IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS

DISSMANN E, Hinssen H (1994)
EUROPEAN JOURNAL OF CELL BIOLOGY 63(2): 336-344.

Journal Article | Published | English

No fulltext has been uploaded

Author
;
Abstract
Gelsolin was localized by immunofluorescence in fibroblasts and skeletal muscle cells using antibodies which eliminated the risk of detecting xenogenic plasma gelsolin. Gelsolin was consistently found to be closely associated with the elements of the microfilament system: In fibroblasts, a preferential labeling of the stress fibers was observed, whereas with myogenic cells and myofibrils isolated from skeletal muscle, a specific staining of the I-Z-I region in the sarcomeres was found. From double labeling of gelsolin and actin it became evident that the staining patterns for both proteins were practically coincident: The width and location of the fluorescent bands varied with the degree of contraction of the myofibrils. The region of cross-bridges in the A-zone, where thick and thin filaments overlap, remained unstained. The gelsolin staining of myofibrils was EGTA-resistant; it persisted after glycerol extraction and extensive washing. The presence of gelsolin in myofibrils after this treatment was also confirmed by immunoblotting. From these observations it was concluded that a significant part of the total gelsolin in skeletal muscle cells is tightly associated with the thin filaments, and is an integral part of the myofibrils even at low Ca++-concentrations. Fmom the coincidence of actin and gelsolin staining in myofibrils it was concluded that gelsolin is localized along the whole length of the thin filaments in the sarcomere. Such a mode of association with filamentous actin is not fully explained by the current models of interaction of gelsolin with F-actin which involve either a filament severing or a capping of the ends of actin filaments rather than a stable lateral binding to the filaments without severing. It is assumed that, in myofibrils, actin-binding proteins like tropomyosin and nebulin inhibit the severing process but not the binding of gelsolin.
Publishing Year
ISSN
PUB-ID

Cite this

DISSMANN E, Hinssen H. IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS. EUROPEAN JOURNAL OF CELL BIOLOGY. 1994;63(2):336-344.
DISSMANN, E., & Hinssen, H. (1994). IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS. EUROPEAN JOURNAL OF CELL BIOLOGY, 63(2), 336-344.
DISSMANN, E., and Hinssen, H. (1994). IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS. EUROPEAN JOURNAL OF CELL BIOLOGY 63, 336-344.
DISSMANN, E., & Hinssen, H., 1994. IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS. EUROPEAN JOURNAL OF CELL BIOLOGY, 63(2), p 336-344.
E. DISSMANN and H. Hinssen, “IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS”, EUROPEAN JOURNAL OF CELL BIOLOGY, vol. 63, 1994, pp. 336-344.
DISSMANN, E., Hinssen, H.: IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS. EUROPEAN JOURNAL OF CELL BIOLOGY. 63, 336-344 (1994).
DISSMANN, E, and Hinssen, Horst. “IMMUNOCYTOCHEMICAL LOCALIZATION OF GELSOLIN IN FIBROBLASTS, MYOGENIC CELLS, AND ISOLATED MYOFIBRILS”. EUROPEAN JOURNAL OF CELL BIOLOGY 63.2 (1994): 336-344.
This data publication is cited in the following publications:
This publication cites the following data publications:

13 Citations in Europe PMC

Data provided by Europe PubMed Central.

Isoforms of gelsolin from lobster striated muscles differ in calcium-dependence.
Unger A, Brunne B, Hinssen H., Arch. Biochem. Biophys. 536(1), 2013
PMID: 23707758
Dynamic regulation of sarcomeric actin filaments in striated muscle.
Ono S., Cytoskeleton (Hoboken) 67(11), 2010
PMID: 20737540
Electron-microscopical localization of gelsolin in various crustacean muscles.
Unger A, Hinssen H., Cell Tissue Res. 341(2), 2010
PMID: 20607291
The deficiency of PIP2 5-phosphatase in Lowe syndrome affects actin polymerization.
Suchy SF, Nussbaum RL., Am. J. Hum. Genet. 71(6), 2002
PMID: 12428211
Distribution of gelsolin and phosphoinositol 4,5-bisphosphate in lamellipodia during EGF-induced motility.
Chou J, Stolz DB, Burke NA, Watkins SC, Wells A., Int. J. Biochem. Cell Biol. 34(7), 2002
PMID: 11950594
Distribution of gelsolin in human testis.
Rousseaux-Prevost R, Delobel B, Hermand E, Rigot JM, Danjou P, Mazeman E, Rousseaux J., Mol. Reprod. Dev. 48(1), 1997
PMID: 9266762
A role for gelsolin in actuating epidermal growth factor receptor-mediated cell motility.
Chen P, Murphy-Ullrich JE, Wells A., J. Cell Biol. 134(3), 1996
PMID: 8707848
Exogenous gelsolin binds to sarcomeric thin filaments without severing.
Gonsior S, Hinssen H., Cell Motil. Cytoskeleton 31(3), 1995
PMID: 7585989

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 8082657
PubMed | Europe PMC

Search this title in

Google Scholar