A freeze-etching study of rabbit spermatozoa with particular reference to head structures

Koehler, James K.

doi:10.1016/s0022-5320(70)90184-x

Cited by 121 publications

(51 citation statements)

References 14 publications

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“…Ordered arrays of particles have previously been observed in the acrosomal region of the head of rabbit (9,10) and human (11) (15), redistribution of label is not a likely explanation for the regional representation of H-Y antigen observed because the secondary antibody and marker were added at low temperature. It will be important to determine whether other sperm-surface antigens are also regionally represented, and if so, whether they are also confined to the acrosomal cap or are present in other regions.…”

Section: Discussionmentioning

confidence: 89%

Topographical Location of H—Y Antigen on Mouse Spermatozoa by Immunoelectronmicroscopy

Koo

Stackpole

Boyse

et al. 1973

Proc. Natl. Acad. Sci. U.S.A.

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H-Y (male) antigen was visually located on mouse sperm by electron microscopy, by use of the indirect hybrid antibody method and tobacco mosaic virus as the visual marker. Labeling was achieved by centrifugation of the sperm through a discontinuous gradient consisting of alternating layers of immune reagents and wash solutions. Treated sperm were examined topographically by preparation of platinum-carbon replicas. Antigen was located mainly on the acrosomal cap of the sperm head.

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Section: Discussionmentioning

confidence: 89%

Topographical Location of H—Y Antigen on Mouse Spermatozoa by Immunoelectronmicroscopy

Koo

Stackpole

Boyse

et al. 1973

Proc. Natl. Acad. Sci. U.S.A.

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“…In vivo, protamine can fix the chromatin structure, whatever the step at which it is introduced to nuclei and whatever the previous local arrangement of chromatin (Courtens, 1982;Biggiogera et al, 1992). The fact that TP1 is located at the periphery of threads, and seems to remain in that place, forming longitudinal decorations in older spermatids, may indicate that it is involved in the formation of the chromatin plates which are present in old spermatids and spermatozoa (Koehler, 1970;Courtens et al, 1991 This raises the question of how it is eliminated, meaning separation from the DNA and release from the dense chromatin. Separation of TP1 from the DNA is probably not due to displacement by protamine as postulated by Green et al (1994), because both nucleoproteins are present together in nuclei for several days during rabbit spermiogenesis and because their immunolocalisations do not overlap.…”

Section: Rabbit-specific Morphological Datamentioning

confidence: 99%

Ultrastructural immunolocalisation of histones (H2B, H3, H4), transition protein (TP1) and protamine in rabbit spermatids and spermatozoa nuclei. Relation to condensation of the chromatin

Courtens¹,

Ws²,

Plöen³

1995

Reprod. Nutr. Dev.

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Summary ― The histones H2B, H3 and H4, the transition protein TP1 and protamine were localised using ultrastructural immunocytochemistry in nuclei of rabbit spermatids and spermatozoa. Histones are present in round spermatid nuclei and are lost during the elongation of nuclei. TP1 and protamine appear simultaneously in all nuclei during this period. TP1 is located at the periphery of chromatin cords, while protamine seems to be located at random in the same cords. TP1 is lost in most elongated spermatids during step 13 of spermiogenesis, and the protamine stays in all sperm nuclei. TP1 remains present in some old spermatids and ejaculated spermatozoa. In the rabbit, 3-6% of sperm nuclei decondense spontaneously.

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“…1, Fig. 4) which can also be seen sometimes in chemically fixed spermatozoa (Koehler, 1970). The tail membranes appeared similar to those of the head region, while the plasma membrane of the middle piece showed a relief corresponding to the underlying mitochondrial chain (PI.…”

Section: Methodsmentioning

confidence: 64%

“…2). 'Striations' were clearly visible on the posterior parts of the head membrane (Koehler, 1965(Koehler, ,1970Plattner, 1971), but there were striking differences between bull and boar spermatozoa in the appearance, extension and amount of'striation' (PI. 1, Figs 2 and 3).…”

Section: Methodsmentioning

confidence: 99%

“…The fine structure of spermatozoa has been investigated primarily after chemical fixation (Blom & Birch-Anderson, 1960,1965Saacke & Almquist, 1964a, b;Hancock, 1966;Nicander & Bane, 1966;Fawcett, 1970) or freeze-etching (Koehler, 1966(Koehler, , 1970. In both techniques cellular components are variably altered by the fixatives, the dehydration media or the cryoprotective agents.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A comparison of the ultrastructure of spray-frozen and freeze-etched or freeze-dried bull and boar spermatozoa with that after chemical fixation

Pfaller¹,

Rovan²,

Mairbäurl³

1976

Reproduction

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Summary. The ultrastructure of bull and boar spermatozoa was investigated following different cryopreparation methods and chemical fixation. Spray-freezing was used for cryofixation in both freeze-etching and freeze-drying studies. Freeze-etching of boar spermatozoa revealed that the arrangement of the postnuclear striations differed from that in the bull. Freeze-drying gave excellent results for structural preservation, which were equal to those of chemical fixation. Some structural details not visible in chemically fixed cells were detected in freeze-dried and vacuum-embedded bull and boar spermatozoa, e.g. the arrangement of the lamellar nuclear contents, known from freeze\x=req-\ fractures, and a fine lamellar structure of the acrosomal contents. Cryofixation by spray-freezing combined with freeze-drying makes any contact of the cells with fixatives, buffer solutions and dehydration media unnecessary, and potentially provides all the advantages of ultrathin sectioning required for histochemical studies.

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A freeze-etching study of rabbit spermatozoa with particular reference to head structures

Cited by 121 publications

References 14 publications

Topographical Location of H—Y Antigen on Mouse Spermatozoa by Immunoelectronmicroscopy

Topographical Location of H—Y Antigen on Mouse Spermatozoa by Immunoelectronmicroscopy

Ultrastructural immunolocalisation of histones (H2B, H3, H4), transition protein (TP1) and protamine in rabbit spermatids and spermatozoa nuclei. Relation to condensation of the chromatin

A comparison of the ultrastructure of spray-frozen and freeze-etched or freeze-dried bull and boar spermatozoa with that after chemical fixation

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