scholarly journals The presence and subcellular distribution of sterol carrier protein 2 in embryonic-chick tissues

1993 ◽  
Vol 295 (3) ◽  
pp. 787-792 ◽  
Author(s):  
M P Reinhart ◽  
S J Avart ◽  
T O Dobson ◽  
T A Foglia

Transport of lipids from the yolk to the tissues of the chick embryo is slow during the first 2 weeks of development, but increases abruptly during the last week. Evidence suggests that the lipid traverses the cytoplasm of the yolk-sac membrane before secretion as lipoprotein into the fetal circulation. Little is known about the cytoplasmic transport of lipid in avian systems, but recently the presence of sterol carrier protein 2 (SCP2) was reported in chicken liver. Here we examine the cells of yolk-sac membrane, liver and small intestine for the presence of this protein as a function of the time of embryonic development. The quantity of SCP2 present in the embryonic cells did not appear to correlate with the rate of lipid flux in these tissues. The abrupt appearance of a high-molecular-mass form of SCP2 was detected in small intestine shortly before hatching, but the significance of this protein is not clear. The presence of SCP2 in these tissues was also confirmed by immunocytochemical techniques. Similarly to SCP2 of mammalian cells, avian SCP2 is localized in both peroxisome-like structures and mitochondria. To a lesser extent it is associated with the endoplasmic reticulum.

2009 ◽  
Vol 20 (2) ◽  
pp. 658-672 ◽  
Author(s):  
Bao Lige ◽  
Bamini Jayabalasingham ◽  
Hui Zhang ◽  
Marc Pypaert ◽  
Isabelle Coppens

The inability to synthesize cholesterol is universal among protozoa. The intracellular pathogen Toxoplasma depends on host lipoprotein-derived cholesterol to replicate in mammalian cells. Mechanisms of cholesterol trafficking in this parasite must be important for delivery to proper organelles. We characterized a unique d-bifunctional protein variant expressed by Toxoplasma consisting of one N-terminal d-3-hydroxyacyl-CoA dehydrogenase domain fused to two tandem sterol carrier protein-2 (SCP-2) domains. This multidomain protein undergoes multiple cleavage steps to release free SCP-2. The most C-terminal SCP-2 carries a PTS1 that directs the protein to vesicles before processing. Abrogation of this signal results in SCP-2 accumulation in the cytoplasm. Cholesterol specifically binds to parasite SCP-2 but with 10-fold lower affinity than phosphatidylcholine. In mammalian cells and Toxoplasma, the two parasite SCP-2 domains promote the circulation of various lipids between organelles and to the surface. Compared with wild-type parasites, TgHAD-2SCP-2–transfected parasites replicate faster and show enhanced uptake of cholesterol and oleate, which are incorporated into neutral lipids that accumulate at the basal end of Toxoplasma. This work provides the first evidence that the lipid transfer capability of an ancestral eukaryotic SCP-2 domain can influence the lipid metabolism of an intracellular pathogen to promote its multiplication in mammalian cells.


2010 ◽  
Vol 47 (2) ◽  
pp. 249-257 ◽  
Author(s):  
Ryan T. Larson ◽  
Jeffrey M. Lorch ◽  
Julia W. Pridgeon ◽  
James J. Becnel ◽  
Gary G. Clark ◽  
...  

2000 ◽  
Vol 119 (6) ◽  
pp. 1708-1719 ◽  
Author(s):  
Silvana Zanlungo ◽  
Ludwig Amigo ◽  
Hegaly Mendoza ◽  
Juan Francisco Miquel ◽  
Carlos Vío ◽  
...  

1991 ◽  
Vol 10 (8) ◽  
pp. 559-569 ◽  
Author(s):  
ZHIGANG HE ◽  
RITSU YAMAMOTO ◽  
EMMA E. FURTH ◽  
LAURA J. SCHANTZ ◽  
SUSAN L. NAYLOR ◽  
...  

2004 ◽  
Vol 279 (51) ◽  
pp. 53544-53553 ◽  
Author(s):  
Johan Edqvist ◽  
Elin Rönnberg ◽  
Sara Rosenquist ◽  
Kristina Blomqvist ◽  
Lenita Viitanen ◽  
...  

1989 ◽  
pp. 415-420
Author(s):  
A. Steinschneider ◽  
M. P. McLean ◽  
J. T. Billheimer ◽  
H. C. Palfrey ◽  
G. Gibori

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