PMID- 10206990
OWN - NLM
STAT- MEDLINE
DCOM- 19990520
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 17
DP  - 1999 Apr 23
TI  - Purification, cDNA cloning, and expression of a new human blood plasma glutamate 
      carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate
      carboxypeptidase/prostate-specific membrane antigen.
PG  - 11742-50
AB  - We describe the identification, cDNA cloning, and biochemical characterization of
      a new human blood plasma glutamate carboxypeptidase (PGCP). PGCP was co-purified 
      from human placenta with lysosomal carboxypeptidase, cathepsin A, lysosomal
      endopeptidase, cathepsin D, and a gamma-interferon-inducible protein, IP-30,
      using an affinity chromatography on a Phe-Leu-agarose column. A PGCP cDNA was
      obtained as an expressed sequence tag clone and completed at 5'-end by rapid
      amplification of cDNA ends polymerase chain reaction. The cDNA contained a
      1623-base pair open reading frame predicting a 541-amino acid protein, with five 
      putative Asn glycosylation sites and a 21-residue signal peptide. PGCP showed
      significant amino acid sequence homology to several cocatalytic metallopeptidases
      including a glutamate carboxypeptidase II also known as
      N-acetyl-aspartyl-alpha-glutamate carboxypeptidase or as prostate-specific
      membrane antigen and expressed glutamate carboxypeptidase activity. Expression of
      the PGCP cDNA in COS-1 cells, followed by Western blotting and metabolic labeling
      showed that PGCP is synthesized as a 62-kDa precursor, which is processed to a
      56-kDa mature form containing two Asn-linked oligosaccharide chains. The mature
      form of PGCP was secreted into the culture medium, which is consistent with its
      intracellular localization in secretion granules. In humans, PGCP is found
      principally in blood plasma, suggesting a potential role in the metabolism of
      secreted peptides.
FAU - Gingras, R
AU  - Gingras R
AD  - Universite de Montreal, Service de Genetique Medicale, Departement de Pediatrie, 
      Hopital Sainte-Justine, Montreal, Quebec H3T 1C5, Canada.
FAU - Richard, C
AU  - Richard C
FAU - El-Alfy, M
AU  - El-Alfy M
FAU - Morales, C R
AU  - Morales CR
FAU - Potier, M
AU  - Potier M
FAU - Pshezhetsky, A V
AU  - Pshezhetsky AV
LA  - eng
SI  - GENBANK/AF119386
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, Surface)
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - EC 3.4.- (Carboxypeptidases)
RN  - EC 3.4.17.11 (glutamate carboxypeptidase)
RN  - EC 3.4.17.21 (FOLH1 protein, human)
RN  - EC 3.4.17.21 (Glutamate Carboxypeptidase II)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Antigens, Surface
MH  - Base Sequence
MH  - COS Cells
MH  - Carboxypeptidases/*genetics/*isolation & purification/metabolism
MH  - Cells, Cultured
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 8
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Fluorescent Antibody Technique
MH  - Glutamate Carboxypeptidase II
MH  - Humans
MH  - Microscopy, Immunoelectron
MH  - Molecular Sequence Data
MH  - RNA, Messenger/genetics
MH  - Sequence Homology, Amino Acid
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1074/jbc.274.17.11742 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 23;274(17):11742-50. doi: 10.1074/jbc.274.17.11742.