User:Z3420150

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Individual Assessment

Lab 1

Eukaryotic cellular structure.jpeg


Web Address: http://www.biomedcentral.com/1471-2148/7/55

Paper title: Nitrogen fixation in eukaryotes – New models for symbiosis [1]


Legend: Endosymbionts adapted for molecular nitrogen fixation,(A) A Bradyrhizobium sp. bacteroid in a root-nodule of Glycine max (soybean). (B) A Spheroid body of the diatom Rhopalodia gibba. SM: Symbiontophoric membrane SBM: Spheroid body membrane.







Copyright

© 2007 Kneip et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Note - This image was originally uploaded as part of a student project and may contain inaccuracies in either description or acknowledgements. Please contact the site coordinator if the uploaded content does not meet the original copyright permission or requirements, for immediate removal.

Lab 2

Evolutionary genomic remodelling of the human 4q subtelomere (4q35.2) [2]

This Journal Article focuses to achieve the observation regarding the functionality of the human 4q35.2 domain that possesses the facioscapulohumeral muscular dystrophy (FSHD) locus. Using modern technique such as confocal microscopy, such visual inspection have been able to identify that 11 in 28 cell samples of 4q35.2 domain to have one allele at the nuclear edge and 4 in 28 sample have both alleles in nuclear edge. This study gave a result that showed the genomic organisation of the gorilla locus that is synthetic to human chromosome 4q35.2. This is significant for tracking family trees such as extensive remodelling of chromosomes in both chimpanzees and humans especially the impact of 4q35.2 condensation in humans. This finding is paramount in quantitative evaluation in studying different locus in human domain like the gorilla locus which is synthetic to human chromosome which can be used in studying evolution.

--Mark Hill (talk) 14:40, 29 April 2013 (EST) This is a reasonable article, referenced correctly, though your title link above does not function.

Lab 3

Microscopy of Golgi body.gif

Partitioning of the Golgi Apparatus during Mitosis in Living HeLa Cells [3]

Using a fluorescent tag protein, the location of the Golgi apparatus has been identified and confirmed using immunogold and immunofluorescence (Golgi markers). Using confocal microscopy, the behavior of Golgi Apparatus has been observed. During metaphase, the cells containing fragments of Golgi seemed to disperse in the cytoplasm. The combination of confocal microscopy and fluorescence microscopy exposed the juxtanuclear reticulum in 90% of the cells which is a characteristic of Golgi apparatus which has also been confirmed by immunoelectron microscopy using GFP antibodies [4]. It identified its location to be found over a subset of one/two stack of cisternae during cell division.


Rockefeller University Press Copyright Policy This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

Note - This image was originally uploaded as part of a student project and may contain inaccuracies in either description or acknowledgements. Please contact the site coordinator if the uploaded content does not meet the original copyright permission or requirements, for immediate removal.


Golgi Biogenesis [5]

In this experiment, the NRK cells has been used to identify the positions of the Golgi apparatus during cell division. When the cells have been treated with 5-inhibitor s-trityl-L-cystein that functions as centrosome inhibitor, the Golgi behaviour has been viewed more clearly and systematically. Such chemical created a fixed triple-stained colour: green for protein GM130, red for a-tubulin and blue for the Golgi's DNA. The images has been collected systematically to show the location of each fragments that composes the whole Golgi body during cell mitosis. By this study, there has been hints to why Golgi undergoes disassembly and reconstruction during the cell division process of all mammalian living things and its significance in cell division. For now, the reason for interaction between Golgi and different mitotic machineries are still unknown, however further studies about ubiquitin ligase would give understanding to p97 which is responsible for post mitotic Golgi membrane fusion.

The Golgi Apparatus Maintains Its Organization Independent of the Endoplasmic Reticulum [6]

In this experiment, the Golgi enzymes has been observed and treated under physiological conditions in the endoplasmic reticulum. The reason for the experiment is to find the reason behind the recycling of golgi membranes in the ER. Using the chemical repamycin that serves its function as an inducer of FKBP and FRAP proteins, it became possible to observe the FKBP-tagged Golgi enzyme to FRAP-ER protein when the enzyme visits the ER. The experiment was paramount since this study suggests that Golgi proteins cycles through the ER and at the same time undergoes into biogenesis in ER as well. This is significant since it exposes the existance of Golgi-ER recycling pathway.

Analysis of De Novo Golgi Complex Formation after Enzyme-based Inactivation [7]

This study focuses on the Golgi maintenance during interphase cell division as well as the relationship of ER and Golgi complex during interphase. Using a drug free method where the Golgi body and its dynamics has been deactivated and replacing it by a synthetic Golgi-like marker with architecture, it has been tested and achieved a result that cells were unable to create a normal trafficking activity during the interphase method. Similar with the third paper, it has been suggested that the interaction between ER is paramount to achieve a balance maintenance during interphase. Such integration would be needed to create a Golgi-like structure that will be essential as a building block for Golgi complexes. Hence, Golgi complexes would be used for biogenesis of new normal Golgi elements when it comes to it's morphological and biochemical functions.

Lab 4

Integrin α6 Antibody (4F10): sc-53356

- is a mouse monoclonal IgG2b provided

- concentration: 200 µg/ml

- raised against SW1222 colorectal cell line of human origin

- recommended for detection of Integrin α6 of human origin by WB, IP, IF and FCM

- fluorescein (sc-53356 FITC) and phycoerythrin (sc-53356 PE) conjugates for FCM, 100 tests

- Application use:

  • By Western Blotting (starting dilution 1:200, dilution range 1:100-1:1000),
  • Immunoprecipitation [1–2 µg per 100–500 µg of total protein (1 ml of cell lysate)],
  • Immunofluorescence (starting dilution 1:50, dilution range 1:50-1:500) and
  • Flow cytometry (1 µg per 1 x 106 cells).

- References:

1. Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25. [8]

2. Miyamoto, S., Akiyama, S.K. and Yamada, K.M. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267: 883-885. [9]

3. Clark, E.A. and Brugge, J.S. 1995. Integrins and signal transduction pathways: the road taken. Science 268: 233-239. [10]

4. Sheppard, D. 1996. Epithelial integrins. BioEssays 18: 655-660. [11]

5. Juliano, R. 1996. Cooperation between soluble factors and integrinmediatedcell anchorage in the control of cell growth and differentiation. BioEssays 18: 911-917. [12]

--Mark Hill (talk) 14:40, 12 June 2013 (EST) There references could have been easily formatted. Example shown below.

R O Hynes Integrins: versatility, modulation, and signaling in cell adhesion. Cell: 1992, 69(1);11-25 PubMed 1555235

S Miyamoto, S K Akiyama, K M Yamada Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science: 1995, 267(5199);883-5 PubMed 7846531

E A Clark, J S Brugge Integrins and signal transduction pathways: the road taken. Science: 1995, 268(5208);233-9 PubMed 7716514

D Sheppard Epithelial integrins. Bioessays: 1996, 18(8);655-60 PubMed 8760339

R Juliano Cooperation between soluble factors and integrin-mediated cell anchorage in the control of cell growth and differentiation. Bioessays: 1996, 18(11);911-7 PubMed 8939069


[13] [14] [15] [16] [17] [18] [19] [20]

[21] [22]

Lab 8

Group 1

The introduction is a little bit basic in a good way. However, try and add a little bit of information that will introduce the ideas that will link to the ideas that you would be talking about for the whole project. The history table does not have enough information. I can see that two columns were left blank. Try and complete those as soon as possible because it looks unprofessional left blank and could affect your marks as well. The overall information in the body of the project lacks information. Try and expand your ideas especially for the Metaphase to Anaphase Transition topic. Also, try and complete the diseases table as well.


Group 2

Your information are well organised. The only comment I can say is do not try and include acronyms without introducing them first and talking about the functions. I know you can find this in the glossary, however your information would flow really good if you include a brief introductions of acronyms before including them. I am not saying that it goes to all the acronyms that you have included because you have successfully introduced quite a number of them. However, you should take in mind that the people who might need your information would have no idea about the biochemical acronyms. One more thing, I just like to point out to try and balance the information and images content. I know that our proctor removed some of your images due to lack of copyright but try and add images again before the time because you might hav good information but lack of images makes it boring.

Overall, well done group 2!!

Group 4

The information here are well balanced however, they are a little bit untidy. When I was reading your information, sometimes I had to scroll down and up to link the information to the other. Also it is good that you have included acronyms and including what they mean, however, you should introduce them first and give a little bit about their functions before including them on your sentences. Remember that people who will access these information in the future might know nothing about all the acronyms so giving a little bit of background about them would be helpful. Fixing this issue will make your whole project flawless :)

The balance between the images and texts are very good. The tables are excellent and the glossary are good. Overall, well done.

Group 5

Your page was very informative. However, try and balance the information that you are providing. Some parts of your project have so much information. Try breaking them down into more simplified and concise way. Your page should be reader friendly. Sometime, I find it very hard to follow the information layout of the project. Remember some potential readers can be undergraduates who may have no or poor background to medical science. Be always straight to the point. Try adding more images as well. It would be much better if the images are diagrams that show the nuclear envelope's molecular processes in each stages of cell division to make it more technical not just microscopic images of the nuclear envelope.

Group 6

My concern to this group is opposite to Group 5 and 2. Try and add more information to your text. The table is set out well. However, I think you have chosen poor colour combination. I can barely see the texts inside the table. Try choosing light purple if you want to use purple. The information are also a little bit untidy and the information does not flow very well as you read through the infromation. However, your information are great and is both suitable for beginners and people who have more background to this area. Your group just need to fix these few problems and it's perfect.

Group 7 Again, you need to balance your text content and the images that you are putting on your project. Less images makes it boring. Try adding images that show biochemical processes that take place in the mitochondria during cell division. In the introduction perhaps talk about the topics that you will be talking about your whole project not just the description of the mitochondria. Overall the information was set up well, however there are acronyms that has not been defined and introduced first regarding their functions before talking about them. However overall, good job group 7.

Reference

  1. Christoph Kneip, Peter Lockhart, Christine Voss, Uwe-G Maier Nitrogen fixation in eukaryotes--new models for symbiosis. BMC Evol. Biol.: 2007, 7;55 PubMed 17408485
  2. Beatrice Bodega, Maria Francesca Cardone, Stefan Müller, Michaela Neusser, Francesca Orzan, Elena Rossi, Elena Battaglioli, Anna Marozzi, Paola Riva, Mariano Rocchi, Raffaella Meneveri, Enrico Ginelli Evolutionary genomic remodelling of the human 4q subtelomere (4q35.2). BMC Evol. Biol.: 2007, 7;39 PubMed 17359533
  3. D T Shima, K Haldar, R Pepperkok, R Watson, G Warren Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol.: 1997, 137(6);1211-28 PubMed 9182657
  4. D Louvard, H Reggio, G Warren Antibodies to the Golgi complex and the rough endoplasmic reticulum. J. Cell Biol.: 1982, 92(1);92-107 PubMed 7199056
  5. Yanzhuang Wang, Joachim Seemann Golgi biogenesis. Cold Spring Harb Perspect Biol: 2011, 3(10);a005330 PubMed 21690214
  6. Matthew Y Pecot, Vivek Malhotra The Golgi apparatus maintains its organization independent of the endoplasmic reticulum. Mol. Biol. Cell: 2006, 17(12);5372-80 PubMed 17050735
  7. Florence Jollivet, Graça Raposo, Ariane Dimitrov, Rachid Sougrat, Bruno Goud, Franck Perez Analysis of de novo Golgi complex formation after enzyme-based inactivation. Mol. Biol. Cell: 2007, 18(11);4637-47 PubMed 17855505
  8. R O Hynes Integrins: versatility, modulation, and signaling in cell adhesion. Cell: 1992, 69(1);11-25 PubMed 1555235
  9. S Miyamoto, S K Akiyama, K M Yamada Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science: 1995, 267(5199);883-5 PubMed 7846531
  10. E A Clark, J S Brugge Integrins and signal transduction pathways: the road taken. Science: 1995, 268(5208);233-9 PubMed 7716514
  11. D Sheppard Epithelial integrins. Bioessays: 1996, 18(8);655-60 PubMed 8760339
  12. R Juliano Cooperation between soluble factors and integrin-mediated cell anchorage in the control of cell growth and differentiation. Bioessays: 1996, 18(11);911-7 PubMed 8939069
  13. J W Daniel Metabolic aspects of antioxidants and preservatives. Xenobiotica: 1986, 16(10-11);1073-8 PubMed 3541396
  14. Final report of the cosmetic ingredient review expert panel on the safety assessment of Polyisobutene and Hydrogenated Polyisobutene as used in cosmetics. Int. J. Toxicol.: 2008, 27 Suppl 4;83-106 PubMed 19101833
  15. E Budayová Effects of sodium nitrite and potassium sorbate on in vitro cultured mammalian cells. Neoplasma: 1985, 32(3);341-50 PubMed 4022194
  16. G Weiss, C Murr, H Zoller, M Haun, B Widner, C Ludescher, D Fuchs Modulation of neopterin formation and tryptophan degradation by Th1- and Th2-derived cytokines in human monocytic cells. Clin. Exp. Immunol.: 1999, 116(3);435-40 PubMed 10361231
  17. Barbara Wirleitner, Katharina Schroecksnadel, Christiana Winkler, Harald Schennach, Dietmar Fuchs Resveratrol suppresses interferon-gamma-induced biochemical pathways in human peripheral blood mononuclear cells in vitro. Immunol. Lett.: 2005, 100(2);159-63 PubMed 16154495
  18. Christian Murr, Katharina Schroecksnadel, Christiana Winkler, Maximilian Ledochowski, Dietmar Fuchs Antioxidants may increase the probability of developing allergic diseases and asthma. Med. Hypotheses: 2005, 64(5);973-7 PubMed 15780494
  19. R Walker Toxicology of sorbic acid and sorbates. Food Addit Contam: 1990, 7(5);671-6 PubMed 2253811
  20. Sergio Romagnani Immunologic influences on allergy and the TH1/TH2 balance. J. Allergy Clin. Immunol.: 2004, 113(3);395-400 PubMed 14758340
  21. Christiana Winkler, Barbara Frick, Katharina Schroecksnadel, Harald Schennach, Dietmar Fuchs Food preservatives sodium sulfite and sorbic acid suppress mitogen-stimulated peripheral blood mononuclear cells. Food Chem. Toxicol.: 2006, 44(12);2003-7 PubMed 16904801
  22. Michael Karin, Florian R Greten NF-kappaB: linking inflammation and immunity to cancer development and progression. Nat. Rev. Immunol.: 2005, 5(10);749-59 PubMed 16175180

Link

http://www.biomedcentral.com/bmcevolbiol/

http://jcb.rupress.org/content/137/6/1211.abstract