Glycogen metabolism in human fetal testes
TL;DR: The ontogeny of glycogen synthetase, glycogen Phosphorylase and α-D-glucosidase, enzymes which are associated with glycogen metabolism and glycogen level has been studied in human fetal testes of gestational age ranging from 14–32 weeks.
Abstract: The ontogeny of glycogen synthetase, glycogen Phosphorylase and α-D-glucosidase, enzymes which are associated with glycogen metabolism and glycogen level has been studied in human fetal testes of gestational age ranging from 14–32 weeks. Glycogen synthetase activity reaches the peak value at 17–20 weeks of gestation, thereafter it decreases. α-D-Glucosidase activity increases with the advancement of pregnancy up to 28 weeks of gestation decreasing thereafter very rapidly. Phosphorylase activity remains more or less constant throughout gestation. The maximum increase in glycogen content at early stages of gestation (17–20 weeks) and gradual reduction with the advancement of pregnancy are correlated with histochemical observation by the periodic acid-Schiff technique.
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TL;DR: It is suggested that GS activity and glycogen synthesis in testis could be regulated and a disruption of this process may be responsible for the apoptosis and degeneration of seminiferous tubules and possible cause of infertility.
Abstract: Glycogen is the main source of glucose for many biological events. However, this molecule may have other functions, including those that have deleterious effects on cells. The rate-limiting enzyme in glycogen synthesis is glycogen synthase (GS). It is encoded by two genes, GYS1, expressed in muscle (muscle glycogen synthase, MGS) and other tissues, and GYS2, primarily expressed in liver (liver glycogen synthase, LGS). Expression of GS and its activity have been widely studied in many tissues. To date, it is not clear which GS isoform is responsible for glycogen synthesis and the role of glycogen in testis. Using RT-PCR, Western blot and immunofluorescence, we have detected expression of MGS but not LGS in mice testis during development. We have also evaluated GS activity and glycogen storage at different days after birth and we show that both GS activity and levels of glycogen are higher during the first days of development. Using RT-PCR, we have also shown that malin and laforin are expressed in testis, key enzymes for regulation of GS activity. These proteins form an active complex that regulates MGS by poly-ubiquitination in both Sertoli cell and male germ cell lines. In addition, PTG overexpression in male germ cell line triggered apoptosis by caspase3 activation, proposing a proapoptotic role of glycogen in testis. These findings suggest that GS activity and glycogen synthesis in testis could be regulated and a disruption of this process may be responsible for the apoptosis and degeneration of seminiferous tubules and possible cause of infertility.
32 citations
Cites background from "Glycogen metabolism in human fetal ..."
...MUSCLE GLYCOGEN SYNTHASE IS EXPRESSED IN TESTIS, IS ACTIVE AND IS RESPONSIBLE FOR THE GLYCOGEN STORE It is almost 60 years ago that glycogen content and glycogen fluctuations were detected in the testis of different mammals [Arzac, 1950, 1953; Ewing et al., 1966; Fabbrini et al., 1969; Fouquet and Guha, 1969; Fawcett and Dym, 1976; Datta et al., 1988]....
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...Many studies have shown changes in enzyme activity and glycogen content in whole testis [Arzac, 1950, 1953; Ewing et al., 1966; Fabbrini et al., 1969; Fouquet and Guha, 1969; Fawcett and Dym, 1976; Datta et al., 1988], but we demonstrate localization and distribution of the enzyme in male germ cell epithelium and also observe glycogen content at different stages of cell differentiation....
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...…and glycogen content in whole testis [Arzac, 1950, 1953; Ewing et al., 1966; Fabbrini et al., 1969; Fouquet and Guha, 1969; Fawcett and Dym, 1976; Datta et al., 1988], but we demonstrate localization and distribution of the enzyme in male germ cell epithelium and also observe glycogen content at…...
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...AND IS RESPONSIBLE FOR THE GLYCOGEN STORE It is almost 60 years ago that glycogen content and glycogen fluctuations were detected in the testis of different mammals [Arzac, 1950, 1953; Ewing et al., 1966; Fabbrini et al., 1969; Fouquet and Guha, 1969; Fawcett and Dym, 1976; Datta et al., 1988]....
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TL;DR: The biochemical and histopathological results in this present study showed testicular toxicity in the rats administered with KBrO3 and T. daniellii leaf protective effect on the testicular function toxicity in rats fed with T.danieLLii leaf rat feed.
17 citations
TL;DR: The comprehensive liver tissue circRNA expression profiles produced in the present study may help to elucidate the functions and mechanisms of EpCAM during liver development.
Abstract: Epithelial cell adhesion molecule (EpCAM) is highly expressed during liver development and carcinogenesis, However, its functions and underlying mechanisms remain unclear. Clustered regularly interspaced short palindromic repeats (CRISPRs)/CRISPR‑associated protein 9 (Cas9) technology was used in the current study to establish EpCAM‑/‑ mice. The expression of EpCAM in the livers of the mice at embryonic day (E)18.5 and post‑natal day (P)0 was detected by immunofluorescence staining. The expression of genes associated with the development and glycogen metabolism was also assessed by reverse transcription‑quantitative PCR. Additionally, the liver tissue of the EpCAM‑/‑ and wild‑type mice was used for non‑coding RNA sequencing. The results of RNA sequencing revealed 11 up‑regulated and 12 downregulated circular RNAs (circRNAs). Kyoto Encyclopedia of Genes and Genomes analysis for resource genes determined that the top altered pathways included cell junctions, cell cycle, immune signaling and metabolism. This analysis was also utilized to predict the target association of the circRNA‑microRNA‑mRNA network. The comprehensive liver tissue circRNA expression profiles produced in the present study may help to elucidate the functions and mechanisms of EpCAM during liver development.
9 citations
TL;DR: It is suggested that ammonium molybdate exerts a deleterious effect on testicular function by altering biochemical and antioxidant status of the testes by altering the concentration of total protein and sialic acid and the activities of acid phosphatase and ascorboic acid.
Abstract: The present study was carried out to investigate the effects of ammonium molybdate on lipid peroxidation, antioxidant, biochemical and semen parameters in male Wistar rats. Group I served as control while group II, III and IV received 50, 100 and 150 mg kgG b.wt. dayG ammonium molybdate orally respectively for 60 days. Group V rats received 150 mg kgG b.wt. dayG for 60 days and thereafter left for recovery study for 60 days. The present study examined the effects of ammonium molybdate on serum testosterone, Follicle Stimulating Hormone (FSH) and Luteinizing Hormone (LH) along with sperm parameters. Estimations were also made for marker biochemical and antioxidant parameters in testis. Ammonium molybdate treatment resulted in a dose dependent reduction in serum testosterone, FSH, LH, sperm count, motility and viability. The concentration of total protein and sialic acid as well as activities of acid phosphatase (ACP) and alkaline phosphatase (ALP) were decreased in a dose dependent manner while there was a significant increase in the glycogen and cholesterol level in testis. The level of Thiobarbituric Acid Reactive substance (TBARs) was increased while the activities of superoxide dismutase and concentration of glutathione and ascorboic acid was decreased significantly in testis of rats treated with ammonium molybdate. All the parameters showed significant improvement after 60 days of treatment withdrawal in highest dose group. The findings suggested that ammonium molybdate exerts a deleterious effect on testicular function by altering biochemical and antioxidant status of the testes.
8 citations
Cites background from "Glycogen metabolism in human fetal ..."
...Testicular glycogen is a crucial requirement for gonadal maturation and proper functioning (Datta et al., 1988)....
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26 Oct 2018
TL;DR: The main metabolic changes that occur during male germ differentiation are summarized, with a specific focus on metabolic sources during spermatocyte to sperMatid transition, and the roles from single molecules to polymers on the viability of male germ cells are described.
Abstract: Spermatogenesis is a complex physiological process that involves cell proliferation, meiotic division and a final cell differentiation of post-meiotic cells into spermatozoa. During this process male germ cells also undergo a metabolic differentiation process, in which post-meiotic spermatogenic cells (spermatids) but not meiotic spermatogenic cells (spermatocytes) respond differentially to D-glucose metabolism, glucose transporters (GLUTs) distribution and utilization of non-hexose substrates, such as lactate/pyruvate or dihydroxyacetone. These differences might be explained by the requirement for a specific metabolic process to support cell differentiation or in some cases, cell viability. In addition, though glycogen is considered to be the main glucose store, in male germ cells this polymer may play a novel role in cell proliferation, acting as a new marker for apoptotic events in testicular tissue via a yet unknown mechanism. In this article, we summarize the main metabolic changes that occur during male germ differentiation, with a specific focus on metabolic sources during spermatocyte to spermatid transition. The latter considering that these cells come from the same cell linage as specialized cells, but are not isolated from their environment, describing the roles from single molecules to polymers on the viability of male germ cells.
7 citations
Cites background from "Glycogen metabolism in human fetal ..."
...In most mammals, quantities of testicular glycogen vary during normal testis development, from being very abundant in the intratubular portion of seminiferous tubules in the pre-puberal stage, to diminished numbers at the onset of puberty (Arzac, 1950, 1953; Ewing et al., 1966; Fabbrini et al., 1969; Fouquet & Guha, 1969; Datta et al., 1988)....
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...…vary during normal testis development, from being very abundant in the intratubular portion of seminiferous tubules in the pre-puberal stage, to diminished numbers at the onset of puberty (Arzac, 1950, 1953; Ewing et al., 1966; Fabbrini et al., 1969; Fouquet & Guha, 1969; Datta et al., 1988)....
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References
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Journal Article•
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
289,852 citations
"Glycogen metabolism in human fetal ..." refers methods in this paper
...Protein was determined by the method of Lowry et al. (1951)....
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Book•
01 Jan 1961
TL;DR: The new Pearse bids fair to become the leader, even amongst so notable a collection of books devoted entirely or largely to histochemical techniques.
Abstract: A. G. E. Pearse is a relative newcomer to the field of histochemistry. He holds an M.D. degree from the University of Cambridge and is now Lecturer in Histochemistry at the Postgraduate Medical School, University of London. One of his first contributions to histochemistry consisted of a critical review of its methodology and interpretation, written for pathologists and appearing in the British Journal of Clinical Pathology 4: 1 (1951). He has also introduced a number of new or modified techniques. Perhaps those having the greatest interest for endocrinologists are presented in a series of papers concerning the demonstration of the glycoprotein hormones of the anterior pituitary gland (Nature 162: 651, 1948; J. Path. & Bad. 61: 195, 1949, 64: 791 & 811, 1952; Stain Technol. 25: 95, 1950). The present volume comprises 17 chapters, beginning with a brief but fairly inclusive history of the development of this branch of science and continuing with 2 chapters on methods of fixation and sectioning, 3 on the staining of proteins, 4 on the demonstration of enzymes, 1 on the use of enzymes as histochemical reagents, and 1 each on carbohydrates, lipids, aldehydes and ketones, pigments, inorganic substances, and physical methods. The book concludes with appendices which give the detailed steps of the histochemical techniques which Dr. Pearse has himself found most useful for demonstrating various tissue constituents. Complete author and subject indices follow. A further valuable feature of the book consists of numerous black-and-white and a few colored photomicrographs illustrating the appearance of sections prepared by some of the histochemical methods discussed. A rash of books devoted entirely or largely to histochemical techniques has appeared in the last few years. Outstanding are the treatises by Lillie (1948), Romeis (1948, 15th ed., German), Glick (1949), Gatenby and Beams (1950, 11th ed.), Gomori (1952), and Lison (1953, 2nd ed., French). In this reviewer's opinion, the new Pearse bids fair to become the leader, even amongst so notable a collection. In each chapter, Dr. Pearse reviews the chemistry and biological importance of the substances in question and then goes on to discuss critically the methods used for their demonstration and differentiation. The bibliographic references are numerous and appear to include most of the major contributions in each area. Pearse has omitted some references which appear fundamental, for example, the definitive experimental paper and review by Marcus Singer concerning the nature of acidic and basic staining of proteins (/. Biol. Chem. 75: 133, 1948; Internal. Rev. Cytol. I: 211, 1952). Likewise, the techniques which he has selected to give in detail represent his particular preferences, whereas numerous methods which are possibly equally satisfactory are barely mentioned. While Pearse's omissions in this respect are not serious, the usefulness of some methods which he has overlooked should not be lost sight of. Needless to say, in a field which is growing so rapidly and to which several journals are now entirely devoted, no book can long remain up-to-date.
7,499 citations
Journal Article•
1,350 citations
Book•
01 Jan 1979
TL;DR: In this article, the biology of the placental prolactin growth hormone gene family and the development of the normal human breast was discussed. And the physiology of penile erection was investigated in domestic ruminants.
Abstract: Sex determination in mammals, A McLares metabolism of the pre-implantation mammalian embryo, Ho Leese the physiology of penile erection, KE Creed et al the biology of the placental prolactin growth hormone gene family, Isabel A Forsyth the development of the normal human breast, D Laurence et al hormones and breast cancer, RD Bulbrook the control of corpus luteum function in domestic ruminants, Hector W Alila and Joseph P Dowd nutrition and reproduction, H l'Anson et al
356 citations
TL;DR: Sex determination in mammals, A. McLares metabolism of the pre-implantation mammalian embryo, Ho Leese the physiology of penile erection, and the biology of the placental prolactin growth hormone gene family are discussed.
338 citations