Serine Proteases

Publication Title: 
Nature

The lengths of human telomeres, which protect chromosome ends from degradation and end fusions, are crucial determinants of cell lifespan. During embryogenesis and in cancer, the telomerase enzyme counteracts telomeric DNA shortening. As shown in cancer cells, human telomerase binds the shelterin component TPP1 at telomeres during the S phase of the cell cycle, and adds ~60 nucleotides in a single round of extension, after which telomerase is turned off by unknown mechanisms.

Author(s): 
Chen, Liuh-Yow
Redon, Sophie
Lingner, Joachim
Publication Title: 
Nature

The lengths of human telomeres, which protect chromosome ends from degradation and end fusions, are crucial determinants of cell lifespan. During embryogenesis and in cancer, the telomerase enzyme counteracts telomeric DNA shortening. As shown in cancer cells, human telomerase binds the shelterin component TPP1 at telomeres during the S phase of the cell cycle, and adds ~60 nucleotides in a single round of extension, after which telomerase is turned off by unknown mechanisms.

Author(s): 
Chen, Liuh-Yow
Redon, Sophie
Lingner, Joachim
Publication Title: 
International Journal of Obesity (2005)

BACKGROUND: Maternal genotype has lifetime effects on progeny, but few specific genes, and no proteases, are known to underlie maternal effects. Prolyl endopeptidase (PREP) is a serine protease with putative substrates that regulate appetite or milk production. OBJECTIVE: To test effects of PREP on obesity phenotypes in mice. DESIGN: Mice with a gene trap (GT) of PREP (PREP(gt/gt)) on the C57BL/6J (B6) background were generated. Minimal PREP protein was detected by western blot.

Author(s): 
Warden, C. H.
Fisler, J. S.
Espinal, G.
Graham, J.
Havel, P. J.
Perroud, B.
Publication Title: 
The Journal of Biological Chemistry

The classical late infantile neuronal ceroid lipofuscinosis (LINCLs) is an autosomal recessive disease, where the defective gene is Cln2, encoding tripeptidyl-peptidase I (TPP1). At the molecular level, LINCL is caused by accumulation of autofluorescent storage materials in neurons and other cell types. Currently, there is no established treatment for this fatal disease. This study reveals a novel use of gemfibrozil and fenofibrate, Food and Drug Administration-approved lipid-lowering drugs, in up-regulating TPP1 in brain cells.

Author(s): 
Ghosh, Arunava
Corbett, Grant T.
Gonzalez, Frank J.
Pahan, Kalipada
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