Sequencing of two alternatively spliced mRNAs corresponding to the extracellular domain of the rat receptor for advanced glycosylation end products (RAGE)

Biochem Biophys Res Commun. 1998 Oct 9;251(1):230-4. doi: 10.1006/bbrc.1998.9446.

Abstract

The receptor for advanced glycosylation end products (RAGE) is an integral membrane protein responsible for the recognition and internalization of those extensively modified proteins. The receptor has an extracellular domain that binds to the advanced glycosylation end products. By reverse-transcription and polymerase chain reaction amplification, we have identified in rat liver and kidney two amplified products that correspond to cDNA coding for a part of the extracellular domain of the receptor. Sequencing of these products showed that these amplified molecules were similar except for a 27-bp fragment that was absent in the smaller product. This spliced region is located close to the transmembrane region of the receptor. We have confirmed the possibility of the alternative splicing in the generation of these mRNA isoforms by cloning a fragment of the rat gene for RAGE. This fragment has a distribution of introns and exons fully compatible with the proposed alternative splicing.

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Diabetes Mellitus, Experimental / genetics
  • Diabetes Mellitus, Experimental / metabolism
  • Glycation End Products, Advanced / metabolism*
  • Humans
  • Kidney / chemistry
  • Liver / chemistry
  • Mice
  • Molecular Sequence Data
  • RNA, Messenger / isolation & purification*
  • Rats
  • Receptor for Advanced Glycation End Products
  • Receptors, Immunologic / chemistry*
  • Receptors, Immunologic / genetics*
  • Sequence Alignment
  • Sequence Analysis, DNA

Substances

  • Glycation End Products, Advanced
  • RNA, Messenger
  • Receptor for Advanced Glycation End Products
  • Receptors, Immunologic