Identification and characterization of rDJL, a novel member of the DnaJ protein family, in rat testis

FEBS Letters ◽  
2005 ◽  
Vol 579 (25) ◽  
pp. 5734-5740 ◽  
Author(s):  
Chunbo Yang ◽  
Shiying Miao ◽  
Shudong Zong ◽  
Samuel S. Koide ◽  
Linfang Wang
Aging ◽  
2019 ◽  
Vol 11 (15) ◽  
pp. 5757-5768 ◽  
Author(s):  
Yifei Liu ◽  
Yu Liang ◽  
Siyi Wang ◽  
Imran Tarique ◽  
Waseem Ali Vistro ◽  
...  

Cell Calcium ◽  
1997 ◽  
Vol 21 (4) ◽  
pp. 311-319 ◽  
Author(s):  
Stephen C. Tovey ◽  
Rita E. Godfrey ◽  
Phillip J. Hughes ◽  
Mokdad Mezna ◽  
Stephen D. Minchin ◽  
...  

1988 ◽  
Vol 79 (2) ◽  
pp. 161-169 ◽  
Author(s):  
Subir K. NagDas ◽  
Shyamali Mukherjee ◽  
Barsanjit Mazumder ◽  
Parimal C. Sen

Parasitology ◽  
2007 ◽  
Vol 135 (1) ◽  
pp. 63-70 ◽  
Author(s):  
H. SAVERWYNS ◽  
A. VISSER ◽  
A. J. NISBET ◽  
I. PEELAERS ◽  
K. GEVAERT ◽  
...  

SUMMARYIt has been shown that the bovine abomasal parasite, Ostertagia ostertagi, drastically modulates its microenvironment, causing epithelial cell damage, accumulation of inflammatory cells and pH changes in the stomach. The mechanisms used by the parasite to change the abomasal environment are largely unknown, but an important role has been attributed to excretory-secretory (ES) products from the parasite. In this study we have identified proteins representing a novel ES protein family, characterized by the SCP/Tpx-1/Ag5/PR-1/Sc7 protein motif. These proteins were named Oo-AL1 and Oo-AL2 (O. ostertagi ASP-like protein). Both proteins contain a signal peptide and 1 predicted N-glycosylation site. The transcript for Oo-AL1 was present from the L4 stage onwards in both male and female adult worms, whereas the Oo-AL2 transcript was hardly detectable. Western blots of somatic extracts and ES products from different developmental stages of O. ostertagi, probed with anti-Oo-AL1 antibodies, revealed Oo-AL proteins in the ES products of adult worms. An analysis of the nematode genome and EST databases indicated that these novel ES proteins are unique to O. ostertagi and its relative, Teladorsagia circumcincta, suggesting a key function in these abomasal parasites.


2005 ◽  
Vol 4 (12) ◽  
pp. 1990-1997 ◽  
Author(s):  
N. de Miguel ◽  
P. C. Echeverria ◽  
S. O. Angel

ABSTRACT The results of this study describe the identification and characterization of the Toxoplasma gondii α-crystallin/small heat shock protein (sHsp) family. By database (www.toxodb.org ) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the previously characterized Hsp30/Bag1) were identified. As expected, they share the homologous α-crystallin domain, which is the key characteristic of sHsps. However, the N-terminal segment of each protein contains unique characteristics in size and sequence. Most T. gondii sHsps are constitutively expressed in tachyzoites and fully differentiated bradyzoites, with the exception of Hsp30/Bag1. Interestingly, by subcellular localization we observed that T. gondii sHsps are located in different compartments. Hsp20 is located at the apical end of the cell, Hsp28 is located inside the mitochondrion, Hsp29 showed a membrane-associated labeling, and Hsp21 appeared throughout the cytosol of the parasites. These particular differences in the immunostaining patterns suggest that their targets and functions might be different.


Sign in / Sign up

Export Citation Format

Share Document