Localization of prostatic basic protein (“probasin”) in the rat prostates by use of monoclonal antibody

Matuo, Yuhsi; Nishi, Nozomu; Muguruma, Yasuyoshi; Yoshitake, Yoshino; Kurata, Noriyuki; Wada, Fumio

doi:10.1016/0006-291x(85)90416-4

Cited by 29 publications

(12 citation statements)

References 8 publications

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“…These secreted proteins include prostatic binding protein [10][11][12][13][14], proline-rich peptide [15], 20-22-kDa glycoprotein [16][17][18], aminopeptidases [19], plasminogen activator [20], and esterase A [21] by the ventral lobe. The lateral prostate secretes a 16-kDa protein [22] and probasin [23,24] while the dorsal lobe secretes dorsal proteins I and II [25] and a secretory transglutaminase [26]. We have also detected Ca2+-stimulated gelatinolytic proteinase activities in the secretions of the ventral [27] and lateral [28] prostatic lobes.…”

Section: Introductionmentioning

confidence: 80%

Gelatinolytic and Caseinolytic Proteinase Activities in the Secretions of the Ventral, Lateral, and Dorsal Lobes of the Rat Prostate1

Wilson

García²,

Woodson³

et al. 1993

Biology of Reproduction

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The ventral, lateral, and dorsal lobes of the rat prostate produce secretions rich in protein. We examined these secretions for proteinase activities, using gelatin- and casein-containing SDS-polyacrylamide gel zymographies. The ventral lobe demonstrated both higher activities and more molecular forms of proteinase activities that cleaved these two protein substrates than did the other lobes. Ca(2+)-stimulated gelatinolytic activities of approximately 48, 51, 58, 64, 74, and 80 kDa were found in ventral prostate secretions in addition to activities detected in the absence of added Ca2+: a very strong 27-kDa activity; prominent 22-, 86-, 90-, and 94-kDa activities; and less active 36-, 41-, 100-, 130-, and 140-kDa activities. Ca(2+)-stimulated gelatinolytic activities of 51, 58, 74, 80, 86, 90, and 94 kDa were present in lateral prostate secretions (none were detected in secretions of the dorsal lobe), and Ca(2+)-independent activities of 25, 27, and 100 kDa were found in secretions of both the lateral and dorsal lobes. The Ca(2+)-stimulated activities were inhibited by EGTA and EDTA. Benzamidine inhibited all gelatinolytic activities except for the 22-, 25-, and 27-kDa Ca(2+)-independent forms when Ca2+ was not added to the reaction buffer. However, in the presence of 5 mM CaCl2, the Ca(2+)-stimulated forms of proteinase were unaffected by benzamidine, whereas the other activities sensitive to benzamidine were inhibited. Prominent Ca(2+)-independent caseinolytic activities of 20, 23, 31, 37, 83, 89, and 94 kDa were detected in ventral lobe secretions along with less active forms of about 39, 48, 53, 57, 60, 63, 80, 103, 110, 125, and 160 kDa. Caseinolytic activities of approximately 23, 31, 53, 89, 94, 103, 120, and 125 kDa were found in lateral prostate secretions, and 89, 94, and 103 kDa activities were found in secretions of the dorsal lobe. Quantitatively, most gelatinolytic and caseinolytic activities were present in the soluble portion of the secretion of each prostatic lobe. The ventral, lateral, and dorsal prostate lobes all secrete gelatinolytic and caseinolytic proteinase activities; however, quantitatively the ventral lobe is the most notable in this function since its secretions contain more molecular forms and greater activities of these proteinases.

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Section: Introductionmentioning

confidence: 80%

Gelatinolytic and Caseinolytic Proteinase Activities in the Secretions of the Ventral, Lateral, and Dorsal Lobes of the Rat Prostate1

Wilson

García²,

Woodson³

et al. 1993

Biology of Reproduction

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“…In contrast with SVSII, rebound of the probasin mRNA level is observed 6 days after castration and reaches a normal level 12 days after castration (21,30). A similar study using immunohistochemistry has shown that probasin is not detected in the acinar lumen, but its staining is still detected in the prostatic epithelium after castration for 7 days (20). However, regulation of the rebound in castrated LP remains unclear.…”

Section: Discussionmentioning

confidence: 93%

A Comparative Study of Hormonal Regulation of Three Secretory Proteins (Prostatic Secretory Protein-PSP94, Probasin, and Seminal Vesicle Secretion II) in Rat Lateral Prostate**This work was supported by an RGC Earmarked Research Grant (CUHK 4131/00M) from the Hong Kong Research Grant Council (to F.L.C.) and a grant from the Medical Research Council of Canada (to J.W.X.).

et al. 2000

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The rat dorsolateral prostate secretes several major known proteins, although their physiological and reproductive functions are largely undefined. In the present study we examined and compared the in vivo hormonal regulation of the messenger RNA (mRNA) expression of three major secretory proteins, including prostatic secretory protein of 94 amino acids (PSP94 or beta-microseminoprotein), probasin, and seminal vesicle secretion II (SVSII), in long-term castrated lateral prostates (LP) by in situ hybridization and semiquantitative RT-PCR. The protein levels of PSP94 in the castrated LPs were also examined by Western blotting. PSP94 is a small protein newly isolated from the rat prostate gland and demonstrates highly specific expression in the LP. The results of in situ hybridization showed that PSP94, probasin, and SVSII were highly expressed in the intact LP. The hybridization signals of probasin and PSP94 disappeared in the 60-day postcastrated LPs, whereas the signals of SVSII dropped sharply in the 14-day postcastrated LPs. Similar patterns of decreasing mRNA levels of the three proteins in the castrated LPs were observed by RT-PCR analysis. Their mRNA transcripts were restored to normal levels after replacement with testosterone. The results indicate that these secretory proteins are all under androgen regulation in the rat LP. Interestingly, we also observed that their degrees of sensitivity or responsiveness to androgen withdrawal are different. Their mRNA levels dropped in response to duration of castration in the following decreasing order: SVSII, PSP94, and probasin. Besides androgen [dihydrotestosterone (DHT)], we also examined the effects of glucocorticoid [dexamethasone (DEX)], progestin [medroxyprogesterone acetate (MPA)], and zinc on their gene expressions in castrated LPs. We observed that the mRNA transcripts of both PSP94 and probasin were increased after treatments with DHT, DEX, and MPA, suggesting that these two proteins could also be regulated by glucocorticoid and progestin. In contrast with probasin, PSP94 and SVSII were not induced by ZnSO4 treatment. On the other hand, SVSII expression was only increased significantly by DHT and moderately by MPA, but not by DEX, suggesting that SVSII is under strict control by androgen.

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“…Since protein expression in both the VP (e.g., prostatic binding proteins (Parker and Scrace, 1979;Parker et al, 1980)) and the DLP (e.g., probasin (Matuo et al, 1985)) is controlled by androgen, it seems unlikely that di erential expression of androgen receptors is responsible. It seems more probable that these lobespeci®c di erences in regulation result from variations in the levels of transcription factors or transcription adapters (co-activators) that are expressed in both VP and DLP but have di erent responses to androgen regulation.…”

Section: Discussionmentioning

confidence: 99%

Expression and androgen regulation of C-CAM cell adhesion molecule isoforms in rat dorsal and ventral prostate

Makarovskiy

et al. 1999

Oncogene

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Localization of prostatic basic protein (“probasin”) in the rat prostates by use of monoclonal antibody

Cited by 29 publications

References 8 publications

Gelatinolytic and Caseinolytic Proteinase Activities in the Secretions of the Ventral, Lateral, and Dorsal Lobes of the Rat Prostate1

Gelatinolytic and Caseinolytic Proteinase Activities in the Secretions of the Ventral, Lateral, and Dorsal Lobes of the Rat Prostate1

Expression and androgen regulation of C-CAM cell adhesion molecule isoforms in rat dorsal and ventral prostate

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