Prostate alpha-protein. Complete amino acid sequence of the component that inhibits nuclear retention of the androgen-receptor complex.

Liao, Shutsung; Chen, Chunshing; Huang, I‐Yih

doi:10.1016/s0021-9258(19)68334-1

Cited by 19 publications

(1 citation statement)

References 14 publications

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“…The 12K polypeptide actually contains two polypeptides of MT13K and 1 IK which, together with the 8K polypeptides, constitute the subunit components of PBP1 (Heyns & De Moor, 1977;Heyns et all., 1978;Lea et al, 1977Lea et al, , 1979Forsgren et al, 1979) a-protein (Shyr & Liao, 1978). PBP has been purified (Heyns et al, 1978;, extensively characterized (Heyns & De Moor, 1977;Peeters et al, 1981Peeters et al, , 1982Liao et al, 1982), and shown to be a steroidbinding prostate secretory protein, but the 20K protein has not been isolated so far. However, initial studies (Parker et al, 1978) of the 20K protein on polyacrylamide gel with Schiff s reagent and by electrophoresis of lectin-bound prostatic proteins indicate that the 20K protein is a glycopeptide.…”

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Isolation, properties, and androgen regulation of a 20-kilodalton protein from rat ventral prostate

Chamberlin¹,

Mpanias²,

Wang³

1983

Biochemistry

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An abundant 20-kilodalton protein has been isolated from the cytosol fraction of rat ventral prostate by ammonium sulfate precipitation, DNA-cellulose chromatography, and gel filtration. The purified 20K protein is a glycoprotein, containing 11% hexose by weight. It contains no fucose, hexosamine, or sialic acid. The 20K protein does not bind androgen. Binding of the 20K protein to DNA is nonspecific, showing affinity toward DNAs of various tissue origins, as well as poly(dA-dT), poly(rI-rC), and phosphocellulose. The 20K protein comprises about 9% of the total cytosolic proteins in rat ventral prostate. Examination of eight different rat organs, including prostate secretion, lateral and dorsal prostates, and rat ejaculate, for the presence of the 20K protein by double immunodiffusion analysis revealed that the protein is a rat ventral prostate specific secretory protein. Hybridization of prostatic poly(A) RNA with a cloned cDNA coding for the 20K protein indicated that the synthesis of the 20K protein is regulated by testosterone at the mRNA level.

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Isolation, properties, and androgen regulation of a 20-kilodalton protein from rat ventral prostate

Chamberlin¹,

Mpanias²,

Wang³

1983

Biochemistry

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Purification of estramustine‐binding protein and production of monoclonal antibodies to its different components

Björk¹,

Donn

Glad

et al. 1995

The Prostate

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Estramustine-binding protein (EMBP) is a heterodimeric 46-kDa glycoprotein that is secreted from the prostate. Upon reductive cleavage it decomposes into two closely related components, C1 and C2, and the shared glycosylated peptide C3. EMBP binds estramustine and estromustine, the active metabolites of estramustine phosphate (Estracyt), which is a drug with antimitotic properties used in the treatment of prostatic carcinoma. In the present study, a two-step procedure (i.e., anion-exchange and Con A-Sepharose chromatography) is described for the isolation of EMBP in high yield from rat prostate tissue. Mouse monoclonal antibodies (mAbs) were produced using the major DEAE-Sepharose fraction of EMBP as an immunogen. Eleven mAbs were selected by screening in a solid-phase ELISA. One displayed high-affinity binding with soluble EMBP (Ka approximately 3 x 10(10) M-1) and crossreacted with a human prostate tumor extract in a radioimmunoassay. The epitopes defined by these mAbs were analyzed by Western immunoblotting. All constituents of EMBP, except component C1, were identified by at least one antibody. Nine visualized either one or both of the two EMBP subunits under denaturing conditions, two of which retained their reactivity after reduction of disulfide bridges. One epitope was exposed to its mAb only when the antigen was in its reduced state. The immunoreactivity was eliminated by protease treatment, whereas deglycosylation with glycopeptidase F had a minimal effect. EMBP has been detected in tissues other than the prostate as well as in prostate neoplastic specimens and in several other human malignancies. Hence, these mAbs will be a useful tool in the characterization of EMBP in different tissues and in evaluating existing and in defining new indications for Estracyt therapy.

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Alpha-Protein: A Marker for Androgen Action in the Rat Ventral Prostate

Judge¹,

Saltzman²,

Liao³

1983

Gene Regulation by Steroid Hormones II

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Prostate alpha-protein. Complete amino acid sequence of the component that inhibits nuclear retention of the androgen-receptor complex.

Cited by 19 publications

References 14 publications

Isolation, properties, and androgen regulation of a 20-kilodalton protein from rat ventral prostate

Isolation, properties, and androgen regulation of a 20-kilodalton protein from rat ventral prostate

Purification of estramustine‐binding protein and production of monoclonal antibodies to its different components

Alpha-Protein: A Marker for Androgen Action in the Rat Ventral Prostate

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