Electron-microscopical localization of gelsolin in various crustacean muscles

Unger A, Hinssen H (2010)

Zeitschriftenaufsatz | Veröffentlicht | Englisch
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Unger, Andreas; Hinssen, HorstUniBi
Abstract / Bemerkung
Gelsolin was localized by immunoelectron microscopy in fast and slow cross-striated muscles of the lobster Homarus americanus. When ultrathin sections of the muscles were labelled with anti-gelsolin and a gold-conjugated second antibody, 90% of all gold particles in the myoplasm were detected on myofibrils, preferentially in the I-band and AI-region of the sarcomeres. Both the region of the H-zone (lacking thin filaments) and the Z-disc contained no or little gold label. Under physiological conditions, a close association of gelsolin with the thin filaments was observed for both muscle types. The preferential localization of particles in the I- and AI-region indicated that gelsolin was distributed randomly over the whole length of the thin filaments. Preincubation of muscle strips with Ringer solution containing 0.5 mM EGTA resulted in a significantly different distribution pattern; gold particles were now localized preferentially in the cell periphery close to the sarcolemma, with significantly decreased abundance in the centre of the cell. Compared with the muscle under physiological conditions, the number of gold particles over sarcomeric structures was significantly reduced. Thus, binding of gelsolin to the thin filaments is apparently reversible in vivo and depends on the presence of calcium ions. We assume a functional role for gelsolin in the actin turnover processes in invertebrate muscle systems.
Homarus americanus (Crustacea); Gelsolin; Cross-striated muscle; Myofibril; Immunoelectron microscopy; Lobster
Page URI


Unger A, Hinssen H. Electron-microscopical localization of gelsolin in various crustacean muscles. CELL AND TISSUE RESEARCH. 2010;341(2):313-323.
Unger, A., & Hinssen, H. (2010). Electron-microscopical localization of gelsolin in various crustacean muscles. CELL AND TISSUE RESEARCH, 341(2), 313-323. https://doi.org/10.1007/s00441-010-1003-7
Unger, Andreas, and Hinssen, Horst. 2010. “Electron-microscopical localization of gelsolin in various crustacean muscles”. CELL AND TISSUE RESEARCH 341 (2): 313-323.
Unger, A., and Hinssen, H. (2010). Electron-microscopical localization of gelsolin in various crustacean muscles. CELL AND TISSUE RESEARCH 341, 313-323.
Unger, A., & Hinssen, H., 2010. Electron-microscopical localization of gelsolin in various crustacean muscles. CELL AND TISSUE RESEARCH, 341(2), p 313-323.
A. Unger and H. Hinssen, “Electron-microscopical localization of gelsolin in various crustacean muscles”, CELL AND TISSUE RESEARCH, vol. 341, 2010, pp. 313-323.
Unger, A., Hinssen, H.: Electron-microscopical localization of gelsolin in various crustacean muscles. CELL AND TISSUE RESEARCH. 341, 313-323 (2010).
Unger, Andreas, and Hinssen, Horst. “Electron-microscopical localization of gelsolin in various crustacean muscles”. CELL AND TISSUE RESEARCH 341.2 (2010): 313-323.

5 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Four paralog gelsolin genes are differentially expressed in the earthworm Lumbricus terrestris.
Thiruketheeswaran P, Thomalla P, Krüger E, Hinssen H, D'Haese J., Comp Biochem Physiol B Biochem Mol Biol 208-209(), 2017
PMID: 28400331
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
The interaction of gelsolin with tropomyosin modulates actin dynamics.
Khaitlina S, Fitz H, Hinssen H., FEBS J 280(18), 2013
PMID: 23844991
Actin-binding Rho activating protein is expressed in the central nervous system of normal adult rats.
Liu L, Luo M, Yang B, Wu X, Zhu W, Guan Y, Cai W, Troidl K, Schaper W, Schaper J., Neural Regen Res 7(13), 2012
PMID: 25722683
Proteomic analysis of serum proteins in acute ischemic stroke patients treated with acupuncture.
Pan S, Zhan X, Su X, Guo L, Lv L, Su B., Exp Biol Med (Maywood) 236(3), 2011
PMID: 21427238

43 References

Daten bereitgestellt von Europe PubMed Central.

A re-evaluation of cytoplasmic gelsolin localization.
Carron CP, Hwo SY, Dingus J, Benson DM, Meza I, Bryan J., J. Cell Biol. 102(1), 1986
PMID: 3001100
Microinjection of gelsolin into living cells.
Cooper JA, Bryan J, Schwab B 3rd, Frieden C, Loftus DJ, Elson EL., J. Cell Biol. 104(3), 1987
PMID: 3029140
Localization and mobility of gelsolin in cells.
Cooper JA, Loftus DJ, Frieden C, Bryan J, Elson EL., J. Cell Biol. 106(4), 1988
PMID: 2834402
Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin.
Cunningham CC, Stossel TP, Kwiatkowski DJ., Science 251(4998), 1991
PMID: 1848726

J, Eur J Cell Biol 48(), 1989

J, J Comp Physiol [B] 248(), 1987
Incorporation of fluorescently labeled actin and tropomyosin into muscle cells.
Dome JS, Mittal B, Pochapin MB, Sanger JM, Sanger JW., Cell Differ. 23(1-2), 1988
PMID: 2453294
C-terminally deleted fragments of 40-kDa earthworm actin modulator still show gelsolin activities.
Giebing T, Obermann WM, Furst D, D'Haese J., FEBS Lett. 417(2), 1997
PMID: 9395293
Exogenous gelsolin binds to sarcomeric thin filaments without severing.
Gonsior S, Hinssen H., Cell Motil. Cytoskeleton 31(3), 1995
PMID: 7585989
Gelsolin--evidence for a role in turnover of junction-related actin filaments in Sertoli cells.
Guttman JA, Janmey P, Vogl AW., J. Cell. Sci. 115(Pt 3), 2002
PMID: 11861757

JA, Anat Rec 290(), 2007
Association of gelsolin with actin filaments and cell membranes of macrophages and platelets.
Hartwig JH, Chambers KA, Stossel TP., J. Cell Biol. 108(2), 1989
PMID: 2537317
Organization of native and in vitro-reassembled myosin filaments from lobster tonic muscle.
Hayashi T, Hinssen H, Cayer ML, Smith DS., Tissue Cell 13(1), 1981
PMID: 7194522
Cloning of a secretory gelsolin from Drosophila melanogaster.
Heintzelman MB, Frankel SA, Artavanis-Tsakonas S, Mooseker MS., J. Mol. Biol. 230(3), 1993
PMID: 8386771

H, 1986

Y, Biomed Res 9(), 1988
Ca2+ regulation of gelsolin activity: binding and severing of F-actin.
Kinosian HJ, Newman J, Lincoln B, Selden LA, Gershman LC, Estes JE., Biophys. J. 75(6), 1998
PMID: 9826630
Interaction of plasma gelsolin with tropomyosin.
Koepf EK, Burtnick LD., FEBS Lett. 309(1), 1992
PMID: 1324850
Muscle is the major source of plasma gelsolin.
Kwiatkowski DJ, Mehl R, Izumo S, Nadal-Ginard B, Yin HL., J. Biol. Chem. 263(17), 1988
PMID: 2836420

M, Comp Biochem Physiol [B] 119(), 1998
Incorporation of fluorescently labeled contractile proteins into freshly isolated living adult cardiac myocytes.
LoRusso SM, Imanaka-Yoshida K, Shuman H, Sanger JM, Sanger JW., Cell Motil. Cytoskeleton 21(2), 1992
PMID: 1559262
A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.
Luck A, D'Haese J, Hinssen H., Biochem. J. 305 ( Pt 3)(), 1995
PMID: 7848275
Domain 2 of gelsolin binds directly to tropomyosin.
Maciver SK, Ternent D, McLaughlin PJ., FEBS Lett. 473(1), 2000
PMID: 10802062
The gelsolin family of actin regulatory proteins: modular structures, versatile functions.
McGough AM, Staiger CJ, Min JK, Simonetti KD., FEBS Lett. 552(2-3), 2003
PMID: 14527663

CJ, Biophys J 68(), 1995
Tropomyosin and gelsolin cooperate in controlling the microfilament system.
Nyakern-Meazza M, Narayan K, Schutt CE, Lindberg U., J. Biol. Chem. 277(32), 2002
PMID: 12048198
Functional characteristics and the complete primary structure of ascidian gelsolin.
Ohtsuka Y, Nakae H, Abe H, Obinata T., Biochim. Biophys. Acta 1383(2), 1998
PMID: 9602133
Muscle gelsolin: isolation from heart tissue and characterization as an integral myofibrillar protein.
Rouayrenc JF, Fattoum A, Gabrion J, Audemard E, Kassab R., FEBS Lett. 167(1), 1984
PMID: 6321238
Identification of secreted and cytosolic gelsolin in Drosophila.
Stella MC, Schauerte H, Straub KL, Leptin M., J. Cell Biol. 125(3), 1994
PMID: 8175883
Gelsolin, a multifunctional actin regulatory protein.
Sun HQ, Yamamoto M, Mejillano M, Yin HL., J. Biol. Chem. 274(47), 1999
PMID: 10559185
Phosphoinositide regulation of the actin cytoskeleton.
Yin HL, Janmey PA., Annu. Rev. Physiol. 65(), 2002
PMID: 12471164

HL, J Biol Chem 274(), 1981

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

PMID: 20607291
PubMed | Europe PMC

Suchen in

Google Scholar