Fine structural immunocytochemistry of catenins in amphibian and mammalian muscle

被引:20
作者
Kurth, T [1 ]
Schwarz, H [1 ]
Schneider, S [1 ]
Hausen, P [1 ]
机构
[1] MAX PLANCK INST ENTWICKLUNGSBIOL, D-72011 TUBINGEN, GERMANY
关键词
cell adhesion; catenins; heart muscle; costamere; Z-disc; dense body; immuno-electron microscopy; Xenopus laevis; guinea pig;
D O I
10.1007/s004410050669
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
In adherens junctions, alpha- and beta-catenin serve to link cadherins to the cortical cytoskeleton. Immunofluorescence and immune-electron microscopy have been applied to elucidate the nature and localization of cadherin/catenin-mediated cell-cell adhesion sites in adult muscle tissues. Antibodies against alpha- and beta-catenin have been used as indicators of such sites in amphibian and mammalian muscle. Intercalated discs are prominent cell-cell adhesion sites in heart muscle. They contain large amounts of the two catenins, the distributions of which are disclosed. In addition and in contrast to their counterparts in guinea pig, cardiomyocytes of Xenopus are also interconnected laterally by catenin-containing cell-cell junctions. These are doubler structures that approach the intercellular contacts of two adjacent cells from both sides and occur in register with the Z-discs. We interpret these structures as catenin/cadherin-based costameres. Ultrastructural details of these structures are described. In addition to its presence in cell-cell adhesion sites, we have found beta-catenin, but not alpha-catenin, in the Z-discs of heart and skeletal striated muscles. In smooth muscle, actin filaments insert into the dense bodies, which are therefore regarded as functional equivalents of the Z-discs. Accordingly, beta-catenin is also found in these structures, again in the absence of alpha-catenin. These non-peripheral intracellular localizations in the Z-discs of striated muscles and the dense bodies of smooth muscle indicate a hitherto unknown function of beta-catenin in these specialized cells.
引用
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页码:1 / 12
页数:12
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