Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle

2007 ◽  
Vol 293 (1) ◽  
pp. C218-C227 ◽  
Author(s):  
Ilona A. Barash ◽  
Marie-Louise Bang ◽  
Liby Mathew ◽  
Marion L. Greaser ◽  
Ju Chen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Time Course ◽  
Fiber Type ◽  
Biological Response ◽  
Ankyrin Repeat ◽  
Wild Type ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Enhanced Expression ◽  
Torque Loss

The biological response of muscle to eccentric contractions (ECs) results in strengthening and protection from further injury. However, the cellular basis for this response remains unclear. Previous studies identified the muscle ankyrin repeat protein ( MARP) family, consisting of cardiac ankyrin repeat protein ( CARP), ankyrin repeat domain 2/ankyrin repeat protein with PEST and proline-rich region ( Ankrd2/Arpp), and diabetes-associated ankyrin repeat protein ( DARP), as rapidly and specifically upregulated in mice after a single bout of EC. To determine the role of these genes in skeletal muscle, a survey of skeletal muscle structural and functional characteristics was performed on mice lacking all three MARP family members (MKO). There was a slight trend toward MKO muscles having a slower fiber type distribution but no differences in muscle fiber size. Single MKO fibers were less stiff, tended to have longer resting sarcomere lengths, and expressed a longer isoform of titin than their wild-type counterparts, indicating that these proteins may play a role in the passive mechanical behavior of muscle. Finally, MKO mice showed a greater degree of torque loss after a bout of ECs compared with wild-type mice, although they recovered from the injury with the same or even improved time course. This recovery was associated with enhanced expression of the muscle regulatory genes MyoD and muscle LIM protein ( MLP), suggesting that the MARP family may play both important structural and gene regulatory roles in skeletal muscle.

scholarly journals Characterization of muscle ankyrin repeat proteins in human skeletal muscle

2017 ◽  
Vol 313 (3) ◽  
pp. C327-C339 ◽  
Author(s):  
Stefan G. Wette ◽  
Heather K. Smith ◽  
Graham D. Lamb ◽  
Robyn M. Murphy
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Ankyrin Repeat ◽  
Absolute Amount ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Repeat Proteins ◽  
Cardiac Ankyrin Repeat Protein ◽  
Repeat Domain ◽  
Ankyrin Repeat Proteins

Muscle ankyrin repeat proteins (MARPs) are a family of titin-associated, stress-response molecules and putative transducers of stretch-induced signaling in skeletal muscle. In cardiac muscle, cardiac ankyrin repeat protein (CARP) and diabetes-related ankyrin repeat protein (DARP) reportedly redistribute from binding sites on titin to the nucleus following a prolonged stretch. However, it is unclear whether ankyrin repeat domain protein 2 (Ankrd 2) shows comparable stretch-induced redistribution to the nucleus. We measured the following in rested human skeletal muscle: 1) the absolute amount of MARPs and 2) the distribution of Ankrd 2 and DARP in both single fibers and whole muscle preparations. In absolute amounts, Ankrd 2 is the most abundant MARP in human skeletal muscle, there being ~3.1 µmol/kg, much greater than DARP and CARP (~0.11 and ~0.02 µmol/kg, respectively). All DARP was found to be tightly bound at cytoskeletal (or possibly nuclear) sites. In contrast, ~70% of the total Ankrd 2 is freely diffusible in the cytosol [including virtually all of the phosphorylated (p)Ankrd 2-Ser99 form], ~15% is bound to non-nuclear membranes, and ~15% is bound at cytoskeletal sites, likely at the N2A region of titin. These data are not consistent with the proposal that Ankrd 2, per se, or pAnkrd 2-Ser99 mediates stretch-induced signaling in skeletal muscle, dissociating from titin and translocating to the nucleus, because the majority of these forms of Ankrd 2 are already free in the cytosol. It will be necessary to show that the titin-associated Ankrd 2 is modified by stretch in some as-yet-unidentified way, distinct from the diffusible pool, if it is to act as a stretch-sensitive signaling molecule.

Identification of Ankrd2, a Novel Skeletal Muscle Gene Coding for a Stretch-Responsive Ankyrin-Repeat Protein

Genomics ◽  
2000 ◽  
Vol 66 (3) ◽  
pp. 229-241 ◽  
Author(s):  
T.J. Kemp ◽  
T.J. Sadusky ◽  
F. Saltisi ◽  
N. Carey ◽  
J. Moss ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ankyrin Repeat ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Gene Coding ◽  
Muscle Gene

scholarly journals Cardiac ankyrin repeat protein is a marker of skeletal muscle pathological remodelling

FEBS Journal ◽  
2008 ◽  
Vol 276 (3) ◽  
pp. 669-684 ◽  
Author(s):  
Lydie Laure ◽  
Laurence Suel ◽  
Carinne Roudaut ◽  
Nathalie Bourg ◽  
Ahmed Ouali ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ankyrin Repeat ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Cardiac Ankyrin Repeat Protein

Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains

2009 ◽  
Vol 106 (4) ◽  
pp. 1419-1424 ◽  
Author(s):  
Maarit Lehti ◽  
Riikka Kivelä ◽  
Paavo Komi ◽  
Jyrki Komulainen ◽  
Heikki Kainulainen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Human Skeletal Muscle ◽  
Mrna Level ◽  
Ankyrin Repeat ◽  
Mrna Levels ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Jumping Exercise ◽  
Calpain 2

Eccentric exercise induced by electrostimulation increases mRNA expression of titin-complex proteins in rodent skeletal muscle. In this study, mRNA expression of titin, muscle LIM protein (MLP), cardiac ankyrin repeat protein (CARP), ankyrin repeat domain protein 2 (Ankrd2), diabetes-related ankyrin repeat protein (DARP), and calcium-activated proteinases, calpains, were investigated in human skeletal muscle after fatiguing jumping exercise. Fatiguing jumping exercise did not change mRNA expression of titin, DARP, calpain 1, or calpain 3. MLP, Ankrd2 and calpain 2 mRNA levels were increased 2 days postexercise. CARP mRNA level was already elevated 30 min and remained elevated 2 days postexercise. Increased mRNA expression of MLP, CARP, and Ankrd2, observed for the first time in human skeletal muscle, may be part of the signaling activated by physical exercise. The rapid increase in the level of CARP mRNA nominates CARP as one of the first genes to respond to exercise. The increase in the mRNA level of calpain 2 suggests its involvement in myofiber remodeling after strenuous jumping exercise.

scholarly journals Accumulation of Muscle Ankyrin Repeat Protein Transcript Reveals Local Activation of Primary Myotube Endcompartments during Muscle Morphogenesis

1997 ◽  
Vol 139 (5) ◽  
pp. 1231-1242 ◽  
Author(s):  
Anja Baumeister ◽  
Silvia Arber ◽  
Pico Caroni
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Early Response ◽  
Ankyrin Repeat ◽  
Denervated Muscle ◽  
Repeat Protein ◽  
Adult Rat ◽  
Ankyrin Repeat Protein ◽  
Cardiac Ankyrin Repeat Protein ◽  
Thrombospondin 4

The characteristic shapes and positions of each individual body muscle are established during the process of muscle morphogenesis in response to patterning information from the surrounding mesenchyme. Throughout muscle morphogenesis, primary myotubes are arranged in small parallel bundles, each myotube spanning the forming muscles from end to end. This unique arrangement potentially assigns a crucial role to primary myotube end regions for muscle morphogenesis. We have cloned muscle ankyrin repeat protein (MARP) as a gene induced in adult rat skeletal muscle by denervation. MARP is the rodent homologue of human C-193 (Chu, W., D.K. Burns, R.A. Swerick, and D.H. Presky. 1995. J. Biol. Chem. 270:10236–10245) and is identical to rat cardiac ankyrin repeat protein. (Zou, Y., S. Evans, J. Chen, H.-C. Kuo, R.P. Harvey, and K.R. Chien. 1997. Development. 124:793–804). In denervated muscle fibers, MARP transcript accumulated in a unique perisynaptic pattern. MARP was also expressed in large blood vessels and in cardiac muscle, where it was further induced by cardiac hypertrophy. During embryonic development, MARP was expressed in forming skeletal muscle. In situ hybridization analysis in mouse embryos revealed that MARP transcript exclusively accumulates at the end regions of primary myotubes during muscle morphogenesis. This closely coincided with the expression of thrombospondin-4 in adjacent prospective tendon mesenchyme, suggesting that these two compartments may constitute a functional unit involved in muscle morphogenesis. Transfection experiments established that MARP protein accumulates in the nucleus and that the levels of both MARP mRNA and protein are controlled by rapid degradation mechanisms characteristic of regulatory early response genes. The results establish the existence of novel regulatory muscle fiber subcompartments associated with muscle morphogenesis and denervation and suggest that MARP may be a crucial nuclear cofactor in local signaling pathways from prospective tendon mesenchyme to forming muscle and from activated muscle interstitial cells to denervated muscle fibers.

scholarly journals Diabetes-Related Ankyrin Repeat Protein (DARP/Ankrd23) Modifies Glucose Homeostasis by Modulating AMPK Activity in Skeletal Muscle

PLoS ONE ◽  
2015 ◽  
Vol 10 (9) ◽  
pp. e0138624 ◽  
Author(s):  
Yoshiaki Shimoda ◽  
Kiyonari Matsuo ◽  
Youhei Kitamura ◽  
Kazunori Ono ◽  
Tomomi Ueyama ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Homeostasis ◽  
Ankyrin Repeat ◽  
Repeat Protein ◽  
Ankyrin Repeat Protein ◽  
Ampk Activity
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