Biomaterial Database

Expression of heme oxygenase-1 (HSP32) in human prostate: normal, hyperplastic, and tumor tissue distribution. 1996

M D Maines, and P A Abrahamsson

Department of Biophysics, University of Rochester School of Medicine, NY 14642, USA.

OBJECTIVE Heme oxygenase isozymes, HO-1 and HO-2, are members of the stress/heat shock (HSP) family of proteins, with the known function of cleaving the heme molecule to biliverdin, iron, and carbon monoxide. The aim of this study was to examine the pattern of tissue expression of HO-1 in the human prostate under different states of proliferation and differentiation and to investigate whether the pattern differs between these states. METHODS Presently, we have determined the pattern of tissue expression of the stress-inducible isozyme, HO-1 (HSP32), in human prostate under normal and pathologic conditions, by immunohistochemistry, using polyclonal antibodies, and have measured HO-1 and HO-2 mRNA levels in normal prostate and benign prostatic hyperplasia (BPH) by Northern blotting. The activity of prostate to catalyze heme degradation was also assessed. RESULTS In normal and BPH tissue, columnar epithelial cells of acini and ducts and cells in stroma displayed HO-1 immunoreactivity; in all cells, perinuclear staining was prominent. In BPH tissue, however, a more intense staining of the epithelial cells occurred, with notable staining of the basal cells. In undifferentiated malignant tumors, intense HO-1 staining was manifest in nearly all tumor cells, and also in the epithelial lining of blood vessels. HO-1 in the prostate tissue was found catalytically active and oxidatively cleaved the heme molecule (Fe-protoporphyrin IX) to biliverdin. Northern blot analysis shows that two forms of HO are present in the human prostate. Compared with normal tissue, predominantly hyperplastic tissue demonstrates a pronounced increase in the approximately 1.8 kb mRNA that hybridizes to the rat HO-1 probe. The levels of two transcripts, approximately 1.3 and approximately 1.7 kb, that hybridize to the rat HO-2 probe are not increased in BPH tissue. CONCLUSIONS The finding that HO-1 expression is increased in BPH and malignant prostate tissue is consistent with a role for this stress protein in the pathogenesis of BPH and prostate cancer; in the context of iron metabolism, an argument is made in support of this possibility.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008875	Middle Aged	An adult aged 45 - 64 years.	Middle Age
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011467	Prostate	A gland in males that surrounds the neck of the URINARY BLADDER and the URETHRA. It secretes a substance that liquefies coagulated semen. It is situated in the pelvic cavity behind the lower part of the PUBIC SYMPHYSIS, above the deep layer of the triangular ligament, and rests upon the RECTUM.	Prostates
D011470	Prostatic Hyperplasia	Increase in constituent cells in the PROSTATE, leading to enlargement of the organ (hypertrophy) and adverse impact on the lower urinary tract function. This can be caused by increased rate of cell proliferation, reduced rate of cell death, or both.	Adenoma, Prostatic,Benign Prostatic Hyperplasia,Prostatic Adenoma,Prostatic Hyperplasia, Benign,Prostatic Hypertrophy,Prostatic Hypertrophy, Benign,Adenomas, Prostatic,Benign Prostatic Hyperplasias,Benign Prostatic Hypertrophy,Hyperplasia, Benign Prostatic,Hyperplasia, Prostatic,Hyperplasias, Benign Prostatic,Hypertrophies, Prostatic,Hypertrophy, Benign Prostatic,Hypertrophy, Prostatic,Prostatic Adenomas,Prostatic Hyperplasias, Benign,Prostatic Hypertrophies
D011471	Prostatic Neoplasms	Tumors or cancer of the PROSTATE.	Cancer of Prostate,Prostate Cancer,Cancer of the Prostate,Neoplasms, Prostate,Neoplasms, Prostatic,Prostate Neoplasms,Prostatic Cancer,Cancer, Prostate,Cancer, Prostatic,Cancers, Prostate,Cancers, Prostatic,Neoplasm, Prostate,Neoplasm, Prostatic,Prostate Cancers,Prostate Neoplasm,Prostatic Cancers,Prostatic Neoplasm
D006419	Heme Oxygenase (Decyclizing)	A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt.	Haem Oxygenase,Heme Oxygenase,Oxygenase, Haem,Oxygenase, Heme
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000368	Aged	A person 65 years of age or older. For a person older than 79 years, AGED, 80 AND OVER is available.	Elderly
D001483	Base Sequence	The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.	DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA