Molecular cloning of rat leptin receptor isoform complementary DNAs—identification of a missense mutation in Zucker fatty (fa/fa) rats

K Takaya, Y Ogawa, N Isse, T Okazaki, N Satoh… - Biochemical and …, 1996 - Elsevier
K Takaya, Y Ogawa, N Isse, T Okazaki, N Satoh, H Masuzaki, K Mori, N Tamura, K Hosoda…
Biochemical and biophysical research communications, 1996Elsevier
We cloned the full-length rat leptin receptor (Ob-R) isoform complementary DNAs (cDNAs)
and examined the gene expression in rats. We also identified a mutation in Ob-R in Zucker
fatty (fa/fa) rats. Three alternatively spliced isoforms (Ob-Ra, Ob-Rb, and Ob-Re) have been
identified, which are closely related to the gp130 signal-transduction component of class I
cytokine receptors. Rat Ob-Ra and Ob-Rb were single transmembrane proteins, which differ
in the C-terminal amino acid sequences. On the other hand, Ob-Re had no transmembrane …
We cloned the full-length rat leptin receptor (Ob-R) isoform complementary DNAs (cDNAs) and examined the gene expression in rats. We also identified a mutation in Ob-R in Zucker fatty (fa/fa) rats. Three alternatively spliced isoforms (Ob-Ra, Ob-Rb, and Ob-Re) have been identified, which are closely related to the gp130 signal-transduction component of class I cytokine receptors. Rat Ob-Ra and Ob-Rb were single transmembrane proteins, which differ in the C-terminal amino acid sequences. On the other hand, Ob-Re had no transmembrane domain and was a soluble form of the receptor. Reverse transcription-polymerase chain reaction analysis revealed that Ob-R isoform messenger RNAs (mRNAs) are expressed in a wide variety of rat tissues in tissue-specific manners. A missense mutation (an A to C conversion at nucleotide position 806) was found in the extracellular domain of all the isoforms in Zucker fatty (fa/fa) rats, which resulted in an amino acid change from Gln to Pro at + 269 (the Gln269Pro mutation). These Ob-R isoform mRNAs were present in the brain from Zucker fatty (fa/fa) rats at comparable amounts to those in their lean littermates. The present study provides new insight into the molecular mechanisms for Ob-R.
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