M. Benchimol et al., Structure and division of the Golgi complex in Trichomonas vaginalis and Tritrichomonas foetus, EUR J CELL, 80(9), 2001, pp. 593-607
We present observations on the fine structure and the division process of t
he Golgi complex in the protists Trichomonas vaginalis and Tritrichomonas f
oetus, parasites of the urogenital tract of humans and cattle, respectively
. The Golgi in trichomonads is a prominent structure, associated with stria
ted parabasal filaments to which this organelle seems to be connected. We f
ollowed by immunofluorescence and electron microscopy the Golgi in interpha
sic and mitotic cells. Ultrastructural studies were performed using fast-fr
eezing fixation, immunocytochemistry using antisera to the known adhesins A
P65 and AP51, cytochemistry (acid phosphatase, Ca-ATPase, zinc iodide-osmiu
m tetroxide technique (ZIO), for analysis of distribution of the endoplasmi
c reticulum and Golgi complex, and Thiery's techniques), routine and serial
thin-sections. Three-dimensional reconstruction, NBD-ceramide, fluorescent
lectin (WGA) and nocodazole treatments were also used. We demonstrate that
: (1) the Golgi in trichomonads is a single-copy organelle; (2) presents a
fenestrated structure; (3) is formed by 8-12 saccules; (4) is connected to
the parabasal filaments by thin filamentous bridges; (5) by cytochemistry,
presents a positive reaction for the lectin WGA, Ca++-ATPase, acid phosphat
ase, ZIO and Thiery's techniques; (6) does not appear to break down at any
point of the cell cycle; (7) elongates during the cell cycle by lateral gro
wth; (8) is labeled by anti-glutamylated tubulin antibodies, but it is not
fragmented by nocodazole treatment; (9) before mitosis, the already elongat
ed Golgi ribbon undergoes progressive medial fission, cisternae by cisterna
e, starting at the cisternae adjacent to the cell surface and ending with t
he cis-most cisternae; (10) the Golgikinesis originates two small Golgi rib
bons; (11) the Golgi is intensely labeled with the antisera to the AP65 and
AP51 adhesins in T. vaginalis, thus seeming to be a key station in the pro
duction of adhesins.