RGD Reference Report - Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus. - Rat Genome Database

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Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus.

Authors: Bozzo, C  Stevens, L  Toniolo, L  Mounier, Y  Reggiani, C 
Citation: Bozzo C, etal., Am J Physiol Cell Physiol. 2003 Sep;285(3):C575-83. Epub 2003 May 14.
RGD ID: 1580242
Pubmed: PMID:12748068   (View Abstract at PubMed)
DOI: DOI:10.1152/ajpcell.00441.2002   (Journal Full-text)

In striated muscles myosin light chain (MLC)2 phosphorylation regulates calcium sensitivity and mediates sarcomere organization. Little is known about the changes in MLC2 phosphorylation in relation to skeletal muscle plasticity. We studied changes in MLC2 phosphorylation in rats receiving three treatment conditions causing slow-to-fast transitions: 1) atrophy induced by 14 days of hindlimb suspension (HS), 2) hypertrophy induced by 14 days of clenbuterol administration (CB), and 3) 14 days of combined treatment (CB-HS). Three variants of the slow (MLC2s) and two variants of the fast MLC2 (MLC2f) isoform were separated with two-dimensional electrophoresis and identified with monoclonal and polyclonal antibodies specific for MLC2; their relative proportions were densitometrically quantified. In control soleus muscle MLC2s predominated over MLC2f (91.4 +/- 3.9% vs. 8.5 +/- 3.9%) and was separated into two spots, the less acidic spot being 73.5 +/- 4.3% of the total. All treatments caused a decrease of the less acidic unphosphorylated spot of MLC2s (CB: 64.1 +/- 5.6%, HS: 62.4 +/- 6.8%, CB-HS: 56.4 +/- 4.4%), the appearance of a third more acidic variant of MLC2s (representing 3.9-5.9% of total MLC2s), an increase of MLC2f (CB: 30.9 +/- 3.1%, HS: 23.9 +/- 3.3%, CB-HS: 25.3 +/- 3.9%), and the phosphorylation of a large fraction of MLC2f (CB: 30.4 +/- 6.7%, HS: 28.7 +/- 6.5%, CB-HS: 21.8 +/- 2.1%). Treatment with alkaline phosphatase or with protein phosphatase 1 (PP1) removed the most acidic spots of both MLC2f and MLC2s. We conclude that in rat skeletal muscles an increase of MLC2 phosphorylation is associated with the slow-to-fast transition regardless of whether hypertrophy or atrophy develops.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Mylk2Ratpeptidyl-serine phosphorylation  TAS  RGD 
Mylk2Ratpositive regulation of fast-twitch skeletal muscle fiber contraction  IMP  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Mylk2  (myosin light chain kinase 2)


Additional Information