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a
5 μm
b
100
80
60
40
20
0
0
2
4
6
8
10
12
14
16
Distance, μm
Fig. 11.3 Fluorescence confocal microscopy of mitochondria and alpha-actinin distribution in
adult rat cardiomyocyte. (a) Regular distribution of individual mitochondria as visualized by
autofluorescence of flavoproteines (
green color
) in between Z-lines that are labeled with rhoda-
mine immunofluorescent for
α
-actinin (
red color
). (b) Analysis of fluorescence intensity along a
selected line:
dotted
flavoproteins. Note that peaks of green fluorescence
intensity corresponding to mitochondria are seen in the regions of “zero” intensity of red
¼ α
-actinin;
solid
¼
α
-actinin
fluorescence. Reproduced from (Gonzalez-Granillo et al.
2012
) with permission
and dimers, and
II tubulin co-distributes with mitochondria (Saks et al.
2012
;
Gonzalez-Granillo et al.
2012
; Guzun et al.
2011a
,
2012
). These findings are in
agreement with data published first in 1990 by Saetersdal et al. regarding the link
between
β
tubulin and mitochondria as revealed by immunogold labeling
(Saetersdal et al.
1990
). According to this study,
β
tubulin interacts with
mitochondria through the outer membrane (MOM) creating links between the
organelle and other cellular structures. The contribution of other cytoskeletal
proteins to structural and functional interactions with mitochondria is under inten-
sive investigation. Desmin and plectin are capable of interacting with voltage-
dependent anion channel (VDAC) at MOM (Capetanaki et al.
2007
; Capetenaki
2002
; Liobikas et al.
2001
; Schroder et al.
2002
). The 1b isotype of plectin of
cardiomyocytes co-localizes with mitochondria via direct interaction with VDAC,
whereas plectin 1d isotype is specifically associated with sarcomeric Z-disks
(Schroder et al.
2002
).
Recently it has been proposed that the T-tubular system, which represents a
network of tubular extensions from the sarcolemma, plays an important role in the
β
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