Transcript Slide 1 - ommbid

Perturbations in desmin filament network formation in cells expressing a recombinant desmin protein harboring a 7-amino-acid deletion found in a patient
with severe generalized myopathy. MCF-7 breast epithelial cells possess an IF network of keratin filaments. Since keratin and desmin do not
copolymerize, they can be used to examine de novo assembly of desmin IFs. Recently, a patient with severe generalized myopathy and Z-band
abnormalities was found to lack the wild-type desmin gene altogether and instead express only a mutant desmin gene encoding a 7-amino-acid residue
deletion within helix 1B.272 Heterozygous carriers within the family showed no overt phenotype. To determine whether this mutation was causative for the
myopathy in the patient, MCF-7 cells were transfected with mammalian expression vectors capable of expressing either (A) wild-type desmin, (B) the 7Source: Disorders of Intermediate Filaments and Their Associated Proteins, The Online Metabolic and Molecular Bases of Inherited Disease
amino-acid deletion mutant of desmin, or (C) a mixture of wild-type and mutant desmin. Forty-eight hours after transfection, cells were fixed and stained
Citation:
Valleand
D, Beaudet
AL, Vogelstein
B, Kinzler
KW, Antonarakis
SE, Ballabio
A, Gibson
K, Mitchell
G. The
Online Metabolic
and Molecular
with antidesmin
antibody,
labeling was
visualized with
a fluorescently
tagged secondary
antibody.
Transfected
cells
are shown.
Note that D7Des
alone
Bases
of
Inherited
Disease;
2014
Available
at:
http://mhmedical.com/
Accessed:
April
01,
2017
cannot form a proper IF network and instead produces punctate labeling at the cell periphery. In contrast, wt Des and a mixture of wt Des and D7Des
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assemble into
a filamentous
Bar represents
(From
Munoz-Marmol et al.272 Used with permission from the Proceedings of the National
Academy of Sciences.)