Phospholipase A&lt;sub&gt;2&lt;/sub&gt; Activity in Prostasomes from Human Seminal Plasma

Lindahl, Mattias; Tagesson, Christer; Ronquist, Gunnar

doi:10.1159/000281999

Cited by 47 publications

(33 citation statements)

References 5 publications

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“…This idea is in line with our previous demonstration of release of CD59 after incubation with PIPLC and their subsequent (re-)saturation with CD59 upon incubation with prostasomes [136]. Prostasomes contain a very active phospholipase A 2 [142] but PIPLC has so far not been reported in prostasomes. A transfer also requires a close interaction between prostasomes and acceptor cells.…”

Section: Mechanism Of Transfer Of Prostasomal Cd59 To Cd59-deficiesupporting

confidence: 89%

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Babiker¹,

Ronquist²,

Nilsson³

et al. 2010

TOPCANJ

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Prostasomes are extracellularly occurring submicron, membrane-surrounded organelles produced by the epithelial cells of the prostate and present in semen after secretion. Even dedifferentiated prostate cancer cells have preserved their ability to produce and export prostasomes to the extracellular space. The precise physiological role of prostasomes is not known, although some of their properties assign them to important physiological and patho-physiological functions that could be exploited in prostate cancer growth and development. In this review, some new properties of seminal and malignant cell line (DU145, PC-3 and LNCaP) prostasomes will be discussed.There are typical differences in the expressions and activities of prostasomal CD59, ATPase, protein kinases and tissue factor (TF) as well as in the transfer of prostasomal CD59 to CD59-deficient erythrocytes (rabbit and human PNH erythrocytes). CD59, protein kinases and TF exhibit characteristic patterns of overexpression by malignant cell prostasomes. A high ATPase activity is recognized on seminal prostasomes with minimal activity on malignant cell prostasomes resulting in more residual ATP available for phosphorylation reactions. Several proteins are phosphorylated by prostasomal protein kinases, namely, complement component C3, fibrinogen, vitronectin and E-cadherin. Furthermore, TF is identified as the main endogenous phosphorylation substrate on prostasomes. In addition, prothrombotic effects of prostasomes are demonstrated. DU145 and PC-3 cell-derived prostasomes exert a higher clotting effect on whole blood and plasma compared to LNCaP cell-derived and seminal prostasomes.In conclusion, malignant cell prostasomes show an increased ability to interact with the biological system in favor of prostate cancer cell promotion and survival. The roles played by prostasomes in this context may improve the understanding of the mechanisms that help the prostate cancer cells to avoid the complement attack (CD59 transfer and phosphorylation and inactivation of C3), to promote angiogenesis (TF) and to metastasize. It may also provide a better understanding of some of the complications usually seen in some terminal prostate cancer patients like thrombotic events and tendency to develop disseminated intravascular coagulation.Keywords: ATPase, CD59, CK, complement, DU145, Extracellular phosphorylation, LNCaP, PC-3, PKA, PKC, prostasomes, prostate cancer, protein kinases, tissue factor. I. GENERAL BACKGROUND A. Prostate CancerProstate cancer is the most prevalent noncutaneous cancer in many of the Western countries and is the second leading cause of cancer death in men in USA [1]. The introduction of prostate specific antigen (PSA) in the latter half of 1980s as a biochemical marker of prostate cancer in serum signified a radical change of the pattern of prostate cancer diagnosis. It meant that more cases were detected at an early stage and substantially fewer at advanced stages [2] [3]. There are also studies showing that increasing incidence of prostate can...

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Section: Mechanism Of Transfer Of Prostasomal Cd59 To Cd59-deficiesupporting

confidence: 89%

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Babiker¹,

Ronquist²,

Nilsson³

et al. 2010

TOPCANJ

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“…The organelles are exceedingly heterogenous as regards protein composition [4, 5]. They have a netto–negative charge [28], and accordingly, the cationic proteins from the seminal vesicles may bind to the prostasome membrane.…”

Section: Discussionmentioning

confidence: 99%

“…They are surrounded by a bilayered and sometimes tri– or multilayered membrane having a diameter of 40–500 nm [3]. The membrane architecture of these organelles is complex and two–dimensional gel electrophoresis of membrane material has revealed about 80 different protein entities [4, 5]. Also, an unusually high cholesterol/phospholipid ratio is inherent in this membrane [6].…”

Section: Introductionmentioning

confidence: 99%

Growth–Inhibitory Effect of Prostasomes on Prostatic Cancer Cell Lines in Culture

Carlsson

Lennartsson²,

Nilsson³

et al. 2000

European Urology

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“…Al though the physiological role of these organelles has not been elucidated, the membrane encasing them is com plex with regard to protein composition [6] and contains several enzyme systems [7], The aim of the present work was to investigate whether LD was associated with pros tasomes to any appreciable extent.…”

Section: Introductionmentioning

confidence: 99%

Isoenzyme Pattern of Lactate Dehydrogenase Associated with Human Prostasomes

Olsson¹,

Ronquist

1990

Urol Int

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Lactate dehydrogenase (LD, EC 1.1.1.27) activity was determined in serum, seminal plasma and prostasomes from normozoospermic and azoospermic (due to vasectomy) men. A 10-fold higher activity was noted in seminal plasma as compared with serum. LD activity was enriched in prostasomes although a fairly large amount of enzyme activity seemed to be free in solution. Isoenzymes LD₁, LD₂ and LD₃, present in prostasomes in about equal amounts, gave rise to a characteristic isoenzyme pattern that differed distinctly from that found in seminal plasma of normozoospermic men, the main isoenzyme of which was LD-X.

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Phospholipase A<sub>2</sub> Activity in Prostasomes from Human Seminal Plasma

Cited by 47 publications

References 5 publications

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Growth–Inhibitory Effect of Prostasomes on Prostatic Cancer Cell Lines in Culture

Isoenzyme Pattern of Lactate Dehydrogenase Associated with Human Prostasomes

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Phospholipase A<sub>2</sub> Activity in Prostasomes from Human Seminal Plasma

Cited by 47 publications

References 5 publications

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Prostasome Involvement in the Development and Growth of Prostate Cancer~!2009-07-10~!2009-12-09~!2010-02-11~!

Growth&ndash;Inhibitory Effect of Prostasomes on Prostatic Cancer Cell Lines in Culture

Isoenzyme Pattern of Lactate Dehydrogenase Associated with Human Prostasomes

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Growth–Inhibitory Effect of Prostasomes on Prostatic Cancer Cell Lines in Culture