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Expression and binding properties of two isoforms of the human growth hormone receptor
Author(s) -
Sobrier Marie-Laure,
Duquesnoy Philippe,
Duriez Bénédicte,
Amselem Serge,
Goossens Michel
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80028-s
Subject(s) - growth hormone receptor , gene isoform , exon , receptor , microbiology and biotechnology , complementary dna , biology , messenger rna , extracellular , chemistry , gene , hormone , biochemistry , growth hormone
Two isoforms of the human growth hormone receptor mRNA, one containing exon 3 (encoding an extracellular domain of the receptor), hGHR, and one excluding exon 3, hGHRd3, have been described. To study the cellular distribution of the two types of messengers we have analysed a panel of tissues. Both isoforms were expressed independently or simultaneously depending on the tissue studied. To investigate the binding properties of hGHRd3 we have cloned its cDNA in a eukaryotic expression vector; transient expression in COS‐7 cells showed that the receptor without exon 3 was expressed on the plasma membrane and was able to bind human growth hormone (hGH) with the same high affinity as hGHR. Human lactogen (hCS) removed 125 I‐hGH bound to the full‐length and exon 3 ‐ excluding receptors to the same extent. These results show that hGHR and hGHRd3 have tissue‐specific expression and share identical binding properties for hGH and hCS and leave open the possibility that exon 3 might influence receptor signalling.