Linked Life Data

12721284

Source:http://linkedlifedata.com/resource/pubmed/id/12721284

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
2003-7-14
pubmed:abstractText
S100A1, a Ca2+-binding protein of the EF-hand type, is most highly expressed in striated muscle and has previously been shown to interact with the skeletal muscle sarcoplasmic reticulum (SR) Ca2+ release channel/ryanodine receptor (RyR1) isoform. However, it was unclear whether S100A1/RyR1 interaction could modulate SR Ca2+ handling and contractile properties in skeletal muscle fibers. Since S100A1 protein is differentially expressed in fast- and slow-twitch skeletal muscle, we used saponin-skinned murine Musculus extensor digitorum longus (EDL) and Musculus soleus (Soleus) fibers to assess the impact of S100A1 protein on SR Ca2+ release and isometric twitch force in functionally intact permeabilized muscle fibers. S100A1 equally enhanced caffeine-induced SR Ca2+ release and Ca2+-induced isometric force transients in both muscle preparations in a dose-dependent manner. Introducing a synthetic S100A1 peptide model (devoid of EF-hand Ca2+-binding sites) allowed identification of the S100A1 C terminus (amino acids 75-94) and hinge region (amino acids 42-54) to differentially enhance SR Ca2+ release with a nearly 3-fold higher activity of the C terminus. These effects were exclusively based on enhanced SR Ca2+ release as S100A1 influenced neither SR Ca2+ uptake nor myofilament Ca2+ sensitivity/cooperativity in our experimental setting. In conclusion, our study shows for the first time that S100A1 augments contractile performance both of fast- and slow-twitch skeletal muscle fibers based on enhanced SR Ca2+ efflux at least mediated by the C terminus of S100A1 protein. Thus, our data suggest that S100A1 may serve as an endogenous enhancer of SR Ca2+ release and might therefore be of physiological relevance in the process of excitation-contraction coupling in skeletal muscle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26356-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12721284-Amino Acid Sequence, pubmed-meshheading:12721284-Animals, pubmed-meshheading:12721284-Caffeine, pubmed-meshheading:12721284-Calcium Signaling, pubmed-meshheading:12721284-Calcium-Binding Proteins, pubmed-meshheading:12721284-Humans, pubmed-meshheading:12721284-Isometric Contraction, pubmed-meshheading:12721284-Male, pubmed-meshheading:12721284-Mice, pubmed-meshheading:12721284-Mice, Inbred BALB C, pubmed-meshheading:12721284-Molecular Sequence Data, pubmed-meshheading:12721284-Muscle, Skeletal, pubmed-meshheading:12721284-Muscle Fibers, Fast-Twitch, pubmed-meshheading:12721284-Muscle Fibers, Slow-Twitch, pubmed-meshheading:12721284-Peptide Fragments, pubmed-meshheading:12721284-Recombinant Proteins, pubmed-meshheading:12721284-Ryanodine Receptor Calcium Release Channel, pubmed-meshheading:12721284-S100 Proteins, pubmed-meshheading:12721284-Sarcoplasmic Reticulum
pubmed:year
2003
pubmed:articleTitle
The C terminus (amino acids 75-94) and the linker region (amino acids 42-54) of the Ca2+-binding protein S100A1 differentially enhance sarcoplasmic Ca2+ release in murine skinned skeletal muscle fibers.
pubmed:affiliation
Abteilung Innere Medizin III (Kardiologie), Universität Heidelberg, 69115 Heidelberg, Germany.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't