scholarly journals High Expression and Purification of Amino-Terminal Fragment of Human Amyloid Precursor Protein inPichia pastorisand Partial Analysis of Its Properties

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Wei Li ◽  
Xiang Gao ◽  
Junle Ren ◽  
Ting An ◽  
Yan Liu
Keyword(s):  
Amyloid Precursor Protein ◽  
Expression System ◽  
Precursor Protein ◽  
High Yield ◽  
Human Neuroblastoma ◽  
Amino Terminal ◽  
Mammalian Expression ◽  
Terminal Fragment ◽  
Mammalian Expression System ◽  
Amino Terminal Fragment

The cleaved amino-terminal fragment of human amyloid precursor protein (N-APP) binds death receptor 6 (DR6) and triggers a caspase-dependent self-destruction process, which was suggested to contribute to Alzheimer’s disease. To investigate the N-APP-DR6-induced degeneration pathway at the molecular level, obtaining abundant and purified N-APP is fundamental and critical. The recombinant N-APP has been produced in mammalian expression system. However, the cost and yield disadvantages of mammalian expression system make it less ideal for protein mass production. Here, we successfully expressed and purified recombinant N-terminal 18-285 amino acid residues of human amyloid precursor protein from the methylotrophic yeastPichia pastoriswith a high yield of 50 mg/L. Flow cytometry indicated the purified N-APP-induced obvious apoptosis of human neuroblastoma SHEP cells.

Identification of a novel amino-terminal fragment of amyloid precursor protein in mouse neuroblastoma Neuro2a cell

2003 ◽  
Vol 353 (2) ◽  
pp. 135-138 ◽  
Author(s):  
Masataka Hoshino ◽  
Naoshi Dohmae ◽  
Koji Takio ◽  
Ichiro Kanazawa ◽  
Nobuyuki Nukina
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Neuro2a Cell ◽  
Amino Terminal ◽  
Mouse Neuroblastoma ◽  
Terminal Fragment ◽  
Amino Terminal Fragment

scholarly journals Evolution of the hedgehog Gene Family

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 965-972 ◽  
Author(s):  
Sudhir Kumar ◽  
Kristi A Balczarek ◽  
Zhi-Chun Lai
Keyword(s):  
Intercellular Communication ◽  
Short Range ◽  
Gene Duplications ◽  
Future Directions ◽  
Amino Terminal ◽  
Terminal Fragment ◽  
Carboxyl Terminal ◽  
Multicellular Organisms ◽  
Amino Terminal Fragment

Abstract Effective intercellular communication is an important feature in the development of multicellular organisms. Secreted hedgehog (hh) protein is essential for both long- and short-range cellular signaling required for body pattern formation in animals. In a molecular evolutionary study, we find that the vertebrate homologs of the Drosophila hh gene arose by two gene duplications: the first gave rise to Desert hh, whereas the second produced the Indian and Sonic hh genes. Both duplications occurred before the emergence of vertebrates and probably before the evolution of chordates. The amino-terminal fragment of the hh precursor, crucial in long- and short-range intercellular communication, evolves two to four times slower than the carboxyl-terminal fragment in both Drosophila hh and its vertebrate homologues, suggesting conservation of mechanism of hh action in animals. A majority of amino acid substitutions in the amino- and carboxyl-terminal fragments are conservative, but the carboxyl-terminal domain has undergone extensive insertion-deletion events while maintaining its autocleavage protease activity. Our results point to similarity of evolutionary constraints among sites of Drosophila and vertebrate hh homologs and suggest some future directions for understanding the role of hh genes in the evolution of developmental complexity in animals.

The amino‐terminal fragment of human urokinase directs a recombinant chimeric toxin to target cells: internalization is toxin mediated

1997 ◽  
Vol 11 (13) ◽  
pp. 1169-1176 ◽  
Author(s):  
M. Serena Fabbrini ◽  
Daniela Carpani ◽  
Iraldo Bello‐Rivero ◽  
Marco R. Soria
Keyword(s):  
Target Cells ◽  
Amino Terminal ◽  
Terminal Fragment ◽  
Amino Terminal Fragment
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