Annexin V, annexin VI, S100A1 and S100B in developing and adult avian skeletal muscles

Department of Experimental Medicine and Biochemical Sciences, Section of Anatomy, University of Perugia, Via del Giochetto, C.P. 81 Succ. 3, 06122 Perugia, Italy.
Neuroscience (Impact Factor: 3.33). 02/2002; 109(2):371-88. DOI: 10.1016/S0306-4522(01)00330-X
Source: PubMed

ABSTRACT Annexins and S100 proteins constitute two multigenic families of Ca2+-modulated proteins that have been implicated in the regulation of both intracellular and extracellular activities. Some annexins can interact with certain S100 protein dimers thereby forming heterotetramers in which an S100 dimer crosslinks two copies of the partner annexin. It is suggested that S100 protein binding to an annexin might serve the function of regulating annexin function and annexin binding to an S100 protein might regulate S100 function. In the present study, annexin V, annexin VI (or ANXA5 and ANXA6, respectively, according to a novel nomenclature), S100A1 and S100B were analyzed for their subcellular localization in developing and adult avian skeletal muscles by confocal laser scanning microscopy, immunogold cytochemistry, and western blotting, and for their ability to form annexin-S100 heterocomplex in vivo by immunoprecipitation. These four proteins displayed distinct expression patterns, ANXA5 being the first to be expressed in myotubes (i.e. at embryonic day 8), followed by ANXA6 (at embryonic day 12) and S100A1 and S100B (between embryonic day 12 and embryonic day 15). The two annexins and the two S100 proteins were found associated to different extents with the sarcolemma, membranes of the sarcoplasmic reticulum, and putative transverse tubules where they appeared to be co-localized from embryonic day 18 onwards. No one of these proteins was found associated with the contractile apparatus of the sarcomeres. Immunoprecipitation studies indicated that ANXA6/S100A1 and ANXA6/S100B complexes formed in vivo. Whereas, ANXA5 was not recovered in S100A1 or S100B immunoprecipitates. From our data we suggest that: (i) ANXA5 and ANXA6, and S100A1 and S100B can be used as markers of skeletal muscle development; (ii) ANXA6 and S100A1 and S100B appear strategically located close to or on skeletal muscle membrane organelles that are critically involved in the regulation of Ca2+ fluxes, thus supporting previous in vitro observations implicating S100A1 and ANXA6 in the stimulation of Ca2+-induced Ca2+ release; and (iii) ANXA6/S100A1 and ANXA6/S100B complexes can form in vivo thereby regulating each other activities and/or acting in concert to regulate membrane-associated activities.

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    Applied Physiology Nutrition and Metabolism 03/2014; 39(3):340-344. DOI:10.1139/apnm-2013-0308 · 2.01 Impact Factor
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    ABSTRACT: S100 Ca(2+)-binding proteins have been associated with a multitude of intracellular Ca(2+)-dependent functions including regulation of the cell cycle, cell differentiation, cell motility and apoptosis, modulation of membrane-cytoskeletal interactions, transduction of intracellular Ca(2+) signals, and in mediating learning and memory. S100 proteins are fine tuned to read the intracellular free Ca(2+) concentration and affect protein phosphorylation, which makes them candidates to modulate certain ion channels and neuronal electrical behavior. Certain S100s are secreted from cells and are found in extracellular fluids where they exert unique extracellular functions. In addition to their neurotrophic activity, some S100 proteins modulate neuronal electrical discharge activity and appear to act directly on ion channels. The first reports regarding these effects suggested S100-mediated alterations in Ca(2+) fluxes, K(+) currents, and neuronal discharge activity. Recent reports revealed direct and indirect interactions with Ca(2+), K(+), Cl(-), and ligand activated channels. This review focuses on studies of the physical and functional interactions of S100 proteins and ion channels.
    Frontiers in Pharmacology 04/2012; 3:67. DOI:10.3389/fphar.2012.00067
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    ABSTRACT: The cerebral S100B protein has been used as a peripheral marker of central nervous system injuries. However, recent studies have shown that S100B protein also increases after physical exercise, yet these increases are not completely understood. Some authors have proposed that S100B increase during exercise is related to active secretion by skeletal muscle. PURPOSE: Investigate serum S100B levels in running versus bicycling exercise, establishing a relationship among S100B and myoglobin, a traditional blood marker for muscle damage. METHODS: 13 male triathletes presenting (mean±SD) age= 33.9 ± 6.0 years, body mass= 74.7±6.8 kg, height = 177.0±0.1 cm and body fat = 11.1±4.7% participated in this study. They randomly completed two sub maximal exercise protocols lasting 40 minutes each at anaerobic threshold intensity. The running exercise was performed in treadmill with no inclination (RUN). The bicycling exercise was done in the athlete's own bicycle using a cycle-simulator (CYC). During each protocol, blood samples were taken before (PRE) and immediately after (POST) exercise. Protocol and time comparisons were made using paired t-tests. The samples were analyzed for S100B and myoglobin (Mb). RESULTS: After treadmill protocol, S100B was increased (PRE=0.109±0.002 vs POST=0.113±0.005 μg/L, p<0.05) as well as Mb (PRE= 38.8±9.1 vs POST=88.7±24.1 ng/ml, p<0.05). In the bicycle test there was no increase after exercise for these two variables. Immediately after exercise serum values for S100B (RUN = 0.113±0.005 vs CYC = 0.109±0.001 μg/L) and Mb (RUN=88.7±24.1 vs CYC = 49.2±13.6 ng/ml, p<0.05) were statistically higher in RUN than in CYC. There was a significant correlation between S100B and myoglobin after RUN and CYC (r=0.59, p=0.03). CONCLUSIONS: Exercise that presents higher muscle damage (RUN) promoted an increase in serum S100B levels, while exercise in the same intensity/duration (CYC) with lesser muscle damage did not present a significant increase in S100B.
    Medicine &amp Science in Sports &amp Exercise 01/2010; 42. DOI:10.1249/01.MSS.0000386277.77794.d3 · 4.46 Impact Factor


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