Spectrin and ankyrin like proteins in spermatids and spermatozoa of the hamster and some other mammals

Abstract

Summary ― The presence of spectrin and ankyrin-like proteins was investigated during the differentiation and maturation of spermatozoa in mammalian species which have previously been studied for actin and calmodulin. These actin-binding proteins were characterized by immunoblotting and localized by immunoelectron microscopy. Neither spectrin nor ankyrin could be detected in the F-actin rich subacrosomal layer of spermatids in any species. In hamster and mouse maturing spermatids and spermatozoa, spectrin was mainly evidenced around the fibrous sheath of the flagellum whereas ankyrin was detected only in the neck. In rabbit spermatozoa, spectrin was evidenced in the outermost cytoplasmic layer of the post-acrosomal region and a light ankyrin labeling appeared in the neck. In rat, monkey and human sperm cells, these 2 proteins were not demonstrated. These results showed that as for actin there was no uniform pattern of distribution of spectrin and ankyrin among the 6 species studied.

Actin, α‐actinin, and spectrin with specific associations with the postacrosomal and acrosomal domains of bovine spermatozoa

“…However, according to Kann et al (1993) the acrosomal cap of human, monkey, and rabbit spermatozoa is devoid of spectrin. In light of the ultrastructure of the present bovine acrosome, the vesiculating cytoskeletal domains apparently are associated with the acrosomal lamina.…”

“…A rigid postacrosomal sheath is a putative site for actin in a number of mammalian spermatozoa (Clarke and Yanagimachi, 1978;Tamblyn, 1980;Clarke et al, 1982;Flaherty et al, 1986Flaherty et al, , 1988Yagi and Paranko, 1992), where it may interact with actin-binding proteins such as spectrin (Kann et al, 1993) and a group of basic proteins including calicin and multiple band proteins (Longo et al, 1987;Paranko et al, 19881, and with less well identified silver binding proteins (Yagi and Paranko, 1994).…”

“…The biological role of nonfilamentous actin (Virtanen et al, 1984;Flaherty et al, 1988;Yagi and Paranko, 1992), tropomyosin, a-actinin (Yagi and Paranko, 19921, myosin (Virtanen et al, 1984), and ankyrin (Kann et al, 1993) in the sperm Reduced labeling is seen in principal piece (P) of the MgC1,-extracted spermatozoa. f,f': Sonicated spermatozoa show staining in the neck (N) and in the fragments of the principal piece (P).…”

Perinuclear theca during spermatozoa maturation leading to fertilization

“…Kann et al (1993) Antigen AJ-p90 This antigen was detected with the monoclonal antibody LH43, which had been originally raised against single cell human keratinocytes (Jassim et al, 1993). Using indirect immunofluorescence microscopy, the LH43 antibody stained the acrosomal zone of ejaculated, epididymal, and testicular spermatozoa.…”

Calpain modulates capacitation and acrosome reaction through cleavage of the spectrin cytoskeleton

“…Diverse cytoskeletal proteins have been found to be associated with these membrane domains, for instance F-actin (Castellani-Ceresa et al 1992, Moreno-Fierros et al 1992, Kann et al 1993, Spungin et al 1995, Yagi & Paranko 1995, spectrin (Virtanen et al 1984, Camatini et al 1991, HernandezGonzalez et al 2000, as well as dystrophin and utrophin (Hernandez-Gonzalez et al 2001. Interestingly, because F-actin and spectrin form a network associated with the plasma and outer acrosomal membranes (Hernandez-Gonzalez et al 2000) that may act as a physical barrier preventing membrane fusion (Spungin et al 1995, Hernandez-Gonzalez et al 2000, remodeling of the cortical actin cytoskeleton could facilitate capacitation and AR (Brener et al 2003, Cabello-Agueros et al 2003.…”