S100a<sub>0</sub> (αα) Protein: Distribution in Muscle Tissues of Various Animals and Purification from Human Pectoral Muscle

Kato, Kanefusa; Kimura, Shigeki; Haimoto, Hajime; Suzuki, Fujiko

doi:10.1111/j.1471-4159.1986.tb01776.x

Cited by 67 publications

(37 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…While the immunoreactive levels of SlOOa which we detected in heart (21.5 ng/mg total protein) were almost identical with the 24.1 ? 4 ng/mg total protein previously reported by Zimmer and Van Eldik [ 19871, they were approximately half the 99.1 i 19.1 ng/mg total protein reported by Kato et al [1986]. The reasons for the 2-fold difference in immunoreactive S 1 OOa levels in heart may reflect differences in the strain or age of the animals, sample preparation techniques, or assay procedures.…”

Section: Discussionmentioning

confidence: 66%

Examination of the calcium‐modulated protein S100α and its target proteins in adult and developing skeletal muscle

Zimmer

1991

Cell Motil. Cytoskeleton

View full text Add to dashboard Cite

In this study radioimmunoassay, immunohistochemistry, Northern blot analysis, and a gel overlay technique have been used to examine the level, subcellular distribution, and potential target proteins of the S100 family of calcium‐modulated proteins in adult and developing rat skeletal muscles. Adult rat muscles contained high levels of S100 proteins but the particular form present was dependent on the muscle type: cardiac muscle contained exclusively S100α, slow‐twitch skeletal muscle fibers contained predominantly S100α, vascular smooth muscle contained both S100α and S100β, and fast‐twitch skeletal muscle fibers contained low but detectable levels of S100α and S100β. While the distribution of S100 mRNAs paralled the protein distribution in all muscles there was no direct correlation between the mRNA and protein levels in different muscle types, suggesting that S100 protein expression is differentially regulated in different muscle types. Immunohistochemical analysis of the cellular distribution of S100 proteins in adult skeletal muscles revealed that S100α staining was associated with muscle cells, while S100β staining was associated with nonmuscle cells. Radioimmunoassays of developing rat skeletal muscles demonstrated that all developing muscles contained low levels of S100α at postnatal day 1 and that as development proceeded the S100α levels increased. In contrast to adult muscle, S100α expression as confined to fast‐twitch fibers in developing skeletal muscle until postnatal day 21. At postnatal day 1, developing contractile elements were S100α positive, but no staining periodicity was detectable. At postnatal day 21, S100α exhibited the same subcellular localization as seen in the adult: colocalization with the A‐band and/or longitudinal sarcoplasmic reticulum. Comparison of the S100α‐binding protein profiles in fast‐ and slow‐twitch fibers of various species revealed few, if any, species‐ or fiber type‐specific S100 binding proteins. Isolated sarcoplasmic reticulum fractions and myo fibrils contained multiple S100α‐hinding proteins. The colocalization of S100α and S100α‐binding proteins with the contractile apparatus and sarcoplasmic reticulum suggest that S100α may regulate excitation and/or contraction in slow‐twitch fibers.

show abstract

Section: Discussionmentioning

confidence: 66%

Examination of the calcium‐modulated protein S100α and its target proteins in adult and developing skeletal muscle

Zimmer

1991

Cell Motil. Cytoskeleton

View full text Add to dashboard Cite

show abstract

“…This is consistent with previous experiments showing that both Ca'+ -binding pro- teins bind to the same site in the autoinhibitory sequence [8,201, and further indicates that the affinity of twitchin for CaM is rather low in solution. This experiment also indicates that the regulation of specifically Ca2 ' /S 100-dependent enzymes should hardly be impaired by Ca'+/CaM in tissues such as cardiac or skeletal muscle, where the SlOOAl protein is present at similarly high concentrations as CaM [23]. Likewise, as SlOO proteins are typically expressed in a highly tissue-specific manner IS, 61, there should be little competition between different isoforms.…”

Section: Impact Of Modular Domains On the Sloo/twitchin Kinase Interamentioning

confidence: 89%

Interaction of the Recombinant S100A1 Protein with Twitchin Kinase, and Comparison with Other Ca²⁺‐Binding Proteins

Heierhorst

Mann

Kemp

1997

European Journal of Biochemistry

View full text Add to dashboard Cite

The giant myosin-associated twitchin kinase, a member of the Ca'+-regulated protein kinase superfamily, is activated by the EF-hand protein SlOOAl in a Ca2+-dependent and Zn'+-enhanced manner. We used recombinant SlOOAl to further characterize the interaction between the two proteins. ZnZ' enhanced the binding of CaZ+/SIOOA1 to twitchin kinase fragments (K, < SO nM) in assays using a BIAcore biosensor by reducing the SlOOAl off rate. Other Ca2+-binding proteins (SlOOA6, calmodulin, and the calmodulin-like domain of Ca2+-dependent protein kinase a) bound to the kinase but did not activate it. These results indicate that binding of Ca2+-binding proteins alone is insufficient to trigger the intramolecular rearrangement of kinase autoinhibitory contacts required for twitchin kinase activation that is specifically elicited by the SlOOAl protein. Kinase fragments that contained only the autoinhibited catalytic sequence or an additional immunoglobulin-like domain had very similar properties, indicating that the tethered immunoglobulin-like domain does not modulate kinase regulation.Keywords: protein kinase; twitchin ; titin; ,5100; calmodulin.Intracellular second messenger functions of calcium ions are mediated by specific calcium-binding proteins [I]. Members of a large protein superfamily bind calcium via the helix-loop-helix EF-hand motif (21. Calmodulin (CaM), the most thoroughly characterized EF-hand protein, associates with its effector enzymes (such as CaM-dependent protein kinases, the phosphatase calcineurin or phosphodiesterase) and regulates their activity upon calcium binding [3, 41. Members of the subfamily of S100-like EF-hand proteins are encoded by at least 16 different genes, most of them clustered on human chromosome lq21 [S, 61. The SlOO family differs from CaM in two important aspects. First, in contrast to CaM that is monomeric and contains four EF-hands/molecule, S100 proteins have only two EF-hands/= 100 amino-acid-residue subunit, but are dimeric; second, while CaM is ubiquitously expressed, S 100 proteins are generally expressed in a tissue-specific and often developmentally regulated manner [5, 61. Some SlOO proteins are reported to have extracellular functions as neurotrophic (e.g. SlOOS) or chemotactic factors (e.g. SIOOAS, SlOOA9), whereas others act intracellularly either as Ca' ' buffer/transport proteins ( e g calbindin) or, similarly to CaM, as proposed trigger proteins that associate with effector proteins to transduce intracellular Ca'+ signals [5, 61.The current understanding of the effector functions of SlOO proteins is limited by the fact that only few targets have been identified. Furthermore, even fewer of the targets are effector enzymes whose activity is significantly regulated by Ca2+/S100 proteins [S-7]. So far, the enzyme most dramatically affected by an S100-like protein is the myosin-associated giant protein kinase twitchin [S], a member of the myosin light-chain kinase family. CaZ+/SlOOA1, but not Ca2+/CaM, stimulates the twitchin kinase V,,, by more than 1000-fold [...

show abstract

“…S100A1 protein is preferentially abundant in the heart, although the protein is also found in lower amounts in skeletal muscle, brain, and kidney (10,12,13,16,46). In the heart, S100A1 is the predominant cardiac S100 protein among other S100 isoforms such as S100A4, S100A6, and S100B and is mainly found in ventricular cardiomyocyes.…”

Section: S100a1: Expression Pattern Subcellular Location and Molecumentioning

confidence: 99%

S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance

Most¹,

Remppis²,

Pleger³

et al. 2007

American Journal of Physiology-Regulatory, Integrative and Comp

View full text Add to dashboard Cite

Most P, Remppis A, Pleger ST, Katus HA, Koch WJ. S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance. Am J Physiol Regul Integr Comp Physiol 293: R568-R577, 2007. First published April 25, 2007 doi:10.1152/ajpregu.00075.2007.-Here we review the considerable body of evidence that has accumulated to support the notion of S100A1, a cardiac-specific Ca 2ϩ -sensor protein of the EF-hand type, as a physiological regulator of excitation-contraction coupling and inotropic reserve mechanisms in the mammalian heart. In particular, molecular mechanisms will be discussed conveying the Ca 2ϩ -dependent inotropic actions of S100A1 protein in cardiomyocytes occurring independently of ␤-adrenergic signaling. Moreover, we will shed light on the molecular structure-function relationship of S100A1 with its cardiac target proteins at the sarcoplasmic reticulum, the sarcomere, and the mitochondria. Furthermore, pathophysiological consequences of disturbed S100A1 protein expression on altered Ca 2ϩ handling and intertwined systems in failing myocardium will be highlighted. Subsequently, therapeutic options by means of genetic manipulation of cardiac S100A1 expression will be discussed, aiming to complete our current understanding of the role of S100A1 in diseased myocardium. excitation-contraction coupling; cardiomyocyte; heart failure; gene therapy , WE PUBLISHED A STUDY (21) showing that elevated levels of the Ca 2ϩ -binding protein S100A1 in myocardium exert profound inotropic actions through modulation of cardiomyocyte Ca 2ϩ homeostasis and myofilament function. This was by no means the first study to demonstrate the potent effects of the Ca 2ϩ sensor on cardiac performance. Due to its altered expression in diseased myocardium (31), clinical interest immediately sparked in its pathophysiological relevance and therapeutic potential. After identification of S100A1 as the predominant cardiac S100 protein isoform among normal human tissues, Remppis et al. (31) were the first to describe altered expression of S100A1 in failing human myocardium. Since then, large efforts have been undertaken to elucidate the role of S100A1 in cardiovascular biology and its contribution to cardiovascular disease. In this review, we focus on concepts supporting a physiological role for S100A1 in the regulation of cardiac excitation-contraction (EC) coupling and inotropic reserve mechanisms. Moreover, pathophysiological consequences of altered S100A1 expression in cardiovascular disease and therapeutic options by the means of genetic manipulation of S100A1 expression will be highlighted, aiming to complete our current understanding of the role of S100A1 in diseased myocardium.

show abstract

S100a₀ (αα) Protein: Distribution in Muscle Tissues of Various Animals and Purification from Human Pectoral Muscle

Cited by 67 publications

References 17 publications

Examination of the calcium‐modulated protein S100α and its target proteins in adult and developing skeletal muscle

Examination of the calcium‐modulated protein S100α and its target proteins in adult and developing skeletal muscle

Interaction of the Recombinant S100A1 Protein with Twitchin Kinase, and Comparison with Other Ca²⁺‐Binding Proteins

S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance

Contact Info

Product

Resources

About

S100a0 (αα) Protein: Distribution in Muscle Tissues of Various Animals and Purification from Human Pectoral Muscle

Cited by 67 publications

References 17 publications

Examination of the calcium‐modulated protein S100α and its target proteins in adult and developing skeletal muscle

Examination of the calcium‐modulated protein S100α and its target proteins in adult and developing skeletal muscle

Interaction of the Recombinant S100A1 Protein with Twitchin Kinase, and Comparison with Other Ca2+‐Binding Proteins

S100A1: a novel inotropic regulator of cardiac performance. Transition from molecular physiology to pathophysiological relevance

Contact Info

Product

Resources

About

S100a₀ (αα) Protein: Distribution in Muscle Tissues of Various Animals and Purification from Human Pectoral Muscle

Interaction of the Recombinant S100A1 Protein with Twitchin Kinase, and Comparison with Other Ca²⁺‐Binding Proteins