Labelling of membrane glycoproteins on rat spermatozoa collected from different regions of the epididymis

Jones, Roy; Pholpramool, Chumpol; Setchell, B. P.; Brown, Colin

doi:10.1042/bj2000457

Cited by 67 publications

(26 citation statements)

References 14 publications

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“…A llOK component is the major surface glycoprotein of rat testicular spermatozoa labeled with the glucose oxidase-tritium borohydride technique, but it is not labeled on cauda epididymal spermatozoa by this procedure (Jones et al, 1981a;Brown et al, 1983). Also, lactoperoxidase-catalyzed iodination studies indicated that rat caput epididymidal sperm have surface components of 94K, 72K, and 59K, which are not iodinated on cauda sperm (Olson and Danzo, 1981).…”

Section: Sperm Surface Components Are Altered During Epididymal Maturmentioning

confidence: 99%

Immunodissection of sperm surface modifications during epididymal maturation

et al. 1985

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Mammalian spermatozoa undergo changes in morphology, composition, and function during transit through the epididymis. These changes correlate with acquisition by sperm of the ability to fertilize ova. It has been found that sperm from the cauda epididymidis, but not those from the caput epididymidis, are able to bind to the zona pellucida. This would imply a modification in sperm surface characteristics. Biochemical and immunological studies have demonstrated changes in sperm surface composition during epididymal maturation. These changes involve addition of epididymal secretory products to the sperm surface, loss or alteration of existing sperm surface molecules, and possibly the unmasking of preexisting molecules or epitopes. Several laboratories have studied the epididymal secretory proteins in the rat, but a consensus has not been reached on the identification, characterization, source, and sperm surface association of these proteins. Monoclonal antibodies are beginning to be used to characterize sperm surface components and sperm maturation antigens. They are proving to be valuable tools for the dissection of epididymal maturation when used in conjunction with biochemical and physiological approaches.

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Section: Sperm Surface Components Are Altered During Epididymal Maturmentioning

confidence: 99%

Immunodissection of sperm surface modifications during epididymal maturation

et al. 1985

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“…Radiolabeled MT used in this study has the native conformation conserved as much as possible and reacts with the MT antibody which recognizes the N112-terminal . During the maturation of spermatozoa in the epididymis, it is well known that many proteins are adsorbed to the cell membrane (Faye et al 1980;Jones et al 1981). The binding site of MT is of course not known, but this result suggested that MT binding to the spermatozoa is mainly a nonspecific form and partly a specific form.…”

Section: Discussionmentioning

confidence: 99%

Binding of Metallothionein to Rat Spermatozoa.

Suzuki

Nakajima

Yamamoto

et al. 1994

Tohoku J. Exp. Med.

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Binding studies of metallothionein and rat spermatozoa were performed using 125I-Tyr-metallothionein (1251-MT). Reactions between 1251-MT and spermatozoa indicated that MT bound in two forms , namely, middle affinity (Kdl=2 x 10-9 M) binding and low affinity (Kd2=1 x 10_8 M) binding. Labeled MT binding to spermatozoa was inhibited by adding anti-MT antibody. Total binding reactions of MT were temperature and incubation time dependent. By transmission electron microscopy using a gold conjugate (indirect method), gold particles bound to MT were shown to bind to the cell membrane of the head and the proximal portion of the tail. By optical autoradiography, grains of labeled MT were localized mainly in the head and the proximal portion of the tail. By electron microscopical autoradiography, grains of labeled MT were identified mainly in the cell membrane of the head and tail and partly in the nucleus. These results suggest that MT has both specific and non-specific binding sites on the spermatozoal membrane. metallothionein (MT); spermatozoa; autoradiography; transmission electron microscopy Metallothionein (MT) is a metal-binding protein with a low molecular weight of approximately 6,000 and with high cysteine and sulfur content (Margoshes and Vallee 1957). It has been identified in a variety of organs, including the prostate (Waalkes et al. 1982;Bataineh et al. 1986;Umeyama et al. 1987;Suzuki et al. 1991), and binds class II-B metals, such as cadmium and zinc. Zinc is concentrated in the prostatic tissue and secreted into prostatic fluid (Mawson and Fisher

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“…Rat CD52, previously named the 'major maturation-associated sperm membrane antigen' (Zeheb and Orr, 1984;Moore et al, 1989), an approximately 26 kDa protein (Myles, 1993), and sperm membrane glycoprotein (SmemG) (Eccleston et al, 1994) may be an example of such a glycoprotein. Rat CD52 was originally identified as the principal molecule labelled by surface carbohydrate-labelling experiments using intact mature spermatozoa from the cauda epididymidis (Olson and Hamilton, 1978;Jones et al, 1981;Brown et al, 1983;Zeheb and Orr, 1984;Hamilton et al, 1986;Olson et al, 1987;Moore et al, 1989;Eccleston et al, 1994). Furthermore, carbohydrate labelling of rat sperm glycoproteins on western blots in vitro (Pera et al, 1997) showed an unexpectedly high selectivity: the only molecule accessible to the periodate oxidation reaction was the counterpart of CD52.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and glycosylation of CD52, the major 'maturation-associated' antigen of rat spermatozoa, in the cauda epididymidis

Derr¹

2001

Reproduction

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Labelling of membrane glycoproteins on rat spermatozoa collected from different regions of the epididymis

Cited by 67 publications

References 14 publications

Immunodissection of sperm surface modifications during epididymal maturation

Immunodissection of sperm surface modifications during epididymal maturation

Binding of Metallothionein to Rat Spermatozoa.

Synthesis and glycosylation of CD52, the major 'maturation-associated' antigen of rat spermatozoa, in the cauda epididymidis

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