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Artículos de revistas sobre el tema "Proteins Synthesis"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 30 de julio de 2024

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1

Nilsson, Bradley L., Matthew B. Soellner, and Ronald T. Raines. "Chemical Synthesis of Proteins." Annual Review of Biophysics and Biomolecular Structure 34, no. 1 (June 2005): 91–118. http://dx.doi.org/10.1146/annurev.biophys.34.040204.144700.

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2

Gibney, Brian R., Francesc Rabanal, and P. Leslie Dutton. "Synthesis of novel proteins." Current Opinion in Chemical Biology 1, no. 4 (December 1997): 537–42. http://dx.doi.org/10.1016/s1367-5931(97)80050-6.

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3

Mejuch, Tom, and Herbert Waldmann. "Synthesis of Lipidated Proteins." Bioconjugate Chemistry 27, no. 8 (August 2016): 1771–83. http://dx.doi.org/10.1021/acs.bioconjchem.6b00261.

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4

Borgia, Jeffrey A., and Gregg B. Fields. "Chemical synthesis of proteins." Trends in Biotechnology 18, no. 6 (June 2000): 243–51. http://dx.doi.org/10.1016/s0167-7799(00)01445-1.

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5

Hilvert, Donald. "Chemical synthesis of proteins." Chemistry & Biology 1, no. 4 (December 1994): 201–3. http://dx.doi.org/10.1016/1074-5521(94)90011-6.

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6

Plocinski, P., N. Arora, K. Sarva, E. Blaszczyk, H. Qin, N. Das, R. Plocinska, et al. "Mycobacterium tuberculosis CwsA Interacts with CrgA and Wag31, and the CrgA-CwsA Complex Is Involved in Peptidoglycan Synthesis and Cell Shape Determination." Journal of Bacteriology 194, no. 23 (September 21, 2012): 6398–409. http://dx.doi.org/10.1128/jb.01005-12.

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ABSTRACTBacterial cell division and cell wall synthesis are highly coordinated processes involving multiple proteins. Here, we show that Rv0008c, a novel small membrane protein fromMycobacterium tuberculosis, localizes to the poles and on membranes and shows an overall punctate localization throughout the cell. Furthermore, Rv0008c interacts with two proteins, CrgA and Wag31, implicated in peptidoglycan (PG) synthesis in mycobacteria. Deletion of the Rv0008c homolog inM. smegmatis, MSMEG_0023, caused bulged cell poles, formation of rounded cells, and defects in polar localization of Wag31 and cell wall synthesis, with cell wall synthesis measured by the incorporation of the [14C]N-acetylglucosamine cell wall precursor. TheM. smegmatisMSMEG_0023crgAdouble mutant strain showed severe defects in growth, viability, cell wall synthesis, cell shape, and the localization of the FtsZ, FtsI, and Wag31 proteins. The double mutant strain also exhibited increased autolytic activity in the presence of detergents. Because CrgA and Wag31 proteins interact with FtsI individually, we believe that regulated cell wall synthesis and cell shape maintenance require the concerted actions of the CrgA, Rv0008c, FtsI, and Wag31 proteins. We propose that, together, CrgA and Rv0008c, renamed CwsA forcellwall synthesis and cellshape proteinA, play crucial roles in septal and polar PG synthesis and help coordinate these processes with the FtsZ-ring assembly in mycobacteria.

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7

Kohen, Amnon, Priyanka Singh, and Qi Guo. "Chemoenzymatic Synthesis of Ubiquitous Biological Redox Cofactors." Synlett 28, no. 10 (April 10, 2017): 1151–59. http://dx.doi.org/10.1055/s-0036-1588768.

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Redox cofactors are utilized by a myriad of proteins, ranging from metabolic enzymes to those performing post-translational modifications. Labeled redox cofactors have served as a vital tool for a broad range of studies. This account describes chemoenzymatic syntheses of the isotopically labeled, biologically important redox cofactors: nicotinamide adenine dinucleotide, methylene tetrahydrofolate, and flavin nucleotides. An overview of the general strategy is presented. These examples demonstrate the utility of enzymatic synthesis.1 Introduction2 Nicotinamide Cofactors2.1 Synthesis of Remote-Labeled 14C-NADPH2.1.1 Synthesis of [Ad-14C]NADPH2.1.2 Synthesis of [Carbonyl-14C]NADPH2.2 Synthesis of S- and R-[4-3H]NADPH2.2.1 One-Step S- and Three-Step R-[4-3H]NADPH Synthesis2.2.2 One-Pot, One-Step R-[4-3H]NADPH Synthesis2.3 Synthesis of S- and R-[Ad-14C, 4-2H]NADPH2.3.1 One-Step S-, Three-Step R-[Ad-14C, 4-2H]NADPH Synthesis2.3.2 One-Pot, One-Step R-[Ad-14C, 4-2H]NADPH Synthesis3 Methylene Tetrahydrofolate4 Flavin Nucleotides5 Conclusions and Outlook

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8

Metanis, Norman, Reem Mousa, and Post Reddy. "Chemical Protein Synthesis through Selenocysteine Chemistry." Synlett 28, no. 12 (March 21, 2017): 1389–93. http://dx.doi.org/10.1055/s-0036-1588762.

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Methods for the preparation of small-to-medium-sized proteins by chemical protein synthesis have matured in recent years and proven valuable for protein science. Thanks to the many recent discoveries and developments in the field, proteins up to 300 amino acids can now be prepared in the lab in a matter of days. This technology gives the scientists the flexibility to substitute any atom in the protein sequence; hence synthesis is not constrained to the 20 canonical amino acids. In this Synpacts article we briefly highlight the recent studies on selenocysteine chemistry in the field of chemical protein synthesis.1 Introduction2 Selenocysteine in Nature and in Folding Studies3 Selenocysteine in Protein Synthesis4 Selenocysteine in Natural Selenoproteins5 Outlook

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9

Whyte, Lyle G., and William E. Inniss. "Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium." Canadian Journal of Microbiology 38, no. 12 (December 1, 1992): 1281–85. http://dx.doi.org/10.1139/m92-211.

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The synthesis of proteins in the psychrotrophic bacterium Bacillus psychrophilus in response to both cold shock and continuous growth at low temperatures was examined. Cold shocks of 20 to 0, 5, or 10 °C resulted in the induction of nine, seven, and five cold shock proteins, respectively, as determined by 2-dimensional gel electrophoresis and computing scanning laser densitometry. Two cold shock proteins, with molecular masses of 61 and 34 kDa, which were induced in B. psychrophilus by cold shocks of 20 to 0 or 5 °C, were not induced in a cold-sensitive mutant of B. psychrophilus. Analysis of protein profiles of B. psychrophilus during continuous growth at 0, 5, or 10 °C revealed the synthesis of 11, 10, and 4 cold acclimation proteins, respectively. Some of these cold acclimation proteins were similar to cold shock proteins. In addition, the relative synthesis of both cold shock proteins and cold acclimation proteins increased with decreasing temperature. Thus, both types of proteins increased both in number and relative synthesis in response to cold shock and continuous growth at low temperature. Key words: cold shock proteins, cold acclimation proteins, psychrotrophic bacterium.

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10

Kent, Stephen B. H. "Total chemical synthesis of proteins." Chem. Soc. Rev. 38, no. 2 (2009): 338–51. http://dx.doi.org/10.1039/b700141j.

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11

Tam, James P., and Clarence T. T. Wong. "Chemical Synthesis of Circular Proteins." Journal of Biological Chemistry 287, no. 32 (June 14, 2012): 27020–25. http://dx.doi.org/10.1074/jbc.r111.323568.

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12

Muir, Tom W., and Stephen B. H. Kent. "The chemical synthesis of proteins." Current Opinion in Biotechnology 4, no. 4 (August 1993): 420–27. http://dx.doi.org/10.1016/0958-1669(93)90007-j.

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13

Huang, Yichao, and Lei Liu. "Chemical synthesis of crystalline proteins." Science China Chemistry 58, no. 12 (July 8, 2015): 1779–81. http://dx.doi.org/10.1007/s11426-015-5462-2.

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14

Sakakibara, Shumpei. "Editorial: Chemical synthesis of proteins." Biopolymers 51, no. 4 (1999): 245–46. http://dx.doi.org/10.1002/(sici)1097-0282(1999)51:4<245::aid-bip1>3.0.co;2-4.

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15

Merrifield, Bruce. "The chemical synthesis of proteins." Protein Science 5, no. 9 (September 1996): 1947–51. http://dx.doi.org/10.1002/pro.5560050925.

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16

Huang, Yi-Chao, Ge-Min Fang, and Lei Liu. "Chemical synthesis of proteins using hydrazide intermediates." National Science Review 3, no. 1 (November 9, 2015): 107–16. http://dx.doi.org/10.1093/nsr/nwv072.

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Abstract Protein chemical synthesis offers useful and otherwise-difficulty-to-obtain biomacromolecules for biological and pharmaceutical studies. Recently, the hydrazide chemistry has drawn attentions in this field as peptide or protein hydrazides can be used as key intermediates for different synthesis and modification purposes. Besides being a traditional bioorthogonal chemical handle, a hydrazide group can serve as a readily accessible precursor of a thioester. This strategy significantly improves the efficiency and scope of native chemical ligation for protein chemical synthesis. Here we review the chemical transformations of peptide or protein hydrazides and total/semi/enzymatic protein synthesis methods involving peptide or protein hydrazides. Several examples of protein chemical synthesis using peptide hydrazides as key intermediates are described.

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17

Austen, Brian M., Joseph M. Sheridan, Omar M. A. El-Agnaf, Hazel Goodwin, and Emma R. Frears. "Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases." Protein & Peptide Letters 7, no. 1 (February 2000): 1–8. http://dx.doi.org/10.2174/092986650701221205144944.

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P-Amyloid protein, the a-synuclein fragment NAC, and protease-resistant forms of prion proteins are found deposited in the pathological lesions associated with neurodegenerative disease. Chemical syntheses of these proteins are notoriously difficult due to aggregation of the peptides on the resin during synthesis. We report optimised solid-phase syntheses of several amyloid peptides in high yield and >90% initial purity.

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18

Chakraborty, Asit Kumar. "Multi-Alignment Comparison of Coronavirus Non-Structural Proteins Nsp13- Nsp16 with Ribosomal Proteins and other DNA/RNA Modifying Enzymes Suggested their Roles in the Regulation of Host Protein Synthesis." International Journal of Clinical & Medical Informatics 3, no. 1 (June 1, 2020): 7–19. http://dx.doi.org/10.46619/ijcmi.2020.1024.

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19

Vallée, Yannick, and Sparta Youssef-Saliba. "Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa." Synthesis 53, no. 16 (April 1, 2021): 2798–808. http://dx.doi.org/10.1055/a-1472-7914.

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AbstractTwo sulfur-containing amino acids are included in the list of the 20 classical protein amino acids. A methionine residue is introduced at the start of the synthesis of all current proteins. Cysteine, thanks to its thiol function, plays an essential role in a very large number of catalytic sites. Here we present what is known about the prebiotic synthesis of these two amino acids and homocysteine, and we discuss their introduction into primitive peptides and more elaborate proteins.1 Introduction2 Sulfur Sources3 Prebiotic Synthesis of Cysteine4 Prebiotic Synthesis of Methionine5 Homocysteine and Its Thiolactone6 Methionine and Cystine in Proteins7 Prebiotic Scenarios Using Sulfur Amino Acids8 Introduction of Cys and Met in the Genetic Code9 Conclusion

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20

Bannon, G. A., R. Perkins-Dameron, and A. Allen-Nash. "Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila." Molecular and Cellular Biology 6, no. 9 (September 1986): 3240–45. http://dx.doi.org/10.1128/mcb.6.9.3240-3245.1986.

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The presence of specific proteins (known as immobilization antigens) on the surface of the ciliated protozoan Tetrahymena thermophila is under environmental regulation. There are five different classes (serotypes) of surface proteins which appear on the cell surface when T. thermophila is cultured under different conditions of temperature or incubation medium; three of these are temperature dependent. The appearance of these proteins on the cell surface is mutually exclusive. We used polyclonal antibodies raised against 30 degrees C (designated SerH3)- and 40 degrees C (designated SerT)-specific surface antigens to study their structure and expression. We showed that these surface proteins contain at least one disulfide bridge. On sodium dodecyl sulfate-denaturing polyacrylamide gels, the nonreduced 30 degrees C- and 40 degrees C-specific surface proteins migrated with molecular sizes of 69 and 36 kilodaltons, respectively. The reduced forms of the proteins migrated with molecular sizes of 58 and 30 kilodaltons, respectively. The synthesis of the surface proteins responded rapidly and with a time course similar to that of the incubation temperature. The synthesis of each surface protein was greatly reduced within 1 h and undetectable by 2 h after a shift to the temperature at which the protein is not expressed. Surface protein synthesis resumed by the end of 1 h after a shift to the temperature at which the protein is expressed. The temperature-dependent induction of these surface proteins appears to be dependent on the synthesis of new mRNA, as indicated by a sensitivity to actinomycin D. Surface protein syntheses were mutually exclusive except at a transition temperature. At 35 degrees C both surface proteins were synthesized by a cell population. These data support the potential of this system as a model for the study of the effects of environmental factors on the genetic regulation of cell surface proteins.

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21

Bannon, G. A., R. Perkins-Dameron, and A. Allen-Nash. "Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila." Molecular and Cellular Biology 6, no. 9 (September 1986): 3240–45. http://dx.doi.org/10.1128/mcb.6.9.3240.

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The presence of specific proteins (known as immobilization antigens) on the surface of the ciliated protozoan Tetrahymena thermophila is under environmental regulation. There are five different classes (serotypes) of surface proteins which appear on the cell surface when T. thermophila is cultured under different conditions of temperature or incubation medium; three of these are temperature dependent. The appearance of these proteins on the cell surface is mutually exclusive. We used polyclonal antibodies raised against 30 degrees C (designated SerH3)- and 40 degrees C (designated SerT)-specific surface antigens to study their structure and expression. We showed that these surface proteins contain at least one disulfide bridge. On sodium dodecyl sulfate-denaturing polyacrylamide gels, the nonreduced 30 degrees C- and 40 degrees C-specific surface proteins migrated with molecular sizes of 69 and 36 kilodaltons, respectively. The reduced forms of the proteins migrated with molecular sizes of 58 and 30 kilodaltons, respectively. The synthesis of the surface proteins responded rapidly and with a time course similar to that of the incubation temperature. The synthesis of each surface protein was greatly reduced within 1 h and undetectable by 2 h after a shift to the temperature at which the protein is not expressed. Surface protein synthesis resumed by the end of 1 h after a shift to the temperature at which the protein is expressed. The temperature-dependent induction of these surface proteins appears to be dependent on the synthesis of new mRNA, as indicated by a sensitivity to actinomycin D. Surface protein syntheses were mutually exclusive except at a transition temperature. At 35 degrees C both surface proteins were synthesized by a cell population. These data support the potential of this system as a model for the study of the effects of environmental factors on the genetic regulation of cell surface proteins.

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22

Tang, Shao Jun, and Erin M. Schuman. "Protein synthesis in the dendrite." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1420 (April 29, 2002): 521–29. http://dx.doi.org/10.1098/rstb.2001.0887.

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In neurons, many proteins that are involved in the transduction of synaptic activity and the expression of neural plasticity are specifically localized at synapses. How these proteins are targeted is not clearly understood. One mechanism is synaptic protein synthesis. According to this idea, messenger RNA (mRNA) translation from the polyribosomes that are observed at the synaptic regions provides a local source of synaptic proteins. Although an increasing number of mRNA species has been detected in the dendrite, information about the synaptic synthesis of specific proteins in a physiological context is still limited. The physiological function of synaptic synthesis of specific proteins in synaptogenesis and neural plasticity expression remains to be shown. Experiments aimed at understanding the mechanisms and functions f synaptic protein synthesis might provide important information about the molecular nature of neural plasticity.

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23

Jaleel, Abdul, Katherine A. Klaus, Dawn M. Morse, Helen Karakelides, Lawrence E. Ward, Brian A. Irving, and K. Sreekumaran Nair. "Differential effects of insulin deprivation and systemic insulin treatment on plasma protein synthesis in type 1 diabetic people." American Journal of Physiology-Endocrinology and Metabolism 297, no. 4 (October 2009): E889—E897. http://dx.doi.org/10.1152/ajpendo.00351.2009.

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It remains to be determined whether systemic insulin replacement normalizes synthesis rates of different plasma proteins and whether there are differential effects on various plasma proteins. We tested a hypothesis that insulin deprivation differentially affects individual plasma protein synthesis and that systemic insulin treatment may not normalize synthesis of all plasma proteins. We measured synthesis rates of 41 plasma proteins in seven each of type 1 diabetic (T1DM) and nondiabetic participants (ND) using [ ring-13C6]phenylalanine as a tracer. T1DM were studied while on chronic insulin treatment and during 8 h insulin deprivation. Insulin treatment normalized glucose levels, but plasma insulin levels were higher during insulin treatment than during insulin deprivation in T1DM and ND. Individual plasma proteins were purified by affinity chromatography and two-dimensional gel electrophoresis. Only 41 protein gel spots from over 300 were chosen based on their protein homogeneity. Insulin deprivation and hyperglycemia either significantly increased ( n = 12) or decreased ( n = 12) synthesis rates of 24 of 41 plasma proteins in T1DM compared with ND. Insulin treatment normalized synthesis rates of 13 of these 24 proteins, which were altered during insulin deprivation. However, insulin treatment significantly altered the synthesis of 14 additional proteins. In conclusion, acute insulin deprivation caused both a decrease and increase in synthesis rates of many plasma proteins with various functions. Moreover, chronic systemic insulin treatment not only did not normalize synthesis of all plasma proteins but also altered synthesis of several additional proteins that were unaltered during insulin deprivation.

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24

KURUMA, Yutetsu, and Takuya UEDA. "Cell-free Synthesis of Membrane Proteins." Seibutsu Butsuri 56, no. 3 (2016): 162–64. http://dx.doi.org/10.2142/biophys.56.162.

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25

van Kasteren, Sander. "Synthesis of post-translationally modified proteins." Biochemical Society Transactions 40, no. 5 (September 19, 2012): 929–44. http://dx.doi.org/10.1042/bst20120144.

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Post-translational modifications of proteins can have dramatic effect on the function of proteins. Significant research effort has gone into understanding the effect of particular modifications on protein parameters. In the present paper, I review some of the recently developed tools for the synthesis of proteins modified with single post-translational modifications at specific sites in the protein, such as amber codon suppression technologies, tag and modify, and native chemical ligation.

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26

Kent, Stephen B. H. "Chemical Synthesis of Peptides and Proteins." Annual Review of Biochemistry 57, no. 1 (June 1988): 957–89. http://dx.doi.org/10.1146/annurev.bi.57.070188.004521.

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27

HANSEN, PAUL ROBERT, ARNE HOLM, and GUNNAR HOUEN. "Solid-phase peptide synthesis on proteins." International Journal of Peptide and Protein Research 41, no. 3 (January 12, 2009): 237–45. http://dx.doi.org/10.1111/j.1399-3011.1993.tb00331.x.

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28

Katz, Y. "Synthesis of complement proteins in amnion." Journal of Clinical Endocrinology & Metabolism 80, no. 7 (July 1, 1995): 2027–32. http://dx.doi.org/10.1210/jc.80.7.2027.

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29

van der Heden van Noort, Gerbrand J., Herman S. Overkleeft, Gijsbert A. van der Marel, and Dmitri V. Filippov. "Synthesis of Nucleotidylated Poliovirus VPg Proteins." Journal of Organic Chemistry 75, no. 16 (August 20, 2010): 5733–36. http://dx.doi.org/10.1021/jo100757t.

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30

Wang, Yanxin J., D. Miklos Szantai-Kis, and E. James Petersson. "Semi-synthesis of thioamide containing proteins." Organic & Biomolecular Chemistry 13, no. 18 (2015): 5074–81. http://dx.doi.org/10.1039/c5ob00224a.

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To make thioamide protein folding experiments applicable to full-sized proteins, our laboratory has used a combination of native chemical ligation of thiopeptide fragments, unnatural amino acid mutagenesis to install fluorophore partners in expressed protein fragments, and chemoenzymatic protein modification to render these expressed protein ligations traceless.

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31

Suttie, J. W. "Synthesis of vitamin K‐dependent proteins." FASEB Journal 7, no. 3 (March 1993): 445–52. http://dx.doi.org/10.1096/fasebj.7.5.8462786.

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32

Katz, Y., S. Gur, M. Aladjem, and R. C. Strunk. "Synthesis of complement proteins in amnion." Journal of Clinical Endocrinology & Metabolism 80, no. 7 (July 1995): 2027–32. http://dx.doi.org/10.1210/jcem.80.7.7608250.

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33

Melnyk, Oleg, and Jérôme Vicogne. "Total chemical synthesis of SUMO proteins." Tetrahedron Letters 57, no. 39 (September 2016): 4319–24. http://dx.doi.org/10.1016/j.tetlet.2016.08.035.

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34

Burkoth, Timothy S., Eric Beausoleil, Surinder Kaur, Dahzi Tang, Fred E. Cohen, and Ronald N. Zuckermann. "Toward the Synthesis of Artificial Proteins." Chemistry & Biology 9, no. 5 (May 2002): 647–54. http://dx.doi.org/10.1016/s1074-5521(02)00140-0.

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35

Rose, Keith. "Facile synthesis of homogeneous artificial proteins." Journal of the American Chemical Society 116, no. 1 (January 1994): 30–33. http://dx.doi.org/10.1021/ja00080a004.

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36

CAULCOTT, C. "Temperature-induced synthesis of recombinant proteins." Trends in Biotechnology 4, no. 6 (June 1986): 142–46. http://dx.doi.org/10.1016/0167-7799(86)90164-2.

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37

Koenig, Edward. "Synthesis of proteins in vertebrate axons." Neurochemistry International 21 (January 1992): A4. http://dx.doi.org/10.1016/0197-0186(92)91910-o.

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38

Boatright, W. L., and G. Lu. "Hexanal Synthesis in Isolated Soy Proteins." Journal of the American Oil Chemists' Society 84, no. 3 (February 1, 2007): 249–57. http://dx.doi.org/10.1007/s11746-007-1036-6.

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39

Yang, Jerry, Irina Gitlin, Vijay M. Krishnamurthy, Jenny A. Vazquez, Catherine E. Costello, and George M. Whitesides. "Synthesis of Monodisperse Polymers from Proteins." Journal of the American Chemical Society 125, no. 41 (October 2003): 12392–93. http://dx.doi.org/10.1021/ja035978l.

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40

He, Mingyue, and Ming-Wei Wang. "Arraying proteins by cell-free synthesis." Biomolecular Engineering 24, no. 4 (October 2007): 375–80. http://dx.doi.org/10.1016/j.bioeng.2007.05.002.

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41

HILVERT, D. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 26, no. 34 (August 17, 2010): no. http://dx.doi.org/10.1002/chin.199534307.

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42

Sakakibara, Shumpei. "Chemical synthesis of proteins in solution." Biopolymers 51, no. 4 (1999): 279–96. http://dx.doi.org/10.1002/(sici)1097-0282(1999)51:4<279::aid-bip4>3.0.co;2-h.

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43

Cotton, Graham J., Maria C. Pietanza, and Tom W. Muir. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 32, no. 7 (May 30, 2010): no. http://dx.doi.org/10.1002/chin.200107248.

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44

Borgia, J. A., and G. B. Fields. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 31, no. 47 (November 21, 2000): no. http://dx.doi.org/10.1002/chin.200047263.

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45

Bayer, Ernst. "Towards the Chemical Synthesis of Proteins." Angewandte Chemie International Edition in English 30, no. 2 (February 1991): 113–29. http://dx.doi.org/10.1002/anie.199101133.

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46

Liu, Lei. "ChemInform Abstract: Chemical Synthesis of Proteins." ChemInform 44, no. 17 (April 4, 2013): no. http://dx.doi.org/10.1002/chin.201317232.

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47

Kraemer, Bjoern F., Stephan Lindemann, and Andrew S. Weyrich. "Protein degradation systems in platelets." Thrombosis and Haemostasis 110, no. 11 (2013): 920–24. http://dx.doi.org/10.1160/th13-03-0183.

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SummaryProtein synthesis and degradation are essential processes that allow cells to survive and adapt to their surrounding milieu. In nucleated cells, the degradation and/or cleavage of proteins is required to eliminate aberrant proteins. Cells also degrade proteins as a mechanism for cell signalling and complex cellular functions. Although the last decade has convincingly shown that platelets synthesise proteins, the roles of protein degradation in these anucleate cytoplasts are less clear. Here we review what is known about protein degradation in platelets placing particular emphasis on the proteasome and the cysteine protease calpain.

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48

Locke, M., E. G. Noble, and B. G. Atkinson. "Exercising mammals synthesize stress proteins." American Journal of Physiology-Cell Physiology 258, no. 4 (April 1, 1990): C723—C729. http://dx.doi.org/10.1152/ajpcell.1990.258.4.c723.

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Spleen cells, peripheral lymphocytes, and soleus muscles were removed from male Sprague-Dawley rats that had been run on a treadmill (24 m/min) for either 20, 40, or 60 min or to exhaustion (86 +/- 41 min) and were labeled in vitro with [35S]methionine at 37 degrees C. Similar tissues from nonrunning control rats were labeled in vitro at either 37 or 43 degrees C (heat shock). Fluorographic analyses of one- and two-dimensional polyacrylamide gel electrophoretic separations of the proteins from cells and tissues of exercised rats demonstrate the new or enhanced synthesis of proteins of approximately 65, 72, 90, and 100 kDa. Although synthesis of these proteins is low or not detectable in tissues from control rats labeled at 37 degrees C, they are prominent products of similar tissues labeled under heat-shock conditions (43 degrees C) and, in fact, correspond in Mr and pI with the so-called heat-shock proteins. These results suggest that exercise is a sufficient stimulus to induce or enhance the synthesis of heat shock and/or stress proteins in mammalian cells and tissues.

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Wang, Wen-Hung, Arunee Thitithanyanont, and Sheng-Fan Wang. "Synthesis, Assembly and Processing of Viral Proteins." Viruses 14, no. 8 (July 27, 2022): 1650. http://dx.doi.org/10.3390/v14081650.

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Franklin, James L., and Eugene M. Johnson. "Control of Neuronal Size Homeostasis by Trophic Factor–mediated Coupling of Protein Degradation to Protein Synthesis." Journal of Cell Biology 142, no. 5 (September 7, 1998): 1313–24. http://dx.doi.org/10.1083/jcb.142.5.1313.

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We demonstrate that NGF couples the rate of degradation of long-lived proteins in sympathetic neurons to the rate of protein synthesis. Inhibiting protein synthesis rate by a specific percentage caused an almost equivalent percentage reduction in the degradation rate of long-lived proteins, indicating nearly 1:1 coupling between the two processes. The rate of degradation of short-lived proteins was unaffected by suppressing protein synthesis. Included in the pool of proteins that had increased half-lives when protein synthesis was inhibited were actin and tubulin. Both of these proteins, which had half-lives of several days, exhibited no degradation over a 3-d period when protein synthesis was completely suppressed. The half-lives of seven other long-lived proteins were quantified and found to increase by 84–225% when protein synthesis was completely blocked. Degradation–synthesis coupling protected cells from protein loss during periods of decreased synthesis. The rate of protein synthesis greatly decreased and coupling between degradation and synthesis was lost after removal of NGF. Uncoupling resulted in net loss of cellular protein and somatic atrophy. We propose that coupling the rate of protein degradation to that of protein synthesis is a fundamental mechanism by which neurotrophic factors maintain homeostatic control of neuronal size and perhaps growth.

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