Subcellular localization of S100A11 (S100C, calgizzarin) in developing and adult avian skeletal muscles

被引:11
作者
Arcuri, C [1 ]
Giambanco, I [1 ]
Bianchi, R [1 ]
Donato, R [1 ]
机构
[1] Univ Perugia, Dept Expt Med & Biochem Sci, Sect Anat, I-06122 Perugia, Italy
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2002年 / 1600卷 / 1-2期
关键词
sarcoplasmic reticulum; T-tubule; calcium; S100A1; S100B; confocal laser scanning microscopy; immunogold cytochemistry;
D O I
10.1016/S1570-9639(02)00448-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
S100A11 is a member of a multigenic family of Ca2+-modulated proteins of the EF-hand type. We studied the subcellular localization of S100A11 in developing and adult avian skeletal muscle cells by confocal laser scanning microscopy and immunogold cytochemistry to get information about possible functional roles of this protein. Analyses of alpha-actinin, S100A1 and S 10013 were done in parallel for comparison. Low levels of S100A11 were found in skeletal muscle cells at embryonic day (E) 8. At E12, S100A11 was found in myotubes in the form of fine dots located between Z-discs, and on the sarcolemma and its invaginations. At E15, S100A11 was found on the sarcolema and internal membranes, likely longitudinal tubules, where the protein was co-localized in part with S100A1 and S100B. At E18 and afterwards, co-localization of the three S100 proteins on internal membranes was almost complete. No evidence for association of S100A11 with the contractile elements of the sarcomeres was obtained. Our data suggests that, like S100A1 and S100B, S100A11 might have a role in the regulation of membrane activities, probably in relation to Ca2+ fluxes in skeletal muscle cells. (C) 2002 Elsevier Science B.V All rights reserved.
引用
收藏
页码:84 / 94
页数:11
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