The chromomere map of the pachytene spermatocyte of the Turkish hamster (Mesocricetus brandti)

Genome ◽  
1991 ◽  
Vol 34 (4) ◽  
pp. 626-630 ◽  
Author(s):  
Jye-Siung Fang ◽  
Georgiana M. Jagiello
Keyword(s):  
Pachytene Spermatocyte ◽  
Pachytene Spermatocytes ◽  
Turkish Hamster

The chromomere map of the early to mid pachytene spermatocyte of the Turkish hamster (Mesocricetus brandti) is described. Each autosomal bivalent was identified and a total of 304 chromomeres was found. A sex bivalent with a despiralized Xq protruding from the sex vesicle and a small number of the polymorphic 16q bivalents were observed.Key words: Turkish hamster, chromomere maps, pachytene spermatocytes.

scholarly journals Synaptonemal complexes are integral components of the isolated mouse spermatocyte nuclear matrix.

1983 ◽  
Vol 96 (6) ◽  
pp. 1717-1726 ◽  
Author(s):  
L A Ierardi ◽  
S B Moss ◽  
A R Bellvé
Keyword(s):  
Nuclear Matrix ◽  
Central Element ◽  
Rnase A ◽  
Pachytene Spermatocyte ◽  
Fiber Network ◽  
Synaptonemal Complexes ◽  
The Matrix ◽  
Electron Microscopes ◽  
Pachytene Spermatocytes ◽  
A Minor

Synaptonemal complexes (SCs) have been isolated as integral components of the nuclear matrix from purified mouse pachytene spermatocytes. These nuclear synaptonemal complex-matrices are prepared by extracting Triton X-100-treated nuclei with low (0.2 M) and high (1.0 or 2.0 M) NaCl, DNase I, and RNase A to remove 85% of the nuclear proteins, 97% of the RNA, and 99% of the DNA. Studies with the light and electron microscopes indicate that these matrices, while lacking a distinct lamina, contain nuclear pores interconnected by a fiber network, residual nucleoli, and interchromatin fibers. In addition, the pachytene spermatocyte matrices contain residual XY heterochromatin and the principal components of the SCs, including two lateral elements, a central element, a presumptive centromere, and attachment plaques. These SCs are preserved within the matrix and retain their structural association with the pore-fiber complex, even when subjected to strong dissociating conditions. Nuclear matrices from pachytene spermatocytes and spermatids (steps 1-8), when analyzed by SDS PAGE, contain an array of polypeptides distinct from those of mouse liver nuclear matrices. Proteins of spermatogenic matrices range in Mr from 8,000 to approximately 150,000. The prominent lamina proteins (Mr approximately 60,000-70,000) of somatic nuclear matrices are either absent or represent only a minor part of the spermatogenic matrix. The polypeptide composition of the pachytene spermatocyte and spermatid matrices are similar, although minor quantitative and qualitative differences are evident. These observations suggest that the SC constituents may consist of a heterogeneous group of proteins present in low proportion relative to total matrix proteins, or they may be retained, but in a different form, within the spermatid matrix.

scholarly journals Pachytene spermatocyte and round spermatid binding to Sertoli cells in vitro

1988 ◽  
Vol 90 (1) ◽  
pp. 105-114
Author(s):  
G.C. Enders ◽  
C.F. Millette
Keyword(s):  
Sertoli Cell ◽  
Sertoli Cells ◽  
Round Spermatid ◽  
Pachytene Spermatocyte ◽  
Assay System ◽  
Spermatogenic Cells ◽  
Vitro Assay ◽  
Cell Monolayers ◽  
Pachytene Spermatocytes

Spermatogenic cells differentiate in vivo while in continuous contact with the Sertoli cell. During differentiation, the spermatogenic cells and Sertoli cells form a number of morphologically distinct stage-specific adhesions. We describe an in vitro assay system for studying the adhesion of spermatogenic cells to Sertoli cell monolayers. Mixed populations of spermatogenic cells or enriched fractions of pachytene spermatocytes and round spermatids were labelled with the vital dye, fluorescein diacetate, prior to their addition to Sertoli cell monolayers so that the adhesion of viable spermatogenic cells could be quantified. Using this assay system, the number of pachytene spermatocyte and round spermatid binding sites on the Sertoli cell monolayer were similar, but the kinetics of binding were different. Pachytene spermatocytes were able to inhibit significantly round spermatid binding, while round spermatids did not significantly inhibit pachytene spermatocyte binding. After coculture for 24–48 h, spermatocytes form junctional structures with Sertoli cells that are similar to desmosome-like junctions. These results suggest that pachytene spermatocytes and round spermatids bind to Sertoli cells by different mechanisms.

scholarly journals Adenine nucleotide translocase 4 deficiency leads to early meiotic arrest of murine male germ cells

Reproduction ◽  
2009 ◽  
Vol 138 (3) ◽  
pp. 463-470 ◽  
Author(s):  
Jeffrey V Brower ◽  
Chae Ho Lim ◽  
Marda Jorgensen ◽  
S Paul Oh ◽  
Naohiro Terada
Keyword(s):  
Adenine Nucleotide ◽  
Strand Break ◽  
Pachytene Spermatocyte ◽  
Inner Mitochondrial Membrane ◽  
Meiotic Arrest ◽  
Atp Production ◽  
Dna Double Strand Break ◽  
Complex Protein ◽  
Synaptonemal Complex Protein ◽  
Pachytene Spermatocytes

Male fertility relies on the highly specialized process of spermatogenesis to continually renew the supply of spermatozoa necessary for reproduction. Central to this unique process is meiosis that is responsible for the production of haploid spermatozoa as well as for generating genetic diversity. During meiosis I, there is a dramatic increase in the number of mitochondria present within the developing spermatocytes, suggesting an increased necessity for ATP production and utilization. Essential for the utilization of ATP is the translocation of ADP and ATP across the inner mitochondrial membrane, which is mediated by the adenine nucleotide translocases (Ant). We recently identified and characterized a novel testis specific Ant, ANT4 (also known as SLC25A31 and Aac4). The generation ofAnt4-deficient animals resulted in the severe disruption of the seminiferous epithelium with an apparent spermatocytic arrest of the germ cell population. In the present study utilizing a chromosomal spread technique, we determined thatAnt4-deficiency results in an accumulation of leptotene spermatocytes, a decrease in pachytene spermatocytes, and an absence of diplotene spermatocytes, indicating early meiotic arrest. Furthermore, the chromosomes ofAnt4-deficient pachytene spermatocyte occasionally demonstrated sustained γH2AX association as well as synaptonemal complex protein 1 (SYCP1)/SYCP3 dissociation beyond the sex body. Large ATP supplies from mitochondria may be critical for normal progression of spermatogenesis during early stages of meiotic prophase I, including DNA double-strand break repair and chromosomal synapsis.

Increased Expression of Estrogen Receptor β in Pachytene Spermatocytes After Short-Term Methoxyacetic Acid Administration

2004 ◽  
Vol 25 (1) ◽  
pp. 84-94 ◽  
Author(s):  
Oscar M. Tirado ◽  
David M. Selva ◽  
Núria Toràn ◽  
Carlos A. Suárez-Quian ◽  
Michelle Jansen ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Β ◽  
Short Term ◽  
Methoxyacetic Acid ◽  
Pachytene Spermatocytes ◽  
Acid Administration

Circadian organization of locomotor activity in the Turkish hamster (Mesocricetus brandti)

1983 ◽  
Vol 37 (2) ◽  
pp. 362-366 ◽  
Author(s):  
H. Elliott Albers ◽  
Dennis S. Carter ◽  
Janet M. Darrow ◽  
Bruce D. Goldman
Keyword(s):  
Locomotor Activity ◽  
Circadian Organization ◽  
Turkish Hamster

scholarly journals Dynamics of intracellular calcium induced by lactate and glucose in rat pachytene spermatocytes and round spermatids

Reproduction ◽  
2002 ◽  
pp. 701-710 ◽  
Author(s):  
JG Reyes ◽  
E Herrera ◽  
L Lobos ◽  
K Salas ◽  
N Lagos ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Carbohydrate Metabolism ◽  
Adenine Nucleotides ◽  
Differential Modulation ◽  
Glycolytic Metabolism ◽  
Spermatogenic Cells ◽  
Lactate Metabolism ◽  
The Media ◽  
Hexose Phosphorylation ◽  
Pachytene Spermatocytes

Glycolytic metabolism in meiotic and post-meiotic spermatogenic cells shows differentiation-related changes. The developmental and physiological significance of these metabolic changes is not known. The aim of the present study was to test the hypothesis that glucose and lactate metabolism can modulate intracellular calcium [Ca2+](i) in spermatogenic cells in an opposing and dynamic manner. Fluorescent probes were used to measure [Ca2+](i) and pH(i), and HPLC was used to measure intracellular adenine nucleotides and mitochondrial sensing of ATP turnover. [Ca2+](i) in pachytene spermatocytes and round spermatids was modulated by changes in lactate and glucose concentrations in the media. The kinetics and magnitude of the [Ca2+](i) changes induced by lactate and glucose were different in meiotic and post-meiotic spermatogenic cells. The presence of glucose in the medium induced a decrease in pH(i) in spermatogenic cells. This glucose-induced pH(i) decrease occurred later than the changes in [Ca2+](i), which were also observed when the pH(i) decrease was inhibited, indicating that the glucose-induced [Ca2+](i) increase was not a consequence of pH(i) changes. Hexose phosphorylation in glycolysis was part of the mechanism by which glucose metabolism induced a [Ca2+](i) increase in spermatogenic cells. The sensitivity of [Ca2+](i) to carbohydrate metabolism was higher in round spermatids than in pachytene spermatocytes. Thus, differentiation-related changes in carbohydrate metabolism in spermatogenic cells determine a dynamic and differential modulation of their [Ca2+](i) by glucose and lactate, two substrates secreted by the Sertoli cells.

Developmentally regulated expression of a human "finger"-containing gene encoded by the 5' half of the ret transforming gene

1988 ◽  
Vol 8 (4) ◽  
pp. 1853-1856
Author(s):  
M Takahashi ◽  
Y Inaguma ◽  
H Hiai ◽  
F Hirose
Keyword(s):  
Human Gene ◽  
Mrna Levels ◽  
Nucleic Acid Binding ◽  
Developmentally Regulated ◽  
Unique Transcript ◽  
Binding Domains ◽  
Regulated Expression ◽  
Pachytene Spermatocytes ◽  
Human Finger ◽  
Transforming Gene

We isolated and sequenced a cDNA clone of the human gene encoded by the 5' half of the ret transforming gene. The nucleotide sequence indicates that it encodes a protein with "finger" structures which represent putative metal- and nucleic acid-binding domains. Transcription of this gene was detected at high levels in a variety of human and rodent tumor cell lines, mouse testis, and embryos. In addition, a unique transcript was observed in testis RNA. When the expression of the unique transcript was examined at different stages of spermatogenesis, a striking increase in mRNA levels accompanied progression from meiotic prophase pachytene spermatocytes to postmeiotic round spermatids. This finger-containing gene may thus function in male germ cell development.

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