High impact information on Egln3

• Additionally, overexpression of SM-20, under conditions where cell death is blocked by a general caspase inhibitor, did not result in widespread release of cytochrome c from mitochondria [1].
• An amino-terminal truncated form of SM-20 was not restricted to mitochondria but instead localized throughout the cytosol and nucleus [1].
• Similar results were obtained with the nonfusing mouse C25 myoblast line, suggesting that SM-20 upregulation is a consequence of biochemical differentiation and is fusion independent [2].
• SM-20 is a novel growth factor-responsive gene regulated during skeletal muscle development and differentiation [2].
• Differentiation by serum withdrawal was associated with a marked induction of SM-20 mRNA and the expression of high levels of SM-20 antigen in myotubes [2].

Biological context of Egln3

• We have now examined SM-20 expression during differentiation of cultured skeletal myoblasts and during skeletal myogenesis in vivo [2].
• SM-20 is a novel, evolutionarily conserved "early response" gene originally cloned from a rat aortic smooth muscle cell (SMC) cDNA library [2].
• During mouse embryogenesis, SM-20 was first observed at 8.5E in the dermomyotomal cells of the rostral somites [2].
• These results indicate that SM-20 is a novel mitochondrial protein that may be an important mediator of neurotrophin-withdrawal-mediated cell death [1].

Anatomical context of Egln3

• Low levels of SM-20 mRNA and protein were expressed in proliferating mouse C2C12 myoblasts [2].
• The rat orthologue of EGLN3 (SM-20) exhibits tissue-restricted expression, is induced by growth factors in cultured vascular smooth muscle, and is up-regulated during myogenesis [3].

Associations of Egln3 with chemical compounds

• SM-20 encodes a cytoplasmic protein, which is induced by platelet-derived growth factor and angiotensin II in cultured SMC and is upregulated in intimal SMC of atherosclerotic plaques and injured arteries [2].

Analytical, diagnostic and therapeutic context of Egln3

• SM-20 immunofluorescence was present in the cytoplasm in a punctate pattern that colocalized with cytochrome oxidase I and with mitochondria-selective dyes [1].

References