Evidence for increased myofibrillar mobility in desmin-null mouse skeletal muscle.

نویسندگان

  • Sameer B Shah
  • Fong-Chin Su
  • Kimberly Jordan
  • Derek J Milner
  • Jan Fridén
  • Yassemi Capetanaki
  • Richard L Lieber
چکیده

Quantitative electron microscopy was used to characterize the longitudinal mobility of myofibrils during muscle extension to investigate the functional roles of skeletal muscle intermediate filaments. Extensor digitorum longus fifth toe muscles from wild-type (+/+) and desmin-null (des -/-) animals were passively stretched to varying lengths, and the horizontal displacement of adjacent Z-disks in neighboring myofibrils (Deltax(myo)) and average sarcomere length (SL) were calculated. At short SL (<2.20 microm), wild-type and desmin-null Deltax(myo) were not significantly different, although there was a trend towards greater Z-disk misalignment in muscles from knockout animals (Deltax(myo) 0.34+/-0.04 microm versus 0.22+/-0.09 microm; P>0.2; means +/- S.E.M.). However, at higher SL (>2.90 microm), muscles from knockout animals displayed a dramatically increased Deltax(myo) relative to wild-type muscles (0.49+/-0.10 microm versus 0.25+/-0.07 microm; P<0.05). The results, which establish a maximum extension of the desmin network surrounding the Z-disk, provide what we believe to be the first quantitative estimation of the functional limits of the desmin intermediate filament system in the presence of an intact myofibrillar lattice. The existence of a limit on the extension of desmin suggests a mechanism for the recruitment of desmin into a network of force transmission, whether as a longitudinal load bearer or as a component in a radial force-transmission system.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Structural and functional roles of desmin in mouse skeletal muscle during passive deformation.

Mechanical interactions between desmin and Z-disks, costameres, and nuclei were measured during passive deformation of single muscle cells. Image processing and continuum kinematics were used to quantify the structural connectivity among these structures. Analysis of both wild-type and desmin-null fibers revealed that the costamere protein talin colocalized with the Z-disk protein alpha-actinin...

متن کامل

Reduced myofibrillar connectivity and increased Z-disk width in nebulin-deficient skeletal muscle.

A prominent feature of striated muscle is the regular lateral alignment of adjacent sarcomeres. An important intermyofibrillar linking protein is the intermediate filament protein desmin, and based on biochemical and structural studies in primary cultures of myocytes it has been proposed that desmin interacts with the sarcomeric protein nebulin. Here we tested whether nebulin is part of a novel...

متن کامل

Influences of Desmin and Keratin 19 on Passive Biomechanical Properties of Mouse Skeletal Muscle

In skeletal muscle fibers, forces must be transmitted between the plasma membrane and the intracellular contractile lattice, and within this lattice between adjacent myofibrils. Based on their prevalence, biomechanical properties and localization, desmin and keratin intermediate filaments (IFs) are likely to participate in structural connectivity and force transmission. We examined the passive ...

متن کامل

Quantitative analysis of neonatal skeletal muscle functional improvement in the mouse.

Postnatal skeletal muscle growth is classically attributed to fiber hypertrophy and myogenic differentiation, but these processes do not account for the size-independent increase of muscle mechanical performance that occurs during postnatal growth. There is also little knowledge about the precise time-course of contractile function or the underlying factors that affect it. The present study inv...

متن کامل

Biomechanical characterization of myofibrillar myopathies.

Myofibrillar myopathies (MFMs) are a group of sporadic and hereditary skeletal muscle diseases, which lead to severe physical disability and premature death. Most MFMs are caused by mutations in genes encoding desmin, plectin, VCP, filamin C, BAG3, FHL-1, αB-crystallin, DNAJB6, myotilin, and ZASP. Biomechanical studies on primary human myoblasts carrying desmin and plectin mutations showed incr...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Journal of experimental biology

دوره 205 Pt 3  شماره 

صفحات  -

تاریخ انتشار 2002