Ultrastructual studies on maturing spermatids and on sertoli cells in the bandicoot Perameles nasuts Geoffroy (Marsupialia)

1969 ◽  
Vol 17 (2) ◽  
pp. 195 ◽  
Author(s):  
CS Sapsford ◽  
CA Rae ◽  
KW Cleland
Keyword(s):  
Sertoli Cell ◽  
Sertoli Cells ◽  
Neck Region ◽  
Secretory Activity ◽  
Axial Filament ◽  
Middle Piece ◽  
Proximal Extremity ◽  
Nuclear Ring ◽  
Nuclear Rotation ◽  
Cyclic Changes

This paper describes maturation changes in bandicoot spermatids after the latter have become embedded in Sertoli cells and are orientated within the seminiferous tubule. The changes are recorded as taking place in four stages, namely the stage of nuclear flattening and condensation, the stage of nuclear rotation, and the early and late post-rotational stages. The changes in shape and reduction in volume of the nucleus taking place during these stages are described, together with the division of the nuclear contents into condensed chromatin and the less electron-dense parachromatin. The disposition of nuclear pores in relation to the distribution of these two substances is discussed. A possible means of the disposal of redundant nuclear envelope substance is outlined. An account of the modifications taking place in the structures of the neck region is given and it is shown that both transverse and longitudinal centrioles persist until the terminal stages of spermiogenesis, when the latter centriole disappears. As a result of the migration of the annulus and the attached proximal extremity of the cytoplasmic canal, the axial filament complex of the future middle piece is left in contact with the general spermatid cytoplasm, and thus is created a pathway whereby spermatid mitochondria can migrate to this part of the complex to form the mitochondria1 sheath of the middle piece. Details are presented of the changes in form, throughout spermiogenesis, of spermatid mitochondria as well as of the acrosome, manchette, and nuclear ring. A description is given of specialized changes in that part of Sertoli cell cytoplasm immediately adjacent to the spermatid acrosome. It is thought that these changes are indicative, and mark out the extent, of a Sertoli cell-spermatid attachment. Cyclic changes in the overall form as well as in the endoplasmic reticulum and mitochondria of Sertoli cells are recorded. Pinocytotic activity in Sertoli cells and spermatids, as well as secretory activity in Sertoli cells, is examined.

The Cytoplasmic Components of Germ-cells during Spermatogenesis in the Domestic Fowl

1947 ◽  
Vol s3-88 (3) ◽  
pp. 353-366
Author(s):  
I. ZLOTNIK
Keyword(s):  
Germ Cells ◽  
Domestic Fowl ◽  
Posterior Part ◽  
Neck Region ◽  
Axial Filament ◽  
Daughter Cells ◽  
Middle Piece ◽  
Nuclear Ring ◽  
Distal Centriole ◽  
Ultimate Fate

1. The Golgi material of the male germ-cells of the domestic fowl is in the form of a localized body, composed of rods and granules which lie on the surface of the archoplasm. 2. During the maturation divisions the localized Golgi material breaks down and forms a number of granules and rods which become dispersed at the beginning of the metaphase. After each division the scattered Golgi elements reassemble in the daughter cells and become once more attached to the archoplasm. 3. After the formation of the acrosome the Golgi material migrates to the residual cytoplasm and, as the Golgi remnant, is eliminated. 4. Accessory bodies are present in the cytoplasm of the spermatocytes from both silver and chrom-osmium preparations; in the spermatids only argentophil bodies are identified. One argentophil accessory body ‘Golgi X’ is included in the neck region of the spermatozoon. 5. The acrosome is formed from the proacrosome; the latter originates within the archoplasmic vacuole inside the Golgi material of the spermatid. The acrosome occupies the anterior tip of the head of the spermatozoon, and is conical in shape. 6. The nuclear ring is present in the early stages of the metamorphosis of the spermatid; with the elongation of the nucleus it disappears. 7. The mitochondria are described during all the stages of spermatogenesis; their ultimate fate is the formation of the mitochondrial sheath of the middlepiece. This sheath often appears in the form of a spiral structure. 8. During the transformation of the nucleus a coiled stage is constant; this is due to the continuous elongation of the nucleus and lack of response from the cytoplasm. The head of the spermatozoon is an elongate worm-like structure. 9. Two centrioles are present in the spermatids of the domestic fowl. The axial filament originates from the two centrioles. The proximal centriole is attached to the posterior end of the head of the spermatozoon, while the distal centriole assumes the shape of a ring and marks the distal limit of the middlepiece. 10. A clear zone surrounds the posterior part of the nucleus of the late spermatid; this zone possibly takes part in the formation of the middle-piece.

Germ cell-Sertoli cell interactions

1990 ◽  
Vol 2 (3) ◽  
pp. 225 ◽  
Author(s):  
Kretser DM de
Keyword(s):  
Germ Cell ◽  
Sertoli Cell ◽  
Germ Cells ◽  
Sertoli Cells ◽  
Cell Interactions ◽  
Cell Contact ◽  
Paracrine Factors ◽  
Cytological Changes ◽  
Cyclic Changes ◽  
Blood Testis Barrier

The interactions between the Sertoli cells and germ cells are progressively becoming an important part of testicular physiology. This paper explores the cytological basis for these interactions, detailing the cyclic changes in the Sertoli cells in concert with the stages of the seminiferous cycle and the nature of the blood-testis barrier. These cytological changes are correlated with a number of variations in the function of Sertoli cells. The mechanisms by which germ cells and Sertoli cells interact are explored and can be divided into those using cell-to-cell contact and others utilizing paracrine factors.

Ultrastructual studies on spematids and sertoli cells during early spermogenesis in the bandicoot Peramelea nasuta geoffroy (Marsupialia)

1967 ◽  
Vol 15 (5) ◽  
pp. 881 ◽  
Author(s):  
CS Sapsford ◽  
CA Rae ◽  
KW Cleland
Keyword(s):  
Plasma Membrane ◽  
Nuclear Envelope ◽  
Sertoli Cell ◽  
Sertoli Cells ◽  
Close Contact ◽  
Cell Cytoplasm ◽  
Axial Filament ◽  
Stage Of Development ◽  
The Future ◽  
Nuclear Protrusion

The present paper deals with spermiogenesis up to and including the attachment of spermatids to Sertoli cells. The first observed step in spermatid differentiation was the development of the anlage of the middle piece and principal piece. This anlage, called the axial filament complex, has the structure of a cilium and arises from the future longitudinal centriole, while the latter, together with the future transverse centriole, lies in the vicinity of the Golgi complex. The definitive acrosomal vacuole, which ultimately becomes attached to and invaginates the nuclear envelope, is formed by the enlargement and coalescence of Golgi vacuoles. While this definitive vacuole is developing, the centrioles and attached axial filament complex migrate to the opposite pole of the nucleus. Before and during migration a number of accessory structures are developed in association with the centrioles, and one of these structures, the proximal junctional body, invaginates the nuclear envelope when the centrioles reach their definitive abacrosomal position. During this period, a cytoplasmic canal forms around the intraspermatid part of the axial filament complex. The definitive acrosomal vacuole ultimately extends out to make close contact with the plasma membrane of the spermatid. This stage of development is followed by a process of nuclear protrusion, initiated by the migration of the nucleus towards the region of contact between acrosomal vacuole and spermatid plasma membrane. During the migratory phase, that part of the nuclear envelope previously invaginated by the acrosomal vacuole becomes everted and the latter collapses, finally becoming sandwiched in between the nucleus and the plasma membrane of the spermatid. The nucleus subsequently projects from the surface of the spermatid, its acrosome-covered apex becoming coneshaped. During these phases of development the accessory structures elaborated in association with the centrioles, and which now lie in the neck region of the spermatid, have become more highly organized. The manchette begins to develop in spermatids at the stage at which the acrosome has become sandwiched in between the nucleus and the plasma membrane of the spermatid. Concurrently the spermatids become surrounded on all sides by Sertoli cell cytoplasm. In the later stages of nuclear protrusion, the manchette elongates and its walls become thicker. The protruding nuclei become orientated with their acrosome-covered apices facing towards the basement membrane of the tubules. Aggregations of finely granular material appear in Sertoli cell cytoplasm in the region of contact with the acrosomal vacuole. The possible role of the manchette and of Sertoli cell cytoplasm in the phenomenon of nuclear protrusion and orientation is discussed.

Arrangement of Mitochondria in Spermatozoa of the Mexican Axolotl, Ambystoma Mexicanum

1973 ◽  
Vol 31 ◽  
pp. 626-627
Author(s):  
Ezzatollah Keyhani ◽  
Larry F. Lemanski ◽  
Sharon L. Lemanski
Keyword(s):  
Plasma Membrane ◽  
Sperm Motility ◽  
Substrate Oxidation ◽  
Ambystoma Mexicanum ◽  
Axial Filament ◽  
Mexican Axolotl ◽  
Middle Piece

Energy for sperm motility is provided by both glycolytic and respiratory pathways. Mitochondria are involved in the latter pathway and conserve energy of substrate oxidation by coupling to phosphorylation. During spermatogenesis, the mitochondria undergo extensive transformation which in many species leads to the formation of a nebemkem. The nebemkem subsequently forms into a helix around the axial filament complex in the middle piece of spermatozoa.Immature spermatozoa of axolotls contain numerous small spherical mitochondria which are randomly distributed throughout the cytoplasm (Fig. 1). As maturation progresses, the mitochondria appear to migrate to the middle piece region where they become tightly packed to form a crystalline-like sheath. The cytoplasm in this region is no longer abundant (Fig. 2) and the plasma membrane is now closely apposed to the outside of the mitochondrial layer.

Freeze-etch observations on the tight junctions of sertoli cells grown in organ culture with FSH

1978 ◽  
Vol 36 (2) ◽  
pp. 340-341
Author(s):  
Rita Meyer ◽  
Zoltan Posalaky ◽  
Dennis Mcginley
Keyword(s):  
Organ Culture ◽  
Tight Junctions ◽  
Sertoli Cell ◽  
Germ Cells ◽  
Sertoli Cells ◽  
Barrier Function ◽  
Cell Junction ◽  
Intramembranous Particles ◽  
Junctional Complexes ◽  
Oriented Parallel

The Sertoli cell tight junctional complexes have been shown to be the most important structural counterpart of the physiological blood-testis barrier. In freeze etch replicas they consist of extensive rows of intramembranous particles which are not only oriented parallel to one another, but to the myoid layer as well. Thus the occluding complex has both an internal and an overall orientation. However, this overall orientation to the myoid layer does not seem to be necessary to its barrier function. The 20 day old rat has extensive parallel tight junctions which are not oriented with respect to the myoid layer, and yet they are inpenetrable by lanthanum. The mechanism(s) for the control of Sertoli cell junction development and orientation has not been established, although such factors as the presence or absence of germ cells, and/or hormones, especially FSH have been implicated.

Effect of nitric oxide on Sertoli cell microtubule of piglets

2009 ◽  
Vol 6 (3) ◽  
pp. 257-263 ◽  
Author(s):  
Yang Li ◽  
Wang Xian-zhong ◽  
Yang Meng-bo ◽  
Zhang Jia-hua
Keyword(s):  
Nitric Oxide ◽  
Enzyme Activity ◽  
Protein Kinase ◽  
Cell Viability ◽  
Sodium Nitroprusside ◽  
Sertoli Cell ◽  
Sertoli Cells ◽  
High Concentration ◽  
Treatment Results ◽  
Anti Oxidant

AbstractTo illustrate the effect of nitric oxide (NO) on the microtubules of Sertoli cells (SC), SCs of piglets were treated with sodium nitroprusside (SNP). Changes in cell viability, anti-oxidant activity, enzyme activity and p38 mutagen-activated protein kinase (p38MAPK) activation were detected. The results were as follows. A low concentration of NO can keep SC microtubule and cell viability normal, and a high concentration of NO could increase p38MAPK activation, decrease anti-oxidant activity and transferrin secretion, and destroy the structure and distribution of the microtubules. The results suggest that SNP treatment results in an increase in NO in SCs and decreased cell anti-oxidant activity. The high concentration of NO destroys cell microtubules by activating p38MAPK.

Sertoli cell expression of the cystic fibrosis transmembrane conductance regulator

1998 ◽  
Vol 274 (4) ◽  
pp. C922-C930 ◽  
Author(s):  
Fredric R. Boockfor ◽  
Rebecca A. Morris ◽  
Dennis C. DeSimone ◽  
D. Margaret Hunt ◽  
Kenneth B. Walsh
Keyword(s):  
Cystic Fibrosis ◽  
Sertoli Cell ◽  
Sertoli Cells ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Patch Clamp Technique ◽  
Immunoreactive Material ◽  
Normal Spermatogenesis ◽  
Cell Expression ◽  
Cystic Fibrosis Transmembrane

Mutations of the cystic fibrosis transmembrane conductance regulator (CFTR) gene have been associated with a number of male reproductive problems, including testis abnormalities and a reduction in germ cell quality and number. To establish at least one site of functional CFTR expression in the testis, we subjected cultured Sertoli cells to analysis of message, protein, and channel activity for CFTR. With reverse transcription-polymerase chain reaction, we obtained evidence for the presence of CFTR RNA when CFTR primers were used with RNA from cultured Sertoli cells. Western analysis performed with both anti-R and anti-C domain CFTR antibodies revealed immunoreactive material in extracts from primary Sertoli cell cultures that seemed consistent with CFTR previously identified in other cells and tissues. This led us to perform more detailed studies using the whole cell arrangement of the patch-clamp technique. Application of the membrane-soluble cAMP analog, 8-chlorophenylthio-cAMP, resulted in the activation of a Cl− current that displayed a permeability sequence of Br− > I− ≥ Cl− and was blocked by diphenylamine-2-carboxylate and glibenclamide. In addition, a 13-pS conductance Cl− channel was measured in excised membrane patches exposed to the catalytic subunit of protein kinase A. When taken together, our findings of evidence of CFTR message, immunoreactive material that appeared consistent with CFTR, and Cl− channels with properties similar to those reported for CFTR provide strong evidence that Sertoli cells express a functional CFTR-like protein. The presence of CFTR in these cells may be needed to maintain the specific nutritional and fluid balance in the seminiferous tubule that is vital for normal spermatogenesis.

scholarly journals Ezrin is an Actin Binding Protein That Regulates Sertoli Cell and Spermatid Adhesion During Spermatogenesis

Endocrinology ◽  
2014 ◽  
Vol 155 (10) ◽  
pp. 3981-3995 ◽  
Author(s):  
N. Ece Gungor-Ordueri ◽  
Elizabeth I. Tang ◽  
Ciler Celik-Ozenci ◽  
C. Yan Cheng
Keyword(s):  
Sertoli Cell ◽  
Sertoli Cells ◽  
Adherens Junction ◽  
Actin Binding ◽  
Permeability Barrier ◽  
Tight Junction Permeability ◽  
Residual Bodies ◽  
Cell Interface

Abstract During spermatogenesis, the transport of spermatids and the release of sperms at spermiation and the remodeling of the blood-testis barrier (BTB) in the seminiferous epithelium of rat testes require rapid reorganization of the actin-based cytoskeleton. However, the mechanism(s) and the regulatory molecule(s) remain unexplored. Herein we report findings that unfold the functional significance of ezrin in the organization of the testis-specific adherens junction at the spermatid-Sertoli cell interface called apical ectoplasmic specialization (ES) in the adluminal compartment and the Sertoli cell-cell interface known as basal ES at the BTB. Ezrin is expressed at the basal ES/BTB in all stages, except from late VIII to IX, of the epithelial cycle. Its knockdown by RNA interference (RNAi) in vitro perturbs the Sertoli cell tight junction-permeability barrier via a disruption of the actin microfilaments in Sertoli cells, which in turn impeded basal ES protein (eg, N-cadherin) distribution, perturbing the BTB function. These findings were confirmed by a knockdown study in vivo. However, the expression of ezrin at the apical ES is restricted to stage VIII of the cycle and limited only between step 19 spermatids and Sertoli cells. A knockdown of ezrin in vivo by RNAi was found to impede spermatid transport, causing defects in spermiation in which spermatids were embedded deep inside the epithelium, and associated with a loss of spermatid polarity. Also, ezrin was associated with residual bodies and phagosomes, and its knockdown by RNAi in the testis also impeded the transport of residual bodies/phagosomes from the apical to the basal compartment. In summary, ezrin is involved in regulating actin microfilament organization at the ES in rat testes.

Expression and localization of androgen receptor-interacting protein-4 in the testis

2007 ◽  
Vol 292 (2) ◽  
pp. E513-E522 ◽  
Author(s):  
Andrii Domanskyi ◽  
Fu-Ping Zhang ◽  
Mirja Nurmio ◽  
Jorma J. Palvimo ◽  
Jorma Toppari ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Sertoli Cell ◽  
Germ Cells ◽  
Sertoli Cells ◽  
Hormone Receptor ◽  
Luteinizing Hormone Receptor ◽  
Dependent Manner ◽  
Cell Nuclei ◽  
Interacting Protein ◽  
Independent Functions

Androgen receptor-interacting protein 4 (ARIP4) belongs to the SNF2 family of proteins involved in chromatin remodeling, DNA excision repair, and homologous recombination. It is a DNA-dependent ATPase, binds to DNA and mononucleosomes, and interacts with androgen receptor (AR) and modulates AR-dependent transactivation. We have examined in this study the expression and cellular localization of ARIP4 during postnatal development of mouse testis. ARIP4 was detected by immunohistochemistry in Sertoli cell nuclei at all ages studied, starting on day 5, and exhibited the highest expression level in adult mice. At the onset of spermatogenesis, ARIP4 expression became evident in spermatogonia, pachytene, and diplotene spermatocytes. Immunoreactive ARIP4 antigen was present in Leydig cell nuclei. In Sertoli cells ARIP4 was expressed in a stage-dependent manner, with high expression levels at stages II–VI and VII–VIII. ARIP4 expression patterns did not differ significantly in testes of wild-type, follicle-stimulating hormone receptor knockout, and luteinizing hormone receptor knockout mice. In testes of hypogonadal mice, ARIP4 was found mainly in interstitial cells and exhibited lower expression in Sertoli and germ cells. In vitro stimulation of rat seminiferous tubule segments with testosterone, FSH, or forskolin did not significantly change stage-specific levels of ARIP4 mRNA. Heterozygous ARIP4+/− mice were haploinsufficient and had reduced levels of Sertoli-cell specific androgen-regulated Rhox5 (also called Pem) mRNA. Collectively, ARIP4 is an AR coregulator in Sertoli cells in vivo, but the expression in the germ cells implies that it has also AR-independent functions in spermatogenesis.

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