The localization and functional significance of arylsulfatases in parasitic sarcosporidian protozoa in the tissue-cyst life cycle phase
Radchenko, A.I.; Beĭer, T.V.; Pashkin, P.I.; Semenov, V.M.
Tsitologiia 39(6): 435-441
1997
ISSN/ISBN: 0041-3771 PMID: 9381560 Document Number: 475872
The hydrolytic enzymes arylsulphatases (AS) were detected in developing tissue cysts of Sarcocystis ovifelis, using two methods: the Goldfischer lead technique, with two different pH values-5.5 (AS-A) and 4.2 (AS-B), and the Hopsu-Havu barium technique (Gayer, 1974). The enzymatic activity was identified by the presence of an electron dense finely granulated precipitation. In cyst cells, lead sulphate precipitation was spotted only in the inner membrane complex (IC) of the pellicle, whereas barium sulphate marked, in addition, the plasma membrane. Besides, AS activity was detected in the endoplasmic reticulum, Golgi complex, lysosomes and micronemes of cyst cells. Of interest is the finding of AS in the outer membrane of IC and matrix of pellicular evaginations. In the cyst ground substance (CGS) of S. ovifelis AS activity is confined to the membrane and matrix of transport vesicles, originating from cyst cell pellicle evaginations. These cystic vesicles carry enzymes from the places of their synthesis, in the cyst cells, to the tissue cyst periphery near the cyst wall. In the CGS, the obvious precipitations of lead and barium sulphate, respectively, are seen around some cyst cells being in the state of destroying due to natural death, and around so-called apoptotic-like bodies made from the destroyed cells. AS activity is seen both in the cyst wall and in vesicles separating from the wall ("wall vesicles") that find eventually their way in the cytoplasm of infected muscle cells, the granulation being observed around destroyed organelles of such cells. The investigated dynamics of AS movement, by means of the transport cystic and wall vesicles, extends general knowledge of the distant metabolic interaction between cells of the host and the parasite in tissue cysts of Sarcocystis spp.