Changes of an androgen-dependent nuclear protein during functional differentiation and by dedifferentiation of the dorsolateral prostate of rats

Matuo, Yuhsi; Nishi, Nozomu; Tanaka, Yukio; Muguruma, Yasuyoshi; Tanaka, Kōichiro; Akatsuka, Yoshiki; Matsui, Sei Ichi; Sandberg, Avery A.; Wada, Fumio

doi:10.1016/0006-291x(84)91326-3

Cited by 15 publications

(9 citation statements)

References 6 publications

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“…Probasin mRNA expression, which is regulated by androgens, gives rise to both a secreted and a nuclear form of probasin [129], the relative abundance of the two forms being correlated with cell type. Probasin concentration also seems to be closely linked with cell age and state of differentiation, consistent with a role in cell regulation [128].…”

Section: Cell Regulationsupporting

confidence: 62%

“…Probasin, originally isolated from the nuclei of rat dorsolateral prostate epithelial cells [128], is another lipocalin implicated in cell regulation. Probasin mRNA expression, which is regulated by androgens, gives rise to both a secreted and a nuclear form of probasin [129], the relative abundance of the two forms being correlated with cell type.…”

Section: Cell Regulationmentioning

confidence: 99%

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The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,527

1,278

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The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level ; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel β-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily : the calycins. Members of the lipocalin family are characterized by several common molecular-

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Section: Cell Regulationsupporting

confidence: 62%

Section: Cell Regulationmentioning

confidence: 99%

The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,527

1,278

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“…Probasin (PB), isolated originally from dorsolateral prostate nuclei, is an androgen-regulated nuclear protein (8) that increases in concentration with zinc uptake (9). In this report, we show that the translation product corresponding to the cDNA clone pM-40 (10) is PB.…”

Section: Introductionmentioning

confidence: 88%

“…The rat pM-40 cDNA sequence (Fig. 1) predicts a protein nearly identical in amino acid composition, molecular weight, and pI to PB, a rat dorsolateral prostate nuclear protein (8,9), suggesting that the pM-40 cDNA encodes PB. This was proven by purification of PB from the prostate and N-terminal sequencing.…”

Section: Methodsmentioning

confidence: 99%

“…The Western blots show that the polyclonal antibody does not crossreact with histones. Initially, Matuo et al (8,9) reported that PB was an abundant prostatic nuclear protein. Subsequently, they reported that immunofluorescence staining with an anti-PB monoclonal antibody localized the protein within prostatic ducts with hardly any staining in the nuclei (24).…”

Section: Pavfkidalnenkvlvl-dtdyki-yllfcmenisaepeqslicqcl ---Vrtmentioning

confidence: 99%

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Regulation of a bifunctional mRNA results in synthesis of secreted and nuclear probasin.

Spence

Sheppard

Davie

et al. 1989

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

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Probasin, a rat prostatic protein, is statistically related to members of a protein family that includes serum, cellular, and nuclear proteins. In vivo, probasin appears both in the secretions and in the nucleus of prostatic epithelial cells. Using primer extension and S1 nuclease protection assays we detected only one probasin mRNA. Thus, the localization of this protein to two separate cellular regions must be encoded by this one mRNA. Furthermore, in vitro translation of synthetic probasin mRNA demonstrated that a protein containing a signal peptide and a protein lacking a signal peptide were synthesized by initiation at different AUG codons. These data are consistent with a mechanism of translational regulation of a eukaryotic bifunctional mRNA.

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Comparison of subcellular proteins of normal prostate, benign prostatic hypertrophy, and prostatic cancer: Presence of BPH‐associated nonhistone proteins

et al. 1985

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Proteins in the cytosol, postnuclear particulate, and nuclear fractions from seven specimens of normal prostate from bladder cancer patients, 14 specimens of benign hypertrophic prostate (BPH), and three specimens of cancerous prostate were analyzed and compared by SDS-polyacrylamide slab gel electrophoresis. Abundant protein species in the cytosol fractions were 60K (species having a molecular weight of about 60,000) and 42K; their relative contents were about 35% for 60K and about 12% for 42K. In the postnuclear particulate fraction, 42K was the most abundant (about 10% of the total). The contents of these major protein species were similar in specimens of normal and diseased prostates. In addition, there are marked similarities in the electrophoretic patterns for all the protein (24-29 species) in the cytosol and postnuclear particulate fractions of the human prostate, except for four minor species in the cytosol fraction. Of the nuclear proteins, the content of core histones (H2A, H2B, H3, and H4) was fundamentally similar among all the specimens, whereas the content of H1 histone was different from one specimen to another. The most remarkable and significant difference was that the 42K-NHP (nonhistone protein having a molecular weight of about 42,000), 55K-NHP, and 190K-NHP concentrations were significantly higher in BPH than in normal and cancerous prostates.

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Changes of an androgen-dependent nuclear protein during functional differentiation and by dedifferentiation of the dorsolateral prostate of rats

Cited by 15 publications

References 6 publications

The lipocalin protein family: structure and function

The lipocalin protein family: structure and function

Regulation of a bifunctional mRNA results in synthesis of secreted and nuclear probasin.

Comparison of subcellular proteins of normal prostate, benign prostatic hypertrophy, and prostatic cancer: Presence of BPH‐associated nonhistone proteins

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