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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

Detection of the antigen on Western blot. Proteins were obtained from 12-day testes (a), adult testis (b) and epididymal sperm (c). Note that the 64-kDa antigenic protein is present in both adult testes and sperm, but not in the 12-day testes. Numbers on left indicate molecular weight markers (×10−3).
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Figure 1: Detection of the antigen on Western blot. Proteins were obtained from 12-day testes (a), adult testis (b) and epididymal sperm (c). Note that the 64-kDa antigenic protein is present in both adult testes and sperm, but not in the 12-day testes. Numbers on left indicate molecular weight markers (×10−3).

Mentions: The molecular weight of the antigen was determined by Western blotting with MC321 (Fig. 1). In the testicular extracts from 12-day-old rats, an immunoreactive band of 77 kDa was prominent and another minor band was detected at a position above the 77-kDa band. The testicular cytosolic proteins prepared from adult rats contained two immunoreactive proteins with relative molecular masses of 77 kDa and 64 kDa. In the sperm proteins extracted with 2% SDS, the 64-kDa band was the only immunoreactive one.


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)

Detection of the antigen on Western blot. Proteins were obtained from 12-day testes (a), adult testis (b) and epididymal sperm (c). Note that the 64-kDa antigenic protein is present in both adult testes and sperm, but not in the 12-day testes. Numbers on left indicate molecular weight markers (×10−3).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC1828079&req=5

Figure 1: Detection of the antigen on Western blot. Proteins were obtained from 12-day testes (a), adult testis (b) and epididymal sperm (c). Note that the 64-kDa antigenic protein is present in both adult testes and sperm, but not in the 12-day testes. Numbers on left indicate molecular weight markers (×10−3).
Mentions: The molecular weight of the antigen was determined by Western blotting with MC321 (Fig. 1). In the testicular extracts from 12-day-old rats, an immunoreactive band of 77 kDa was prominent and another minor band was detected at a position above the 77-kDa band. The testicular cytosolic proteins prepared from adult rats contained two immunoreactive proteins with relative molecular masses of 77 kDa and 64 kDa. In the sperm proteins extracted with 2% SDS, the 64-kDa band was the only immunoreactive one.

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