Immunohistochemical study of protein 4.1B in the normal and W/W(v) mouse seminiferous epithelium.
Cell-cell adhesion is crucial not only for mechanical adhesion but also for tissue morphogenesis. Protein 4.1B, a member of the protein 4.1 family named from an erythrocyte membrane protein, is a potential organizer of an adherens system. In adult mouse seminiferous tubules, protein 4.1B localized in the basal compartment, especially in the attaching region of spermatogonia and Sertoli cells. Protein 4.1B localization and appearance were not different in each spermatogenic stage. Developmentally, protein 4.1B was not detected at postnatal day 3 (P3), was diffusely localized at P15, and was found in the basal compartment during the third week. By double staining for protein 4.1B and F-actin, their localizations were shown to be different, indicating that protein 4.1B was localized in a region lower than the basal ectoplasmic specialization that formed the Sertoli-Sertoli junction. By electron microscopy, immunoreactive products were seen mainly on the membranes of Sertoli cells. In the W/W(v) mutant mouse, the seminiferous epithelium had few germ cells. Protein 4.1B and beta-catenin were not detected, although the basal ectoplasmic specialization was retained. These results indicate that protein 4.1B may be related to the adhesion between Sertoli cells and germ cells, especially the spermatogonium.
Terada
Nobuo
N
Department of Anatomy, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Tamaho, Japan. nobuot@yamanashi.ac.jp
Ohno
Nobuhiko
N
Yamakawa
Hisashi
H
Baba
Takeshi
T
Fujii
Yasuhisa
Y
Zea
Zagreb
Z
Ohara
Osamu
O
Ohno
Shinichi
S
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D007150:Immunohistochemistry; D008297:Male; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008817:Mice, Mutant Strains; D008856:Microscopy, Fluorescence; D016253:Microscopy, Immunoelectron; D012670:Seminiferous Epithelium / Q000254:growth & development / Q000378:metabolism* / Q000648:ultrastructure; D012708:Sertoli Cells / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism; D051176:beta Catenin
C495267:CTNNB1 protein, mouse; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D015534:Trans-Activators; D051176:beta Catenin; C028841:erythrocyte membrane band 4.1 protein