| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on July 28, 2003
Accepted on December 8, 2003
1 Departments of Urology (SO, FJ, XC, RH, ZD, and ZW) and Molecular Pharmacology and Biological Chemistry (SO, FJ, and ZW), The Robert H. Lurie Comprehensive Cancer Center (ZW), Feinberg School of Medicine, Northwestern University, Chicago, IL 60611
* To whom correspondence should be addressed. E-mail: wangz{at}northwestern.edu.
The ARD-like protein 1 (ALP1) gene was identified in a comprehensive cDNA subtraction aimed at identifying genes regulated by androgens in the rat ventral prostate. ALP1 is homologs to the ARD/ ARD', aci-reductone dioxygenases, that were discovered in Klebsiella pneumoniae as enzymes that have the same polypeptide sequence and differ only in their metal content. This family of proteins is evolutionarily conserved from bacteria to humans and is involved in the methionine salvage pathway. Northern and Western blot confirmed the regulation of ALP1 by androgens in the rat ventral prostate. ALP1 mRNA is expressed in a variety of tissues; however, its regulation by androgens was specific to the prostate. ALP1 is expressed by the glandular epithelial cells of the rat prostate, with little or no expression in the stromal cells. ALP1 is down-regulated in the different rat Dunning tumor cell lines compared with the normal or castrated rat prostate. Expression studies showed that ALP1 overexpression is not tolerated by AT6.1 cells. Further studies demonstrated that ALP1 is also down-regulated in the human prostate cancer cell lines LNCaP, PC3, and DU145 and overexpression induces cell death in these cells. Taken together, our observations suggest that ALP1 may have an important role in androgen regulated prostate homeostasis as well as in prostate cancer progression by regulating cell death of prostate cancer cells.
This article has been cited by other articles:
 |
|
 |
|
  I. Gotoh, T. Uekita, and M. Seiki Regulated nucleo-cytoplasmic shuttling of human aci-reductone dioxygenase (hADI1) and its potential role in mRNA processing. Genes Cells, January 1, 2007; 12(1): 105 - 117. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Zer and G. Chanfreau Regulation and Surveillance of Normal and 3'-Extended Forms of the Yeast Aci-reductone Dioxygenase mRNA by RNase III Cleavage and Exonucleolytic Degradation J. Biol. Chem., August 12, 2005; 280(32): 28997 - 29003. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Hirano, I. Gotoh, T. Uekita, and M. Seiki Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway Genes Cells, June 1, 2005; 10(6): 565 - 574. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Endocrinology | Endocrine Reviews | J. Clin. End. & Metab. |
| Molecular Endocrinology | Recent Prog. Horm. Res. | All Endocrine Journals |
