Muscular and Cytoplasmic Contractile Proteins

Gröschel‐Stewart, Ute; Drenckhahn, Detlev

doi:10.1016/s0174-173x(82)80002-2

Cited by 27 publications

(4 citation statements)

References 556 publications

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“…In smooth muscle, anti-vinculin displayed a typical "dense patch"-and "dense band"-like pattern (38) confined to the cellular periphery. These findings are fully consistent with the current view of the subcellular distribution of actin, a-actinin, and vinculin in smooth and striated muscle (24). This clearly documents the specificity and power of the technique used.…”

Section: Fluorescence Microscopy Technical Consideration: Specificity Of Staining In Striated and Smooth Musclesupporting

confidence: 90%

“…First, vinculin is a protein confined to particular actin filament membrane associations in various cell types in vitro and in situ (19,24,29). a-Actinin, the actin filament cross-linking protein of the muscular Z-line, is also a characteristic component of plasmalemmal anchoring sites of actin filaments (19,24,29). It is reasonable, therefore, that the actin-, vinculin-, and a-actinin-containing plaques associated with the lateral cell surface represent places where actin filaments are attached to the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

“…Several lines of evidence strongly indicate the association of type II plaques with actin, a-actinin, and vinculin. First, vinculin is a protein confined to particular actin filament membrane associations in various cell types in vitro and in situ (19,24,29). a-Actinin, the actin filament cross-linking protein of the muscular Z-line, is also a characteristic component of plasmalemmal anchoring sites of actin filaments (19,24,29).…”

Section: Discussionmentioning

confidence: 99%

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Identification of actin-, alpha-actinin-, and vinculin-containing plaques at the lateral membrane of epithelial cells.

Drenckhahn¹,

Franz²

1986

The Journal of Cell Biology

141

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Abstract. In this paper, a new type of spot desmosome-like junction (type II plaque) is described that is scattered along the entire lateral plasma membrane of rat and human intestinal epithelium. Ultrastructurally type II plaques differed from the classical type of epithelial spot desmosome ("macula adherens", further denoted as type I desmosome) by (a) weak electron density of the membrane-associated plaque material, (b) association of the plaques with microfilaments rather than intermediate filaments, and (c) poorly visible material across the intercellular space. Thus, type II plaques resemble cross-sections of the zonula adherens. Immunofluorescence-microscopic studies were done using antibodies to a main protein associated with the plaques of type I desmosomes (desmoplakin I) and to the three major proteins located at the plaques of the zonula adherens (actin, a-actinin, and vinculin). Two types of plaques were visualized along the lateral surface of intestinal and prostatic epithelium: (a) the type I desmosomes, which were labeled with anti-desmoplakin but did not bind antibodies to actin, a-actinin, and vinculin, and (b) a further set of similarly sized plaques, which bound antibodies to actin, a-actinin, and vinculin but were not stained with anti-desmoplakin. Three-dimensional computer reconstruction of serial sections double-labeled with anti-desmoplakin and anti-a-actinin further confirmed that both types of plaques are spatially completely separated from each other along the lateral plasma membrane. The computer graphs further revealed that the actin-, a-actinin-, and vinculin-containing plaques have the tendency to form clusters, a feature also typical of type II plaques. It is suggested that the type II plaques represent spot desmosomelike intercellular junctions, which, like the zonula adherens, appear to be linked to the actin filament system. As the type II plaques cover a considerable part of the lateral cell surface, they might play a particular role in controlling cellular shape and intercellular adhesion.

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Section: Fluorescence Microscopy Technical Consideration: Specificity Of Staining In Striated and Smooth Musclesupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of actin-, alpha-actinin-, and vinculin-containing plaques at the lateral membrane of epithelial cells.

Drenckhahn¹,

Franz²

1986

The Journal of Cell Biology

141

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“…Фермент міозин є головним білком товстого філаменту ГМ. Імунологічно він відрізняється від міозину скелетних м'язів [6 ] і складається з двох високомолекулярних субодиниць, або важких ланцюгів (ВЛ), і двох типів низькомолекулярних субодйниць, або легких ланцюгів (ЛЛ) (рис. 1).…”

unclassified

Untitled

1996

Biopolym. Cell

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В огляді проаналізовано останні досягнення в області біохімії і молекулярної фізіології регуляції скорочувальних процесів в гладеньких м'язах. Скорочення гладенького м'яза потребує фосфорилювання міозину. Цей процес пов'язаний з внутрішньоклітинним викидом Са і наступним утворенням Са-кальмодулінового комплексу та активацією кінази легких ланцюгів міозину. Розслаблення забезпечується дефосфорилюванням міозину за допомогою фосфатази легких ланцюгів міозину. Існує припущення, що дефосфорилювання не регулюється. Інші можливі механізми регуляції включають зв'язані з тонкими філаментами білки, такі як кальдесмон і кальпонін.

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