NDLI: Differential expression of two distinct forms of mRNA encoding members of a dipeptidyl aminopeptidase family.

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Differential expression of two distinct forms of mRNA encoding members of a dipeptidyl aminopeptidase family.

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Differential expression of two distinct forms of mRNA encoding members of a dipeptidyl aminopeptidase family.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hunter, C. Doi, K. Wenthold, R. J. Wada, K. Yokotani, N. Shimasaki, S.
Description	Author Affiliation: Wada K ( Laboratory of Neurochemistry, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD 20892.);
Abstract	We have identified two cDNAs encoding dipeptidyl aminopeptidase-like proteins (DPPXs) in both bovine and rat brains that have different N-terminal cytoplasmic domains but share an identical transmembrane domain and a long C-terminal extracellular domain. In both species, one of the cDNAs encodes a protein (designated DPPX-S) of 803 amino acid residues with a short cytoplasmic domain of 32 amino acids, and the other cDNA encodes a protein (designated DPPX-L) with a longer cytoplasmic domain--the bovine cDNA encodes 92 amino acids and the rat cDNA encodes 88 amino acids. The membrane topology of DPPX-S and -L is similar to that of other transmembrane peptidases, and DPPX-S share approximately 30% identity and 50% similarity with reported yeast and rat liver dipeptidyl aminopeptidase amino acid sequences, suggesting that DPPX is a member of the dipeptidyl aminopeptidase family. DPPX-S mRNA is expressed in brain and some peripheral tissues including kidney, ovary, and testis; in contrast, DPPX-L mRNA is expressed almost exclusively in brain. No transcripts for either form are found in heart, liver, or spleen. In situ hybridization studies show that the two transcripts have different distributions in the brain. DPPX-L mRNA is expressed in limited regions of brain with the highest level of expression in the medial habenula. More widespread expression is seen for DPPX-S mRNA. The differential distribution of mRNAs for the DPPX-S and -L suggests that these proteins are involved in the metabolism of certain localized peptides and that the cytoplasmic domain may play a key role in determining the physiological specificity of DPPX.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dipeptidyl-Peptidases And Tripeptidyl-Peptidases Genetics Amino Acid Sequence Animals Brain Physiology DNA Gene Expression Molecular Sequence Data Nucleic Acid Hybridization Oligodeoxyribonucleotides Chemistry Polymerase Chain Reaction RNA Splicing RNA, Messenger Restriction Mapping Sequence Alignment Tissue Distribution Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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