Prostate-specific membrane antigen: evidence for the existence of a second related human gene

Leek, J.P.; Lench, Nicholas; Maraj, BH; Bailey, Andrew M.; Carr, IM; Andersen, S; Cross, Justin R.; Whelan, Patrick; MacLennan, KA; Meredith, D; Markham, AF

doi:10.1038/bjc.1995.377

Cited by 78 publications

(57 citation statements)

References 16 publications

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“…12). Preliminary data indicate that I100 is localized to chromosome 11 2 and may potentially explain the second weaker fluorescent in situ hybridization band that has been previously reported for the PSM gene (34,35).…”

Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of a Novel Peptidase from Rat and Human Ileum

Shneider

Thevananther

Moyer

et al. 1997

Journal of Biological Chemistry

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A novel 100-kDa ileal brush border membrane protein (I100) has been purified by anionic glycocholate affinity chromatography. Polyclonal antibodies raised against this protein were utilized to clone and characterize I100 in rats. A partial length human I100 cDNA was identified by hybridization screening. In the rat, the I100 protein is a 746-amino acid glycosylated (calculated core molecular mass of 80 kDa) type II integral membrane protein found on the apical surface of ileal villus enterocytes. Its 2.6-kilobase mRNA is expressed in distal small intestine in rats and in humans. The I100 cDNA is homologous to but distinct from human prostate-specific membrane antigen and rat brain N-acetylaspartylglutamate peptidase. It is expressed on both the basolateral and apical surfaces of stably transfected Madin Darby canine kidney cells. Analysis of these stably transfected Madin Darby canine kidney cells and I100 immunoprecipitates of rat ileal brush border membrane vesicles reveals that it has dipeptidyl peptidase IV activity. Future invesitgations will need to determine the exact substrate specificity of this novel peptidase.

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Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of a Novel Peptidase from Rat and Human Ileum

Shneider

Thevananther

Moyer

et al. 1997

Journal of Biological Chemistry

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“…10). Whether these three species arise by expression from different genes (23,24) or from differential splicing (25) or consist of heteronuclear RNAs remains to be determined. In previous Northern blot experiments, three additional smaller bands of hybridization had been detected in rat brain and kidney with estimated sizes of 2,100, 750, and 500 nucleotides (10).…”

Section: Resultsmentioning

confidence: 99%

Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II

Lüthi-Carter

Berger

Barczak

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…Chromosome 11 contains a number of genetic disease loci in these regions, including vitreoretinopathy (11q13-q23), xeroderma pigmentosa (11q12-q13), atopy (11q12-q13), and perhaps more interestingly, a tumor suppression locus (11p11.2-p11.13) involved in rat prostate carcinoma. Introduction of this portion of the chromosome into highly metastatic rat prostatic cells was able to suppress cancer metastases without suppression of the in vivo growth rate or tumorigenicity of the cells (32). Since it has been shown that NAALADase I expression increases with decreasing androgen levels, it is possible that current prostate cancer treatments involving androgen level reduction (e.g.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Expression of Novel Human Glutamate Carboxypeptidases with N-Acetylated α-Linked Acidic Dipeptidase and Dipeptidyl Peptidase IV Activity

Pangalos¹,

Neefs

Somers³

et al. 1999

Journal of Biological Chemistry

104

107

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Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-Lglutamate (NAAG) by N-acetylated ␣-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. The neuropeptide N-acetyl-L-aspartate-L-glutamate (NAAG)1 is expressed both in the central nervous system and in the periphery. NAAG has been localized to specific sub-populations of neurones and is one of the most abundant peptides in brain, being present in millimolar concentrations in certain brain regions (for review see Ref.

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Prostate-specific membrane antigen: evidence for the existence of a second related human gene

Cited by 78 publications

References 16 publications

Cloning and Characterization of a Novel Peptidase from Rat and Human Ileum

Cloning and Characterization of a Novel Peptidase from Rat and Human Ileum

Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II

Isolation and Expression of Novel Human Glutamate Carboxypeptidases with N-Acetylated α-Linked Acidic Dipeptidase and Dipeptidyl Peptidase IV Activity

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