scholarly journals Isolation and Characterization of Type I Signal Peptidase of Different Malaria Parasites

2005 ◽  
Vol 2005 (4) ◽  
pp. 301-309 ◽  
Author(s):  
Sutikshan Sharma ◽  
Arun Pradhan ◽  
Virander S. Chauhan ◽  
Renu Tuteja
2018 ◽  
Vol 21 (05) ◽  
pp. 829-840
Author(s):  
Hamid Mahmood ◽  
Nasir Zulfiqar ◽  
Ghazia Irfan ◽  
Hashim Riaz ◽  
Ammara Waqar ◽  
...  

Introduction: The two HCV envelope glycoproteins E1 and E2 are released fromHCV polyprotein by signal peptidase cleavages. These glycoproteins are type I transmembraneproteins with a highly glycosylated N-terminal ectodomain and a C-terminal hydrophobicanchor. Methods and pathways: After their synthesis, HCV glycoproteins E1 and E2 associateas a non covalent heterodimer. The transmembrane domains of HCV envelope glycoproteinsplay a major role in E1–E2 heterodimer assembly and subcellular localization. The envelopeglycoprotein complex E1–E2 has been proposed to be essential for HCV entry. Results andconclusions: However, for a long time, HCV entry studies have been limited by the lack of arobust cell culture system for HCV replication and viral particle production. Recently, a modelmimicking the entry process of HCV lifecycle has been developed by pseudo typing retroviralparticles with native HCV envelope glycoproteins, allowing the characterization of functionalE1–E2 envelope glycoproteins., we review our understanding to date on the assembly of thefunctional HCV glycoprotein heterodimer.


1980 ◽  
Vol 8 (8) ◽  
pp. 1823-1837 ◽  
Author(s):  
G. Vogeli ◽  
E.V. Avvedimento ◽  
M. Sullivan ◽  
J.V. Maizel ◽  
G. Lozano ◽  
...  

2012 ◽  
Vol 23 (7) ◽  
pp. 1729-1738 ◽  
Author(s):  
Anguchamy Veeruraj ◽  
Muthuvel Arumugam ◽  
Thangappan Ajithkumar ◽  
Thangavel Balasubramanian

FEBS Journal ◽  
2011 ◽  
Vol 278 (19) ◽  
pp. 3699-3710 ◽  
Author(s):  
Rod S. Hobbs ◽  
Margaret A. Shears ◽  
Laurie A. Graham ◽  
Peter L. Davies ◽  
Garth. L. Fletcher

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Uttio Roy Chowdhury ◽  
Cindy K. Bahler ◽  
Cheryl R. Hann ◽  
Bradley H. Holman ◽  
Michael P. Fautsch

AbstractOcular hypertension occurs due to increased resistance to aqueous humor removal through the conventional outflow pathway. Unlike the proximal region of the conventional outflow pathway, the distal region has not been well studied, mostly due to lack of model systems. Here we describe isolation and characterization of human primary vascular distal outflow pathway (VDOP) cells from the distal region of the conventional outflow pathway. Tissue from the distal region was isolated from human corneo-scleral rims, digested with collagenase type I (100 U/ml) and placed on gelatin coated plates to allow cellular growth in Dulbecco’s Modified Eagle’s Medium (low glucose) containing fetal bovine serum and antibiotic/antimycotic. VDOP cells showed consistent proliferation for up to 7 passages, retained endothelial-like nature of the parent tissues and showed a unique marker phenotype of Lectin+VEGFR2-CD34-NG2- that was distinct from neighboring trabecular meshwork (Lectin+VEGFR2-CD34-NG2+) and Schlemm’s canal (Lectin+VEGFR2+CD34+NG2+) cells. Dexamethasone treated VDOP cells did not express myocilin and did not form cross-linked actin networks, in contrast to trabecular meshwork cells. These data show that VDOP cells are unique to the distal outflow region and can be used as a viable in vitro model system to understand the biology of the distal outflow pathway and intraocular pressure regulation.


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