the beta-chain is restricted on hemopoietic cells. The alpha-chain probably corresponds to the low-affinity GM-CSF receptor whose cDNA has been cloned and sequenced.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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