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Preferential localization of rat GAPDS on the ribs of fibrous sheath of sperm flagellum and its expression during flagellar formation.

Tanii I, Yagura T, Inagaki N, Nakayama T, Imaizumi K, Yoshinaga K - Acta Histochem Cytochem (2007)

Bottom Line: To obtain information on the assembly of the glycolytic enzyme into the flagellum, the precise localization of rat GAPDS in the flagellum and the stage of incorporation into the flagellum were examined using a monoclonal antibody.Immunoreactivity was first detected in the cytoplasm and flagella of the step-16 spermatids during the final step of FS formation.Together with the expression of other FS proteins, the present results indicate the sequential assembly of FS components, suggesting that the expression and transport of GAPDS is regulated in a coordinated manner during sperm flagellar formation.

View Article: PubMed Central - PubMed

Affiliation: Division of Molecular and Cellular Biology, Department of Anatomy, Faculty of Medicine, University of Miyazaki, Miyazaki 889-1692, Japan.

ABSTRACT
The proper assembly of sperm flagellar proteins is fundamental for sperm motility. The sperm- and spermatid-specific isoform of glyceraldehyde 3-phosphate dehydrogenase, GAPDS, is a flagellar protein indispensable for sperm flagellar movement. To obtain information on the assembly of the glycolytic enzyme into the flagellum, the precise localization of rat GAPDS in the flagellum and the stage of incorporation into the flagellum were examined using a monoclonal antibody. Immunolocalization of rat GAPDS was restricted to the fibrous sheath (FS) in the sperm flagellum, and was predominant in the circumferential ribs rather than the longitudinal columns. Immunoreactivity was first detected in the cytoplasm and flagella of the step-16 spermatids during the final step of FS formation. Together with the expression of other FS proteins, the present results indicate the sequential assembly of FS components, suggesting that the expression and transport of GAPDS is regulated in a coordinated manner during sperm flagellar formation.

No MeSH data available.


Related in: MedlinePlus

Immunodetection of the antigen in busulfan-treated adult testes. A: Section of busulfan-treated testis stained with hematoxylin-eosin. Bar=200 µm. B: Western blotting. Proteins were obtained from busulfan-treated testes (a) and control testes without treatment (b). Numbers on left indicate molecular weight markers (×10−3).
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Figure 2: Immunodetection of the antigen in busulfan-treated adult testes. A: Section of busulfan-treated testis stained with hematoxylin-eosin. Bar=200 µm. B: Western blotting. Proteins were obtained from busulfan-treated testes (a) and control testes without treatment (b). Numbers on left indicate molecular weight markers (×10−3).

Mentions: Two antigenic proteins of 64-kDa and 77-kDa were detected in the testicular extract from adult rats (Fig. 1b). To determine the origin of the antigens, we used the adult testes at 58 days after the injection of a single dose of busulfan, in which most of the elongating spermatids and testicular sperm were depleted by the treatment (Fig. 2A). In the Western blots of the extract from the busulfan-treated testes, the 77-kDa protein was prominent while the 64-kDa protein was hardly detected (Fig. 2B). This result shows that the 64-kDa protein is derived exclusively from the sperm and elongating spermatids. Together with the finding that the 77-kDa band was prominent in the 12-day testes, the 77-kDa protein is presumably derived from Sertoli cells, meiotic or premeiotic spermatogenic cells.


Preferential localization of rat GAPDS on the ribs of fibrous sheath of sperm flagellum and its expression during flagellar formation.

Tanii I, Yagura T, Inagaki N, Nakayama T, Imaizumi K, Yoshinaga K - Acta Histochem Cytochem (2007)

Immunodetection of the antigen in busulfan-treated adult testes. A: Section of busulfan-treated testis stained with hematoxylin-eosin. Bar=200 µm. B: Western blotting. Proteins were obtained from busulfan-treated testes (a) and control testes without treatment (b). Numbers on left indicate molecular weight markers (×10−3).
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC1828079&req=5

Figure 2: Immunodetection of the antigen in busulfan-treated adult testes. A: Section of busulfan-treated testis stained with hematoxylin-eosin. Bar=200 µm. B: Western blotting. Proteins were obtained from busulfan-treated testes (a) and control testes without treatment (b). Numbers on left indicate molecular weight markers (×10−3).
Mentions: Two antigenic proteins of 64-kDa and 77-kDa were detected in the testicular extract from adult rats (Fig. 1b). To determine the origin of the antigens, we used the adult testes at 58 days after the injection of a single dose of busulfan, in which most of the elongating spermatids and testicular sperm were depleted by the treatment (Fig. 2A). In the Western blots of the extract from the busulfan-treated testes, the 77-kDa protein was prominent while the 64-kDa protein was hardly detected (Fig. 2B). This result shows that the 64-kDa protein is derived exclusively from the sperm and elongating spermatids. Together with the finding that the 77-kDa band was prominent in the 12-day testes, the 77-kDa protein is presumably derived from Sertoli cells, meiotic or premeiotic spermatogenic cells.

Bottom Line: To obtain information on the assembly of the glycolytic enzyme into the flagellum, the precise localization of rat GAPDS in the flagellum and the stage of incorporation into the flagellum were examined using a monoclonal antibody.Immunoreactivity was first detected in the cytoplasm and flagella of the step-16 spermatids during the final step of FS formation.Together with the expression of other FS proteins, the present results indicate the sequential assembly of FS components, suggesting that the expression and transport of GAPDS is regulated in a coordinated manner during sperm flagellar formation.

View Article: PubMed Central - PubMed

Affiliation: Division of Molecular and Cellular Biology, Department of Anatomy, Faculty of Medicine, University of Miyazaki, Miyazaki 889-1692, Japan.

ABSTRACT
The proper assembly of sperm flagellar proteins is fundamental for sperm motility. The sperm- and spermatid-specific isoform of glyceraldehyde 3-phosphate dehydrogenase, GAPDS, is a flagellar protein indispensable for sperm flagellar movement. To obtain information on the assembly of the glycolytic enzyme into the flagellum, the precise localization of rat GAPDS in the flagellum and the stage of incorporation into the flagellum were examined using a monoclonal antibody. Immunolocalization of rat GAPDS was restricted to the fibrous sheath (FS) in the sperm flagellum, and was predominant in the circumferential ribs rather than the longitudinal columns. Immunoreactivity was first detected in the cytoplasm and flagella of the step-16 spermatids during the final step of FS formation. Together with the expression of other FS proteins, the present results indicate the sequential assembly of FS components, suggesting that the expression and transport of GAPDS is regulated in a coordinated manner during sperm flagellar formation.

No MeSH data available.


Related in: MedlinePlus