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BOR - Papers in Press, published online ahead of print November 19, 2003.
Biol Reprod 2003, 10.1095/biolreprod.103.022723
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BIOLOGY OF REPRODUCTION 70, 805–812 (2004)
DOI: 10.1095/biolreprod.103.022723
© 2004 by the Society for the Study of Reproduction, Inc.

Testis

Non-Muscle Cofilin Is a Component of Tubulobulbar Complexes in the Testis1

J.A. Guttman3, T. Obinata4, J. Shima5, M. Griswold5, and A.W. Vogl2,3

Department of Anatomy and Cell Biology,3 The University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3 Department of Biology,4 Chiba University, Chiba 263-8522, Japan Department of Molecular Biosciences,5 Washington State University, Pullman, Washington 99164-4660

Tubulobulbar complexes are finger-like structures that form at the interface between maturing spermatids and Sertoli cells prior to sperm release and at the interface between two Sertoli cells near the base of the seminiferous epithelium. They originate in areas previously occupied by actin filament-associated intercellular adhesion plaques known as ectoplasmic specializations. Actin filaments also are associated with tubulobulbar complexes where they appear to form a network, rather than the tightly packed bundles found in ectoplasmic specializations. Cofilin, a calcium-independent actin-depolymerizing protein, previously has been identified in the testis, but has not been localized to specific structures in the seminiferous epithelium. To determine if cofilin is found in Sertoli cells and is concentrated at actin-rich structures, we reacted fixed frozen sections of rat testis, fixed fragmented tissue, and blots of seminiferous epithelium with pan-specific and non-muscle cofilin antibodies. In addition, GeneChip microarrays (Affymetrix, Santa Clara, CA) were utilized to determine the abundance of mRNA for all cofilin isoforms in Sertoli cells. Using the monoclonal pan-specific cofilin antibody, we found specific labeling exclusively at tubulobulbar complexes and not at ectoplasmic specializations. On one-dimensional (1D) Western blots this antibody reacted monospecifically with one band, and on 2D blots reacted with two dots, which we interpret as phosphorylated and nonphosphorylated forms of a single cofilin isotype. Messenger RNA for non-muscle cofilin in Sertoli cells is about 8.5-fold higher than for muscle-type cofilin. To confirm that the non-muscle isoform of cofilin is present at tubulobulbar complexes, we used antibodies specific to non-muscle cofilin for immunofluorescent localization. As with the pan-specific antibody, we found that the non-muscle cofilin antibody exclusively labeled tubulobulbar complexes. Results presented here indicate that non-muscle cofilin is concentrated at tubulobulbar complexes. Our results also indicate that cofilin is not concentrated at ectoplasmic specializations.

1 Supported by the CIHR operating grant MOP 62728 awarded to A.W.V., NICHD grants HD 10808 and HD 42454 awarded to M.G., and a CIHR doctoral research award to J.A.G.

2 Correspondence: A. Wayne Vogl, 313-2177 Wesbrook Mall, The University of British Columbia, Department of Anatomy and Cell Biology, Vancouver, BC, Canada V6T 1Z3. FAX: 604 822 2316; vogl{at}interchange.ubc.ca




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