PMID- 10085079
OWN - NLM
STAT- MEDLINE
DCOM- 19990429
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 13
DP  - 1999 Mar 26
TI  - Isolation and expression of novel human glutamate carboxypeptidases with
      N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV
      activity.
PG  - 8470-83
AB  - Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by
      N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may
      be important in a number of neurodegenerative disorders in which excitotoxic
      mechanisms are implicated. The gene coding for human prostate-specific membrane
      antigen, a marker of prostatic carcinomas, and its rat homologue glutamate
      carboxypeptidase II have recently been shown to possess such NAALADase activity. 
      In contrast, a closely related member of this gene family, rat ileal 100-kDa
      protein, possesses a dipeptidyl peptidase IV activity. Here, we describe the
      cloning of human ileal 100-kDa protein, which we have called a NAALADase- "like" 
      (NAALADase L) peptidase based on its sequence similarity to other members of this
      gene family, and its inability to hydrolyze NAAG in transient transfection
      experiments. Furthermore, we describe the cloning of a third novel member of this
      gene family, NAALADase II, which codes for a type II integral membrane protein
      and which we have localized to chromosome 11 by fluorescent in situ hybridization
      analysis. Transient transfection of NAALADase II cDNA confers both NAALADase and 
      dipeptidyl peptidase IV activity to COS cells. Expression studies using reverse
      transcription-polymerase chain reaction and Northern blot hybridization show that
      NAALADase II is highly expressed in ovary and testis as well as within discrete
      brain areas.
FAU - Pangalos, M N
AU  - Pangalos MN
AD  - Janssen Research Foundation, B2340 Beerse, Belgium. menelas_n_pangalos@sbphrd.com
FAU - Neefs, J M
AU  - Neefs JM
FAU - Somers, M
AU  - Somers M
FAU - Verhasselt, P
AU  - Verhasselt P
FAU - Bekkers, M
AU  - Bekkers M
FAU - van der Helm, L
AU  - van der Helm L
FAU - Fraiponts, E
AU  - Fraiponts E
FAU - Ashton, D
AU  - Ashton D
FAU - Gordon, R D
AU  - Gordon RD
LA  - eng
SI  - GENBANK/AJ012370
SI  - GENBANK/AJ012371
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, Surface)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (RNA, Messenger)
RN  - EC 3.4.- (Carboxypeptidases)
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.14.5 (Dipeptidyl Peptidase 4)
RN  - EC 3.4.17.21 (FOLH1 protein, human)
RN  - EC 3.4.17.21 (Glutamate Carboxypeptidase II)
SB  - IM
MH  - Alternative Splicing/genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Antigens, Surface
MH  - Base Sequence
MH  - COS Cells
MH  - Carboxypeptidases/chemistry/*genetics
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 11/genetics
MH  - Cloning, Molecular
MH  - Dipeptidyl Peptidase 4/chemistry/*genetics
MH  - Glutamate Carboxypeptidase II
MH  - Humans
MH  - In Situ Hybridization, Fluorescence
MH  - Molecular Sequence Data
MH  - Neoplasm Proteins/chemistry/genetics
MH  - Peptide Hydrolases/chemistry/*genetics
MH  - RNA, Messenger/metabolism
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1999/03/20 00:00
MHDA- 1999/03/20 00:01
CRDT- 1999/03/20 00:00
PHST- 1999/03/20 00:00 [pubmed]
PHST- 1999/03/20 00:01 [medline]
PHST- 1999/03/20 00:00 [entrez]
AID - 10.1074/jbc.274.13.8470 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 26;274(13):8470-83. doi: 10.1074/jbc.274.13.8470.