Prostasomes from four different species are able to produce extracellular adenosine triphosphate (ATP).
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Ronquist KG, Ek B, Morrell J, Stavreus-Evers A, Ström Holst B, Humblot P, Ronquist G, Larsson A
Biochim. Biophys. Acta 1830 (10) 4604-4610 [2013-10-00; online 2013-05-22]
Prostasomes are extracellular vesicles. Intracellularly they are enclosed by another larger vesicle, a so called "storage vesicle" equivalent to a multivesicular body of late endosomal origin. Prostasomes in their extracellular context are thought to play a crucial role in fertilization. Prostasomes were purified according to a well worked-out schedule from seminal plasmas obtained from human, canine, equine and bovine species. The various prostasomes were subjected to SDS-PAGE separation and protein banding patterns were compared. To gain knowledge of the prostasomal protein systems pertaining to prostasomes of four different species proteins were analyzed using a proteomic approach. An in vitro assay was employed to demonstrate ATP formation by prostasomes of different species. The SDS-PAGE banding pattern of prostasomes from the four species revealed a richly faceted picture with most protein bands within the molecular weight range of 10-150kDa. Some protein bands seemed to be concordant among species although differently expressed and the number of protein bands of dog prostasomes seemed to be distinctly fewer. Special emphasis was put on proteins involved in energy metabolic turnover. Prostasomes from all four species were able to form extracellular adenosine triphosphate (ATP). ATP formation was balanced by ATPase activity linked to the four types of prostasomes. These potencies of a possession of functional ATP-forming enzymes by different prostasome types should be regarded against the knowledge of ATP having a profound effect on cell responses and now explicitly on the success of the sperm cell to fertilize the ovum. This study unravels energy metabolic relationships of prostasomes from four different species.
PubMed 23707955
DOI 10.1016/j.bbagen.2013.05.019
Crossref 10.1016/j.bbagen.2013.05.019
pii: S0304-4165(13)00215-8