title: Tissue specificity of the hormonal response in sex accessory tissues is associated with nuclear matrix protein patterns.
abstract: The DNA of interphase nuclei have very specific three-dimensional organizations that are different in different cell types, and it is possible that this varying DNA organization is responsible for the tissue specificity of gene expression. The nuclear matrix organizes the three-dimensional structure of the DNA and is believed to be involved in the control of gene expression. This study compares the nuclear structural proteins between two sex accessory tissues in the same animal responding to the same androgen stimulation by the differential expression of major tissue-specific secretory proteins. We demonstrate here that the nuclear matrix is tissue specific in the rat ventral prostate and seminal vesicle, and undergoes characteristic alterations in its protein composition upon androgen withdrawal. Three types of nuclear matrix proteins were observed: 1) nuclear matrix proteins that are different and tissue specific in the rat ventral prostate and seminal vesicle, 2) a set of nuclear matrix proteins that either appear or disappear upon androgen withdrawal, and 3) a set of proteins that are common to both the ventral prostate and seminal vesicle and do not change with the hormonal state of the animal. Since the nuclear matrix is known to bind androgen receptors in a tissue- and steroid-specific manner, we propose that the tissue specificity of the nuclear matrix arranges the DNA in a unique conformation, which may be involved in the specific interaction of transcription factors with DNA sequences, resulting in tissue-specific patterns of secretory protein expression.
authors.affiliation: Department of Urology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
authors.forename: R H
authors.initials: RH
authors.lastname: Getzenberg
authors.forename: D S
authors.initials: DS
authors.lastname: Coffey
mesh_terms: D000727:Androgen-Binding Protein / Q000096:biosynthesis; D000728:Androgens / Q000502:physiology*; D000818:Animals; D003850:Deoxyribonuclease I / Q000494:pharmacology; D015180:Electrophoresis, Gel, Two-Dimensional; D008297:Male; D015530:Nuclear Matrix / Q000737:chemistry / Q000378:metabolism*; D009687:Nuclear Proteins / Q000032:analysis / Q000378:metabolism*; D009919:Orchiectomy; D011467:Prostate / Q000737:chemistry / Q000378:metabolism*; D060789:Prostatein; D029584:Prostatic Secretory Proteins; D014176:Protein Biosynthesis; D051381:Rats; D011919:Rats, Inbred Strains; D012259:Ribonuclease, Pancreatic / Q000494:pharmacology; D060765:Secretoglobins; D029589:Seminal Plasma Proteins; D012669:Seminal Vesicles / Q000737:chemistry / Q000378:metabolism*; D014018:Tissue Distribution; D014598:Uteroglobin; D060788:Mammaglobin B
chemical_list: D000727:Androgen-Binding Protein; D000728:Androgens; D003850:Deoxyribonuclease I; D009687:Nuclear Proteins; D060789:Prostatein; D029584:Prostatic Secretory Proteins; D012259:Ribonuclease, Pancreatic; D060765:Secretoglobins; D029589:Seminal Plasma Proteins; D014598:Uteroglobin; C511484:Scgb1d2 protein, rat; C511483:Scgb1d4 protein, rat; C043076:beta-microseminoprotein; C556468:Scgb2a1 protein, rat; D060788:Mammaglobin B