An Inhibitor of Urokinase and Tissue Plasminogen Activators in Dunning R3327H Prostate Tumors of Rats Treated with &lt;i&gt;D&lt;/i&gt;&lt;i&gt;-&lt;/i&gt;Trp&lt;sup&gt;6&lt;/sup&gt;-LH-RH

Hierowski, Marion T.

doi:10.1159/000180036

Cited by 9 publications

(4 citation statements)

References 27 publications

(35 reference statements)

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“…The PAI synthesized by cultured rat granulosa cells is also immunologically related to the BAE PAI (40), suggesting that this class ofPAIs may regulate a variety of processes involving plasminogen activation. The relationship of these PAIs to the PAIs elaborated by macrophages (37), uterine cells (41), and tumor cells (42) remains to be determined.…”

Section: Resultsmentioning

confidence: 99%

The primary plasminogen-activator inhibitors in endothelial cells, platelets, serum, and plasma are immunologically related.

Erickson¹,

Hekman²,

Loskutoff³

1985

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

142

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Monospecific antiserum to an unusually stable Mr 50,000 plasmmiogen-activator inhibitor (PAI) purified from cultured bovine aortic endothelial cells was employed in conjunction with reverse fibrin autography to determine whether human platelets, serum, and plasma contain immunologically related inhibitors. Reverse fibrin autography revealed the presence of a Mr 50,000 inhibitor in the platelet and serum samples but not in normal plasma. However, a Mr 50,000 inhibitor was detected in plasma obtained from individuals with increased PAI activity. In each case, treatment of

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Section: Resultsmentioning

confidence: 99%

The primary plasminogen-activator inhibitors in endothelial cells, platelets, serum, and plasma are immunologically related.

Erickson¹,

Hekman²,

Loskutoff³

1985

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

142

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“…Both urokinase and tissuetype activator are expressed in the PA-I11 tumor cell line from Lobund-Wistar rats (Strickland et al, 1983) and in the spontaneous tumors found in the ventral prostate of aged Fisher-344 rats . Treatment of rats bearing Dunning R3327H tumors with D-trp'-LH-RH decreases tumor volume and tumor plasminogen activator activities; the latter are blocked by a 21 kDa inhibitor that is induced in the tumor by this treatment (Hierowski and Schally, 1985). Thus, there is also a strong correlation of increased plasminogen activator activities with prostatic tumors in the rat.…”

Section: Proteases In Prostate Diseasementioning

confidence: 91%

Proteases in prostate development, function, and pathology

Wilson

1995

Microscopy Res & Technique

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INTRODUCTIONThe prostate gland and its secretions have long been known to contain a variety of potent proteolytic activities (Mann and Lutwak-Mann, 1981). The functions of these proteases and peptidases in the control of normal cellular operations in the prostate gland (especially as affected by androgens), in the steps of tumor progression in prostate cancer, and in interacting with sperm and seminal constituents secreted by other accessory glands into the semen are not understood. The proteases secreted into the semen have been postulated to degrade seminal proteins, especially to produce liquefaction of seminal coagulum in humans, and to possibly interact with sperm so as to modify their cell surfaces and affect their fertilizing ability. Recently, more attention has been given to prostatic proteases that can modify extracellular matrix proteins and especially in relation to tissue organization changes that occur during normal growth in prostate development and in the generation of pathology in prostate diseases. Proteases and peptidases of each catalytic group (i.e., serine, cysteine, aspartic, and metalloproteases) are produced by the prostate and are found in its secretions. Although a number of amino-and carboxy-exopeptidases and serine and metallopeptidases active towards small peptides are produced by the prostate and may have important functions in the gland and in its secretion, this review will focus on our present understanding of the roles of proteases (endopeptidases that cleave internal peptide bonds in proteins) in the development of the prostate, in its secretions, and in the generation of pathology that commonly occurs with aging in the gland.

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“…Using these cell lines it was demonstrated that various biochemical markers for metastatic phenotypes, such as Ecadherin, differed in the sublines [23][24][25]. Elevated levels of plasminogen activator [26], and of MMP-2 and MMP-9 [16], were found in the Dunning rat prostate tumor when compared with the dorsal prostate, which is considered the tissue source of the original tumor [21]. Although Lowe and Isaacs [23] did not detect any difference in plasminogen activator or matrix metalloproteinase activities in variants of the Dunning tumor cell lines, inhibition of u-PA activity was shown to decrease tumor volume [26].…”

Section: Introductionmentioning

confidence: 99%

Plasminogen activator and matrix metalloproteinase production and extracellular matrix degradation by rat prostate cancer cells in vitro: Correlation with metastatic behavior in vivo

Quax¹,

Bart²,

Schalken

et al. 1997

Prostate

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An Inhibitor of Urokinase and Tissue Plasminogen Activators in Dunning R3327H Prostate Tumors of Rats Treated with <i>D</i><i>-</i>Trp<sup>6</sup>-LH-RH

Cited by 9 publications

References 27 publications

The primary plasminogen-activator inhibitors in endothelial cells, platelets, serum, and plasma are immunologically related.

The primary plasminogen-activator inhibitors in endothelial cells, platelets, serum, and plasma are immunologically related.

Proteases in prostate development, function, and pathology

Plasminogen activator and matrix metalloproteinase production and extracellular matrix degradation by rat prostate cancer cells in vitro: Correlation with metastatic behavior in vivo

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