Certain mutations in the dystrophin gene disrupt the reading
frame, leading to little or no dystrophin production and the severe clinical
features seen in Duchenne muscular dystrophy (DMD). However, when the reading
frame is preserved—even if parts of the protein are missing—muscle function is
partially maintained, as observed in Becker muscular dystrophy.

How do antisense oligonucleotide therapies exploit this
difference to improve outcomes in patients with DMD?

Question

Certain mutations in the dystrophin gene disrupt the reading
frame, leading to little or no dystrophin production and the severe clinical
features seen in Duchenne muscular dystrophy (DMD). However, when the reading
frame is preserved—even if parts of the protein are missing—muscle function is
partially maintained, as observed in Becker muscular dystrophy.

How do antisense oligonucleotide therapies exploit this
difference to improve outcomes in patients with DMD?

Accepted Answer

By
modifying pre-mRNA splicing to bypass the mutated exon and re-establish the
correct reading frame

Answer

By
selectively degrading mutant dystrophin mRNA via RNase H activation

Answer

By
inhibiting translation of dystrophin mRNA to prevent accumulation of
dysfunctional protein

Answer

By
upregulating dystrophin transcription to offset loss of protein function

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Certain mutations in the dystrophin gene disrupt the reading frame, leading to ...

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