The Synthesis and Migration of Nuclear Proteins during Mitosis and differentiation of Cells in Rats

Hooded rats were given an intraperitoneal injection of 3H-tyrosine, and killed in pairs 10 min, 30 min, 12 h, 36 h, 7 days, and 30 days later. A piece of skin with white growing hair, and the tongue, were taken from each animal and radioautographs were prepared. Silver grains were counted over whole nuclei and whole mitotic figures of the germinal cells and whole nuclei of differentiating cells of both tissues. It was found that the interphase nuclei have significantly more silver grains over them than the chromosomes at all stages of mitosis and there are virtually no grains over metaphase, anaphase, and early telophase chromosomes in both tissues of all the animals killed up to 36 h after the injection. The difference between the grain counts over the interphase nuclei and the chromosomes of dividing cells is at least 20-fold at 30 min in the hair matrix, at least 5-fold at 30 min in the tongue and at 36 h in both tissues. It was established that the differences observed between the radioactivities of the nuclei and chromosomes of mitotic figures are real from estimates of: the radioactivity of the cell cytoplasm, volumes of the metaphase chromosomes and interphase nuclei within 1µ of the photographic emulsion, and the volumes of cytoplasm separating the photographic emulsion and these structures. No protein synthesis was demonstrable in the chromosomes during metaphase, anaphase, and early telophase. Nuclear proteins leave the chromosomes during prophase and prometaphase and return to the nucleus during late telophase. The cells in the matrix and upper bulb of the growing hair follicle and those in the germinal, prickle, and granular cell layers of the tongue are in different functional states; 30 min after injection of 3H-tyrosine they have different amounts of it in their nuclear proteins. It is suggested that the amount incorporated into each nucleus is related to the rate at which proteins are being synthesized by the cell.

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Intranasal delivery of mitochondria for treatment of Parkinson’s Disease model rats lesioned with 6-hydroxydopamine

Scientific Reports ◽

10.1038/s41598-021-90094-w ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Jui-Chih Chang ◽

Yi-Chun Chao ◽

Huei-Shin Chang ◽

Yu-Ling Wu ◽

Hui-Ju Chang ◽

...

Keyword(s):

Parkinson’S Disease ◽

Parkinson's Disease ◽

Olfactory Bulb ◽

Disease Model ◽

Intranasal Delivery ◽

The Difference ◽

And Migration ◽

6 Hydroxydopamine ◽

Locomotor Behaviors ◽

Migratory Stream

AbstractThe feasibility of delivering mitochondria intranasally so as to bypass the blood–brain barrier in treating Parkinson's disease (PD), was evaluated in unilaterally 6-OHDA-lesioned rats. Intranasal infusion of allogeneic mitochondria conjugated with Pep-1 (P-Mito) or unconjugated (Mito) was performed once a week on the ipsilateral sides of lesioned brains for three months. A significant improvement of rotational and locomotor behaviors in PD rats was observed in both mitochondrial groups, compared to sham or Pep-1-only groups. Dopaminergic (DA) neuron survival and recovery > 60% occurred in lesions of the substantia nigra (SN) and striatum in Mito and P-Mito rats. The treatment effect was stronger in the P-Mito group than the Mito group, but the difference was insignificant. This recovery was associated with restoration of mitochondrial function and attenuation of oxidative damage in lesioned SN. Notably, P-Mito suppressed plasma levels of inflammatory cytokines. Mitochondria penetrated the accessory olfactory bulb and doublecortin-positive neurons of the rostral migratory stream (RMS) on the ipsilateral sides of lesions and were expressed in striatal, but not SN DA neurons, of both cerebral hemispheres, evidently via commissural fibers. This study shows promise for intranasal delivery of mitochondria, confirming mitochondrial internalization and migration via RMS neurons in the olfactory bulb for PD therapy.

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Intermittent Fasting Ameliorated High-Fat Diet-Induced Memory Impairment in Rats via Reducing Oxidative Stress and Glial Fibrillary Acidic Protein Expression in Brain

Nutrients ◽

10.3390/nu13010010 ◽

2020 ◽

Vol 13 (1) ◽

pp. 10

Author(s):

Suzan M. Hazzaa ◽

Mabrouk A. Abd Eldaim ◽

Amira A. Fouda ◽

Asmaa Shams El Dein Mohamed ◽

Mohamed Mohamed Soliman ◽

...

Keyword(s):

Body Weight ◽

Glial Fibrillary Acidic Protein ◽

Brain Tissue ◽

High Fat Diet ◽

Serum Lipids ◽

Memory Performance ◽

Granular Cell ◽

Intermittent Fasting ◽

High Fat ◽

Cell Layers

Intermittent fasting (IF) plays an important role in the protection against metabolic syndrome-induced memory defects. This study aimed to assess the protective effects of both prophylactic and curative IF against high-fat diet (HFD)-induced memory defects in rats. The control group received a normal diet; the second group received a HFD; the third group was fed a HFD for 12 weeks and subjected to IF during the last four weeks (curative IF); the fourth group was fed a HFD and subjected to IF simultaneously (prophylactic IF). A high-fat diet significantly increased body weight, serum lipids levels, malondialdehyde (MDA) concentration, glial fibrillary acidic protein (GFAP) and H score in brain tissue and altered memory performance. In addition, it significantly decreased reduced glutathione (GSH) concentration in brain tissue and viability and thickness of pyramidal and hippocampus granular cell layers. However, both types of IF significantly decreased body weight, serum lipids, GFAP protein expression and H score and MDA concentration in brain tissue, and improved memory performance, while it significantly increased GSH concentration in brain tissue, viability, and thickness of pyramidal and granular cell layers of the hippocampus. This study indicated that IF ameliorated HFD-induced memory disturbance and brain tissue damage and the prophylactic IF was more potent than curative IF.

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SYNTHESIS AND MIGRATION OF PROTEINS IN THE CELLS OF THE EXOCRINE PANCREAS AS REVEALED BY SPECIFIC ACTIVITY DETERMINATION FROM RADIOAUTOGRAPHS

The Journal of Cell Biology ◽

10.1083/jcb.16.1.1 ◽

1963 ◽

Vol 16 (1) ◽

pp. 1-23 ◽

Cited By ~ 118

Author(s):

H. Warshawsky ◽

C. P. Leblond ◽

B. Droz

Keyword(s):

Specific Activity ◽

Acinar Cells ◽

Pancreatic Acinar Cells ◽

Zymogen Granule ◽

Zymogen Granules ◽

The Mean ◽

And Migration ◽

Rats And Mice ◽

Silver Grains ◽

Golgi Zone

Radioautographs of pancreatic acinar cells were prepared in rats and mice sacrificed at various times after injection of leucine-, glycine-, or methionine-H3. Measurements of radioactivity concentration (number of silver grains per unit area) and relative protein concentration (by microspectrophotometry of Millon-treated sections) yielded the mean specific activity of proteins in various regions of the acinar cells. The 2 to 5 minute radioautographs as well as the specific activity time curves demonstrate protein synthesis in ergastoplasm. From there, most newly synthesized proteins migrate to and accumulate in the Golgi zone. Then they spread to the whole zymogen region and, finally, enter the excretory ducts. An attempt at estimating turnover times indicated that two classes of proteins are synthesized in the ergastoplasm: "sedentary" with a slow turnover (62.5 hours) and "exportable" with rapid turnover (4.7 minutes). It is estimated that the exportable proteins spend approximately 11.7 minutes in the Golgi zone where they are built up into zymogen granules, and thereafter 36.0 minutes as fully formed zymogen granules, before they are released outside the acinar cell as pancreatic secretion. The mean life span of a zymogen granule in the cell is estimated to be 47.7 minutes.

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Non-cell-autonomous function of the Antirrhinum floral homeotic proteins DEFICIENS and GLOBOSA is exerted by their polar cell-to-cell trafficking

Development ◽

10.1242/dev.122.11.3433 ◽

1996 ◽

Vol 122 (11) ◽

pp. 3433-3441 ◽

Cited By ~ 8

Author(s):

M.C. Perbal ◽

G. Haughn ◽

H. Saedler ◽

Z. Schwarz-Sommer

Keyword(s):

Cell Layer ◽

Epidermal Cells ◽

Molecular Techniques ◽

Cell Trafficking ◽

Mads Box ◽

Organ Identity ◽

Cell Layers ◽

Periclinal Chimeras ◽

The Difference ◽

Cell Autonomy

In Antirrhinum majus, petal and stamen organ identity is controlled by two MADS-box transcription factors, DEFICIENS and GLOBOSA. Mutations in either of these genes result in the replacement of petals by sepaloid organs and stamens by carpelloid organs. Somatically stable def and glo periclinal chimeras, generated by transposon excision events, were used to study the non-cell-autonomous functions of these two MADS-box proteins. Two morphologically distinct types of chimeras were analysed using genetic, morphological and molecular techniques. Restoration of DEF expression in the L1 cell layer results in the reestablishment of DEF and GLO functions in L1-derived cells only; inner layer cells retain their mutant sepaloid features. Nevertheless, this activity is sufficient to allow the expansion of petal lobes, highlighting the role of DEF in the stimulation of cell proliferation and/or cell shape and elongation when expressed in the L1 layer. Establishment of DEF or GLO expression in L2 and L3 cell layers is accompanied by the recovery of petaloid identity of the epidermal cells but it is insufficient to allow petal lobe expansion. We show by in situ immunolocalisation that the non-cell-autonomy is due to direct trafficking of DEF and GLO proteins from the inner layer to the epidermal cells. At least for DEF, this movement appears to be polar since DEF acts cell-autonomously when expressed in the L1 cell layer. Furthermore, the petaloid revertant sectors observed on second whorl mutant organs and the mutant margins of petals of L2L3 chimeras suggest that DEF and GLO intradermal movement is limited. This restriction may reflect the difference in the regulation of primary plasmodesmata connecting cells from the same layer and secondary plasmodesmata connecting cells from different layers. We propose that control of intradermal trafficking of DEF and GLO could play a role in maintaining of the boundaries of their expression domains.

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Nuclear proteins of quiescent and mitotically active cells in shoot meristems of Tradescantia paludosa

Canadian Journal of Botany ◽

10.1139/b74-263 ◽

1974 ◽

Vol 52 (9) ◽

pp. 2049-2053 ◽

Cited By ~ 5

Author(s):

R. S. Tobin ◽

Kyu-Byung Yun ◽

J. M. Naylor

Keyword(s):

Nuclear Proteins ◽

Zone Of Inhibition ◽

Interphase Nuclei ◽

Lateral Buds ◽

Dye Binding ◽

Tradescantia Paludosa ◽

Shoot Meristems

In inhibited lateral buds of Tradescantia paludosa, interphase nuclei in the apical zone of inhibition contain higher levels of arginine per unit DNA than those of mitotically active cells in interphase or prophase. Supplementary dye-binding experiments suggest that this reflects a corresponding difference between the composition of the histone complement of chromatin in the two cells populations. The possible implications of this phenomenon are discussed.

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HMBG1 as a Driver of Inflammatory and Immune Processes in the Pathogenesis of Ocular Diseases

Journal of Ophthalmology ◽

10.1155/2018/5195290 ◽

2018 ◽

Vol 2018 ◽

pp. 1-8

Author(s):

Yi Liu ◽

Guo-Bin Zhuang ◽

Xue-Zhi Zhou

Keyword(s):

Current Knowledge ◽

High Mobility ◽

Retinal Cell ◽

Ocular Diseases ◽

Wide Range ◽

Glycation End Products ◽

Cell Layers ◽

Proinflammatory Activity ◽

And Migration ◽

Proliferation And Migration

High-mobility group box 1 (HMGB1) is a nuclear protein that can also act as an extracellular trigger of inflammation, proliferation, and migration in eye diseases. It induces signaling pathways by binding to the receptor for advanced glycation end products (RAGE) and Toll-like receptors (TLRs) 2, 4, and 9. This proinflammatory activity is considered to be important in the pathogenesis of a wide range of ocular diseases resulting from hemodynamic changes, presence of neovascular endothelial cells, secretion of intraocular immune factors or inflammation, and apoptosis of retinal cell layers. Further work is needed to elucidate in detail how HMGB1 contributes to ocular disease and how its damaging activity can be modulated. In this review, we summarize current knowledge on HMGB1 as a ligand that can evoke inflammation and immune responses in ocular diseases.

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A Light Microscope Study of Linker Histone Distribution in Rat Metaphase Chromosomes and Interphase Nuclei

Experimental Cell Research ◽

10.1006/excr.1993.1115 ◽

1993 ◽

Vol 206 (1) ◽

pp. 16-26 ◽

Cited By ~ 25

Author(s):

John W. Breneman ◽

Peter Yau ◽

Raymond L. Teplitz ◽

E.Morton Bradbury

Keyword(s):

Microscope Study ◽

Light Microscope ◽

Linker Histone ◽

Metaphase Chromosomes ◽

Interphase Nuclei

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26. International Refugee and Migration Law

International Law ◽

10.1093/he/9780198791836.003.0026 ◽

2018 ◽

Author(s):

Geoff Gilbert ◽

Anna Magdalena Rüsch

Keyword(s):

International Law ◽

International Human Rights Law ◽

Refugee Status ◽

Internally Displaced ◽

Durable Solutions ◽

Local Integration ◽

The Difference ◽

And Migration ◽

Definition Of ◽

International Border

This chapter explores the definition of refugee status in international law, its scope and limitations and consequent protection gaps for those forcibly displaced, including internally displaced persons (IDPs), who have crossed no international border. There is no equivalent definition for migrants, but like refugees, asylum-seekers, and IDPs, international human rights law provides a framework for their protection. The chapter explains the difference between refugee status and asylum, focusing on non-refoulement in international law. It discusses the rights that are guaranteed during displacement, particularly those pertaining to detention and humanitarian relief. Given that refugee status is intended to be temporary, the final section looks at cessation and durable solutions, either following voluntary return, through local integration, or resettlement in some third State.

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261 LABELING SEX-SPECIFIC DNA SEQUENCES IN MAMMALIAN SPERM

Reproduction Fertility and Development ◽

10.1071/rdv20n1ab261 ◽

2008 ◽

Vol 20 (1) ◽

pp. 210

Author(s):

B. A. Didion ◽

R. Bleher

Keyword(s):

Dna Sequences ◽

Somatic Cells ◽

Complete Separation ◽

Cell Nuclei ◽

Metaphase Chromosomes ◽

Telomeric Sequences ◽

Synthetic Dna ◽

Y Chromosomes ◽

Boar Sperm ◽

The Difference

While flow cytometric separation of X- andY-chromosome- bearing sperm has advanced to the point of acceptance in the commercial production of sex-preselected cattle, it is important to continue researching this area to improve efficiencies. For example, the difference in DNA sequence between the X- andY-chromosomes has merit as a foundation for an alternative sperm sexing approach that could enable the complete separation and use of an entire ejaculate. We used synthetic DNA mimics conjugated to a fluorescent dye for in situ detection of Y-chromosomes in metaphase preparations of porcine somatic cells and spermatozoa. Peptide nucleic acids (PNA) are synthetic compounds with higher affinity and stability than conventional DNA probes and are used as specific hybridization probes to complementary DNA. The application of PNA probes was demonstrated previously in telomere analysis studies, and we confirmed their efficacy using a CY3-(CCCTAA)3 PNA to probe bull and boar sperm telomeric sequences. Using male porcine somatic cells and theY-chromosome as a template, we arranged for the synthesis of a CY3-conjugated PNA to bind 13-15 base pairs of unique, Y-chromosome sequence. By testing different labeling conditions, we found that brief incubation of metaphase chromosomes with the PNA produced a localized signal on theY-chromosome. No signals were present when chromosomes of porcine female somatic cells were incubated with the PNA probes. Because chromosomes occupy non-random territories in all cell nuclei including those in sperm, we expected to find centrally located signals in 50% of fixed boar sperm when these were treated with the same PNA as used for the somatic cells. We found the signals present in 161 of 302 (53.3%) sperm to consist of a single, centrally located, round fluorescent dot in the sperm head. Further research is required to establish the uptake of PNA in live sperm toward evaluation of this approach for sperm sexing.

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