Biochemical characterization of the Golgi-complex proteins of Tritrichomonas foetus

Ja, Díaz; W, de Souza

doi:10.1007/s004360050483

Cited by 4 publications

(1 citation statement)

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“…There are very few studies concerning the biochemical properties and functions of this organelle (Benchimol and DeSouza 1985;Queiroz et al 1991;Morgado and DeSouza 1998). Its large size indicates a signi®cant role, probably analogous to that in other cells, that is, acting as an intermediate sorting and processing site for most proteins synthesized in the rough endoplasmic reticulum (ER).…”

Section: Introductionmentioning

confidence: 99%

Ultrastructural localization of glycoconjugates in Tritrichomonas foetus

Benchimol

Bernardino

2002

Parasitol Res

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We have probed Tritrichomonas foetus, a protozoan parasite of the urogenital tract of cattle, with gold-labeled and fluorescent lectins, for the localization of glycoconjugates, at the cell surface and in internal cell compartments. The following lectins were used: Con A, PNA, WGA, BSI, BSII, HPA, WFA, SBA, LFA, HPA, and LCA. Carbohydrates were also localized using the Thiéry's technique. Carbohydrate residues were observed in the Golgi and vesicles with all lectins used. However, the labeling pattern varied among the cisternae. A high heterogeneity of cell labeling was detected in the same preparation. The nucleus and the nuclear envelope were labeled with Con A, WGA, BSI, and UEA I, suggesting the presence of D-Man, and/or D-glucose, L-fucose, and GlcNAc. Lysosomes were labeled with Con A and intensely labeled with HPA. The intensity of labeling of the plasma and flagellar membranes varied according to the lectin used.

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Section: Introductionmentioning

confidence: 99%

Ultrastructural localization of glycoconjugates in Tritrichomonas foetus

Benchimol

Bernardino

2002

Parasitol Res

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New insights on the Golgi complex ofTritrichomonas foetus

et al. 2013

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Tritrichomonas foetus is a protist that causes bovine trichomoniasis and presents a well-developed Golgi. There are very few studies concerning the Golgi in trichomonads. In this work, monoclonal antibodies were raised against Golgi of T. foetus and used as a tool on morphologic and biochemical studies of this organelle. Among the antibodies produced, one was named mAb anti-Golgi 20.3, which recognized specifically the Golgi complex by fluorescence and electron microscopy. By immunoblotting this antibody recognized two proteins with 60 and 66 kDa that were identified as putative beta-tubulin and adenosine triphosphatase, respectively. The mAb 20.3 also recognized the Golgi complex of the Trichomonas vaginalis, a human parasite. In addition, the nucleotide coding sequences of these proteins were identified and included in the T. foetus database, and the 3D structure of the proteins was predicted. In conclusion, this study indicated: (1) adenosine triphosphatase is present in the Golgi, (2) ATPase is conserved between T. foetus and T. vaginalis, (3) there is new information concerning the nucleic acid sequences and protein structures of adenosine triphosphatase and beta-tubulin from T. foetus and (4) the mAb anti-Golgi 20.3 is a good Golgi marker and can be used in future studies.

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