Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris

Krueger E, Hinssen H, D'Haese J (2008)
CELL AND TISSUE RESEARCH 332(1): 141-150.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Krueger, Evelyn; Hinssen, HorstUniBi; D'Haese, Jochen
Abstract / Bemerkung
A gelsolin-related protein was isolated from seminal vesicles of the annelid Lumbricus terrestris. Compared with the isoforms of the gelsolin-related protein previously found in the muscle of the annelid body wall, the isolated protein was assigned to the first isoform (EWAM-P1) because of its electrophoretic mobility, chromatographic elution behaviour, immunological cross-reactivity and identical nucleotide sequence of segments obtained by reverse transcription/polymerase chain reaction. Immunofluorescence studies with smear preparations of developing male germ cells revealed characteristic changes of the local distribution of actin and EWAM-P1 during spermatogenesis. These changes were correlated with the developmental transport processes and structural alterations. F-actin, as revealed by rhodamine-phalloidin staining, formed a toroid-shaped structure in cytoplasmic bridges connecting the germ cells to a central cytophore during the developmental stages. An actin antibody reacting with both G- and F-actin demonstrated that actin was concentrated at the proximal and distal parts of the spermatocytes. EWAM-P1 was also localized in these regions, with intense staining in the distal part of spermatocytes and young spermatids in which the Golgi complex and proacrosome resided. The anti-actin antibody further stained the periphery of the nucleus. This staining gradually reduced during sperm maturation and covered about half of the length of the nucleus in elongated spermatids. Co-localization of EWAM with actin implied a functional significance of this gelsolin-related protein for the rearrangement of the actin cytoskeleton during earthworm spermiogenesis.
Stichworte
earthworm actin modulator; cytoskeleton; gelsolin-related protein; remodelling; spermatogenesis; Lumbricus terrestris (annelida); earthworm
Erscheinungsjahr
2008
Zeitschriftentitel
CELL AND TISSUE RESEARCH
Band
332
Ausgabe
1
Seite(n)
141-150
ISSN
0302-766X
eISSN
1432-0878
Page URI
https://pub.uni-bielefeld.de/record/1592231

Zitieren

Krueger E, Hinssen H, D'Haese J. Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris. CELL AND TISSUE RESEARCH. 2008;332(1):141-150.
Krueger, E., Hinssen, H., & D'Haese, J. (2008). Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris. CELL AND TISSUE RESEARCH, 332(1), 141-150. https://doi.org/10.1007/s00441-007-0561-9
Krueger, Evelyn, Hinssen, Horst, and D'Haese, Jochen. 2008. “Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris”. CELL AND TISSUE RESEARCH 332 (1): 141-150.
Krueger, E., Hinssen, H., and D'Haese, J. (2008). Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris. CELL AND TISSUE RESEARCH 332, 141-150.
Krueger, E., Hinssen, H., & D'Haese, J., 2008. Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris. CELL AND TISSUE RESEARCH, 332(1), p 141-150.
E. Krueger, H. Hinssen, and J. D'Haese, “Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris”, CELL AND TISSUE RESEARCH, vol. 332, 2008, pp. 141-150.
Krueger, E., Hinssen, H., D'Haese, J.: Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris. CELL AND TISSUE RESEARCH. 332, 141-150 (2008).
Krueger, Evelyn, Hinssen, Horst, and D'Haese, Jochen. “Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris”. CELL AND TISSUE RESEARCH 332.1 (2008): 141-150.

7 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
Unique phenotypes in the sperm of the earthworm Eudrilus eugeniae for assessing radiation hazards.
Yesudhason BV, Jegathambigai J, Thangasamy PA, Lakshmanan DD, Selvan Christyraj JR, Sathya Balasingh Thangapandi EJ, Krishnan M, Sivasubramaniam S., Environ Monit Assess 185(6), 2013
PMID: 23093367
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

39 References

Daten bereitgestellt von Europe PubMed Central.

pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis.
Adams RR, Tavares AA, Salzberg A, Bellen HJ, Glover DM., Genes Dev. 12(10), 1998
PMID: 9585508

KG, 1983
Characterization of actin isoforms in ejaculated boar spermatozoa.
Casale A, Camatini M, Skalli O, Gabbiani G., Gamete Res 20(2), 1988
PMID: 3069684

N, Methods Enzymol 69(), 1980

J, J Comp Physiol [B] 248(), 1987

T, Eur J Biochem 255(), 1994
Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis.
Gunsalus KC, Bonaccorsi S, Williams E, Verni F, Gatti M, Goldberg ML., J. Cell Biol. 131(5), 1995
PMID: 8522587

GR, J Cell Sci 109(), 1996
Myosin VI is required for asymmetric segregation of cellular components during C. elegans spermatogenesis.
Kelleher JF, Mandell MA, Moulder G, Hill KL, L'Hernault SW, Barstead R, Titus MA., Curr. Biol. 10(23), 2000
PMID: 11114515

E, J Muscle Res Cell Motil 22(), 2001
Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.
Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL., Nature 323(6087), 1986
PMID: 3020431

M, Comp Biochem Physiol [B] 119(), 1998

S, J Biochem (Tokyo) 92(), 1982

E, Zool Jahrb (Anat) 58(), 1934
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
Actin in ejaculated human sperm cells.
Ochs D, Wolf DP., Biol. Reprod. 33(5), 1985
PMID: 4074810
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
Calcium-dependent actin filament-severing protein scinderin levels and localization in bovine testis, epididymis, and spermatozoa.
Pelletier R, Trifaro JM, Carbajal ME, Okawara Y, Vitale ML., Biol. Reprod. 60(5), 1999
PMID: 10208974
Membrane trafficking, organelle transport, and the cytoskeleton.
Rogers SL, Gelfand VI., Curr. Opin. Cell Biol. 12(1), 2000
PMID: 10679352
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

W, Zool Jahrb (Anat) 24(), 1907
The three-dimensional structure of the Limulus acrosomal process: a dynamic actin bundle.
Sherman MB, Jakana J, Sun S, Matsudaira P, Chiu W, Schmid MF., J. Mol. Biol. 294(1), 1999
PMID: 10556034

B, Zoomorphology 109(), 1989
Identification of secreted and cytosolic gelsolin in Drosophila.
Stella MC, Schauerte H, Straub KL, Leptin M., J. Cell Biol. 125(3), 1994
PMID: 8175883
Fasciola hepatica: disruption of spermatogenesis by the microfilament inhibitor cytochalasin B.
Stitt AW, Fairweather I, Johnston CF., Parasitol. Res. 77(2), 1991
PMID: 2027880
Gelsolin, a multifunctional actin regulatory protein.
Sun HQ, Yamamoto M, Mejillano M, Yin HL., J. Biol. Chem. 274(47), 1999
PMID: 10559185
Physarum amoebae express a distinct fragmin-like actin-binding protein that controls in vitro phosphorylation of actin by the actin-fragmin kinase.
T'jampens D, Bailey J, Cook LJ, Constantin B, Vandekerckhove J, Gettemans J., Eur. J. Biochem. 265(1), 1999
PMID: 10491179

LG, J Cell Biol 77(), 1978

D, Biol Cell 37(), 1980

D, Biol Cell 37(), 1980
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 18197420
PubMed | Europe PMC

Suchen in

Google Scholar