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Journal articles on the topic 'Protein synthesis'

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Published: 4 June 2021
Last updated: 25 May 2024

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1

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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2

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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3

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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4

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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5

Ruboyianes, Mark V., Min Chen, Mathew S. Dubrava, James E. Cherwa, and Bentley A. Fane. "The Expression of N-Terminal Deletion DNA Pilot Proteins Inhibits the Early Stages of φX174 Replication." Journal of Virology 83, no. 19 (July 29, 2009): 9952–56. http://dx.doi.org/10.1128/jvi.01077-09.

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ABSTRACT The φX174 DNA pilot protein H contains four predicted C-terminal coiled-coil domains. The region of the gene encoding these structures was cloned, expressed in vivo, and found to strongly inhibit wild-type replication. DNA and protein synthesis was investigated in the absence of de novo H protein synthesis and in wild-type-infected cells expressing the inhibitory proteins (ΔH). The expression of the ΔH proteins interfered with early stages of DNA replication, which did not require de novo H protein synthesis, suggesting that the inhibitory proteins interfere with the wild-type H protein that enters the cell with the penetrating DNA. As transcription and protein synthesis are dependent on DNA replication in positive single-stranded DNA life cycles, viral protein synthesis was also reduced. However, unlike DNA synthesis, efficient viral protein synthesis required de novo H protein synthesis, a novel function for this protein. A single amino acid change in the C terminus of protein H was both necessary and sufficient to confer resistance to the inhibitory ΔH proteins, restoring both DNA and protein synthesis to wild-type levels. ΔH proteins derived from the resistant mutant did not inhibit wild-type or resistant mutant replication. The inhibitory effects of the ΔH proteins were lessened by the coexpression of the internal scaffolding protein, which may suppress H-H protein interactions. While coexpression relieved the block in DNA biosynthesis, viral protein synthesis remained suppressed. These data indicate that protein H's role in DNA replication and stimulating viral protein synthesis can be uncoupled.
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6

Duncan, R. F., and J. W. Hershey. "Initiation factor protein modifications and inhibition of protein synthesis." Molecular and Cellular Biology 7, no. 3 (March 1987): 1293–95. http://dx.doi.org/10.1128/mcb.7.3.1293-1295.1987.

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The protein covalent modification state of eucaryotic initiation factors eIF-2 and eIF-4B in HeLa cells was examined after they were exposed to a variety of conditions or treatments that regulate protein synthesis. A few factors (e.g., variant pH and sodium fluoride) altered the phosphorylation state of the initiation factor proteins, but the majority (hypertonic medium, ethanol, dimethyl sulfoxide sodium selenite, sodium azide, and colchicine) had no effect on either protein. While initiation factor phosphorylation may regulate protein synthesis in response to many physiological situations, other pathways can regulate protein synthesis under nonphysiological circumstances.
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7

Duncan, R. F., and J. W. Hershey. "Initiation factor protein modifications and inhibition of protein synthesis." Molecular and Cellular Biology 7, no. 3 (March 1987): 1293–95. http://dx.doi.org/10.1128/mcb.7.3.1293.

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The protein covalent modification state of eucaryotic initiation factors eIF-2 and eIF-4B in HeLa cells was examined after they were exposed to a variety of conditions or treatments that regulate protein synthesis. A few factors (e.g., variant pH and sodium fluoride) altered the phosphorylation state of the initiation factor proteins, but the majority (hypertonic medium, ethanol, dimethyl sulfoxide sodium selenite, sodium azide, and colchicine) had no effect on either protein. While initiation factor phosphorylation may regulate protein synthesis in response to many physiological situations, other pathways can regulate protein synthesis under nonphysiological circumstances.
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8

Stephens, Samuel B., and Christopher V. Nicchitta. "Divergent Regulation of Protein Synthesis in the Cytosol and Endoplasmic Reticulum Compartments of Mammalian Cells." Molecular Biology of the Cell 19, no. 2 (February 2008): 623–32. http://dx.doi.org/10.1091/mbc.e07-07-0677.

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In eukaryotic cells, mRNAs encoding signal sequence-bearing proteins undergo translation-dependent trafficking to the endoplasmic reticulum (ER), thereby restricting secretory and integral membrane protein synthesis to the ER compartment. However, recent studies demonstrating that mRNAs encoding cytosolic/nucleoplasmic proteins are represented on ER-bound polyribosomes suggest a global role for the ER in cellular protein synthesis. Here, we examined the steady-state protein synthesis rates and compartmental distribution of newly synthesized proteins in the cytosol and ER compartments. We report that ER protein synthesis rates exceed cytosolic protein synthesis rates by 2.5- to 4-fold; yet, completed proteins accumulate to similar levels in the two compartments. These data suggest that a significant fraction of cytosolic proteins undergo synthesis on ER-bound ribosomes. The compartmental differences in steady-state protein synthesis rates correlated with a divergent regulation of the tRNA aminoacylation/deacylation cycle. In the cytosol, two pathways were observed to compete for aminoacyl-tRNAs—protein synthesis and aminoacyl-tRNA hydrolysis—whereas on the ER tRNA deacylation is tightly coupled to protein synthesis. These findings identify a role for the ER in global protein synthesis, and they suggest models where compartmentalization of the tRNA acylation/deacylation cycle contributes to the regulation of global protein synthesis rates.
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9

N. Marinov, Marin. "SYNTHESIS OF SOME NON-PROTEIN AMINO ACIDS DERIVED FROM SPIROHYDANTOINS." Journal Scientific and Applied Research 10, no. 1 (November 11, 2016): 39–46. http://dx.doi.org/10.46687/jsar.v10i1.204.

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This article presents a synthesis of non-protein amino acids derived from 6- and 8- substituted cyclohexanespiro-5-hydantoins, spiro(adamantane-2',4'-imidazolidine)- 2,5-dione and 3',4'-dihydro-2H,2'H,5H-spiro[imidazolidine-4,1'-naphthalene]-2,5-dione. The target compounds were prepared by an alkaline hydrolysis of the corresponding spirohydantoins with barium hydroxide. The products obtained were characterized by physicochemical parameters, IR , 1H and 13C NMR spectral data.
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10

Estrada, Andrea Lee, William Max Hudson, Paul Y. Kim, Claire Marie Stewart, Frederick F. Peelor, Yuren Wei, Dong Wang, Karyn L. Hamilton, Benjamin F. Miller, and Michael J. Pagliassotti. "Short-term changes in diet composition do not affect in vivo hepatic protein synthesis in rats." American Journal of Physiology-Endocrinology and Metabolism 314, no. 3 (March 1, 2018): E241—E250. http://dx.doi.org/10.1152/ajpendo.00209.2017.

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Protein synthesis is critical to protein homeostasis (proteostasis), and modifications in protein synthesis influence lifespan and the development of comorbidities associated with obesity. In the present study, we examined the acute response of liver protein synthesis to either high-fat or high-sucrose diets in order to elucidate nutrient-mediated regulation of hepatic protein synthesis in the absence of body fat accumulation. Total and endoplasmic reticulum-associated protein syntheses were assessed by use of the stable isotope, deuterium oxide (2H2O), in rats provided a control diet or diets enriched in polyunsaturated fat, saturated fat, or sucrose for 2, 4, or 7 days. The three experimental diets increased hepatic triglycerides 46–91% on day 7 and fasting insulin levels 83–117% on day 7, but did not result in differences in body weight when compared with control ( n = 6/diet/time). The fraction of newly synthesized proteins in total liver lysates and microsomes was not significantly different among dietary groups ( n = 3/diet/time). To determine whether the experimental diets provoked a transcriptional response to enhance the capacity for protein synthesis, we also measured a panel of genes linked to amino acid transport, synthesis, and processing. There were no significant differences in any of the genes measured among groups. Therefore, dietary treatments that have been linked to impaired proteostasis and that promote hepatic steatosis and insulin resistance, did not result in significant changes in total or ER-associated protein synthesis in the liver over a 7-day period.
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11

Nally, Jarlath E., John F. Timoney, and Brian Stevenson. "Temperature-Regulated Protein Synthesis by Leptospira interrogans." Infection and Immunity 69, no. 1 (January 1, 2001): 400–404. http://dx.doi.org/10.1128/iai.69.1.400-404.2001.

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ABSTRACT Leptospira interrogans is an important mammalian pathogen. Transmission from an environmental source requires adaptations to a range of new environmental conditions in the organs and tissues of the infected host. Since many pathogenic bacteria utilize temperature to discern their environment and regulate the synthesis of appropriate proteins, we investigated the effects of temperature on protein synthesis in L. interrogans. Bacteria were grown for several days after culture temperatures were shifted from 30 to 37°C. Triton X-114 cellular fractionation identified several proteins of the cytoplasm, periplasm, and outer membrane for which synthesis was dependent on the culture temperature. Synthesis of a cytoplasmic protein of 20 kDa was switched off at 37°C, whereas synthesis of a 66-kDa periplasmic protein was increased at the higher temperature. Increased synthesis of a 25-kDa outer membrane protein was observed when the organisms were shifted from 30 to 37°C. A 36-kDa protein synthesized at 30 but not at 37°C was identified as LipL36, an outer membrane lipoprotein. In contrast, expression of another lipoprotein, LipL41, was the same at either temperature. Immunoblotting with convalescent equine sera revealed that some proteins exhibiting thermoregulation of synthesis elicited antibody responses during infection. Our results show that sera from horses which aborted as a result of naturally acquired infection withL. interrogans serovar pomona type kennewicki recognize periplasmic and outer membrane proteins which are differentially synthesized in response to temperature and which therefore may be important in the host-pathogen interaction during infection.
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12

Walther, Udo Ingbert, Johannes Schulze, and Wolfgang Forth. "Inhibition of protein synthesis by zinc: comparison between protein synthesis and RNA synthesis." Human & Experimental Toxicology 17, no. 12 (December 1998): 661–67. http://dx.doi.org/10.1177/096032719801701203.

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Inhalation of zinc fumes may lead to the acute respiratory distress syndrome. The mechanisms of pulmonary zinc toxicity are not yet understood. Therefore we investigated zinc-dependent depression of protein and RNA synthesis in rat and human lung cell lines. 1 After exposure to 120 or 150 mmol/l zinc, RNA synthesis as assessed by uridine incorporation decreased by 60-70% between 0 and 2 h exposition in rat alveolar type II cells (L2 cells) and human fibroblast-like cells (11Lu and 16Lu cells), and by 90% between 0 and 4 h in carcinoma-derived cells (A549 cells). 2 After 2 h exposure, L2, 11Lu, and 16Lu cells were half-maximally inhibited by 50 mmol/l zinc, whereas A549 cells were more resistant with half-maximal inhibition at 100 mmol/zinc. 3 Protein and RNA synthesis was inhibited in parallel in L2, 11Lu, and A549 cells as indicated by simultaneous determination of uridine and amino acid incorporation. In 16Lu cells, the decline in protein synthesis preceded RNA synthesis inhibition. Pretreatment with RNA synthesis inhibitors (amanitin or actinomycin D) had no effect on time curve and intensity of RNA synthesis inhibition. Taken together, our results indicate that the suppression of RNA and protein synthesis likely are independent phenomena, due to direct zinc effects on these biosynthetic pathways.
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13

Conibear, Anne C., Emma E. Watson, Richard J. Payne, and Christian F. W. Becker. "Native chemical ligation in protein synthesis and semi-synthesis." Chemical Society Reviews 47, no. 24 (2018): 9046–68. http://dx.doi.org/10.1039/c8cs00573g.

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14

Jensen, P. E. "Protein synthesis in antigen processing." Journal of Immunology 141, no. 8 (October 15, 1988): 2545–50. http://dx.doi.org/10.4049/jimmunol.141.8.2545.

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Abstract Recent studies indicate that Ag pass through a chloroquine-sensitive intracellular pathway in accessory cells before they are recognized by class II-restricted T cells. Our results indicate that this is also true for insulin. Unexpectedly, we find that protein synthesis is required for optimal accessory cell-dependent processing of insulin and other proteins by adherent macrophages. Treatment of APC with inhibitors of protein synthesis, before and during exposure to Ag, inhibits their subsequent ability to activate murine T cell hybridomas. Experiments are described which suggest that this effect is localized to intracellular processing of Ag rather than uptake or presentation, per se. Inhibition is reversible, and is not observed in special situations where intracellular processing of Ag is not required. A distinct lag period is required for inhibition of processing after inhibition of macrophage protein synthesis. One possible interpretation is that protein synthesis is necessary for maintenance of a labile protein crucial for intracellular processing of Ag. Alternatively, the susceptibility of processing to inhibitors of protein synthesis may reflect an obligate intracellular association of Ag and newly synthesized class II histocompatibility molecules.
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15

Carvalho, J. C. Q., E. M. Miranda, C. C. P. Da Silva, V. A. David, T. E. L. De Souza, P. Kleine, L. B. De Almeida, and L. D. S. Abel. "PROTEIN SYNTHESIS GAME." Revista de Ensino de Bioquímica 2, no. 2 (May 15, 2004): 15. http://dx.doi.org/10.16923/reb.v2i2.147.

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The theoretical explanation of biological concepts, associated with the use of teaching games andmodels, intensify the comprehension and increase students interest, stimulating them to participateactively on the teaching-learning process. The sta of dissemination from Centro de BiotecnologiaMolecular Estrutural (CBME), in partnership with the Centro de Divulgac~ao Cientca e Cultural(CDCC), presents, in this work, a new educational resource denoted: Protein Synthesis Game. Theapproach of the game involves the cytological aspects of protein synthesis, directed to high schoolstudents. Students are presented to day-by-day facts related to the function of a given protein in thehuman body. Such task leads players to the goal of solving out a problem through synthesizing aspecied protein. The game comprises: (1) a board illustrated with the transversal section of animalcell, with its main structures and organelles and sequences of hypothetical genes; (2) cards with thedescription of steps and other structures required for protein synthesis in eukaryotic cells; (3) piecesrepresenting nucleotides, polynucleotides, ribosome, amino acids, and polypeptide chains. In order toplay the game, students take cards that sequentially permit them to acquire the necessary pieces forproduction of the protein described in each objective. Players must move the pieces on the board andsimulate the steps of protein synthesis. The dynamic of the game allows students to easily comprehendprocesses of transcription and translation. This game was presented to dierent groups of high schoolteachers and students. Their judgments have been heard and indicated points to be improved, whichhelped us with the game development. Furthermore, the opinions colleted were always favorable forthe application of this game as a teaching resource in classrooms.
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16

Moldave, K. "Eukaryotic Protein Synthesis." Annual Review of Biochemistry 54, no. 1 (June 1985): 1109–49. http://dx.doi.org/10.1146/annurev.bi.54.070185.005333.

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17

Kochendoerfer, Gerd G., and Stephen BH Kent. "Chemical protein synthesis." Current Opinion in Chemical Biology 3, no. 6 (December 1999): 665–71. http://dx.doi.org/10.1016/s1367-5931(99)00024-1.

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18

Wilken, Jill, and Stephen BH Kent. "Chemical protein synthesis." Current Opinion in Biotechnology 9, no. 4 (August 1998): 412–26. http://dx.doi.org/10.1016/s0958-1669(98)80016-5.

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19

Casi, G. "Convergent protein synthesis." Current Opinion in Structural Biology 13, no. 5 (October 2003): 589–94. http://dx.doi.org/10.1016/j.sbi.2003.09.008.

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20

Huot, Joshua R., and Susan T. Arthur. "Elevating Protein Synthesis." Medicine & Science in Sports & Exercise 50, no. 5S (May 2018): 806. http://dx.doi.org/10.1249/01.mss.0000538657.46065.89.

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21

Alewood, Paul, Martin Engelhard, and Stephen B. H. Kent. "Chemical protein synthesis." Journal of Peptide Science 16, no. 10 (September 16, 2010): 513. http://dx.doi.org/10.1002/psc.1291.

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22

Becker, Christian F. W., Ashraf Brik, Phil Dawson, and Christian P. R. Hackenberger. "Chemical protein synthesis." Journal of Peptide Science 20, no. 2 (January 20, 2014): 63. http://dx.doi.org/10.1002/psc.2607.

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23

Gupta, Naba K. "Eukaryotic protein synthesis:." Trends in Biochemical Sciences 12 (January 1987): 101–2. http://dx.doi.org/10.1016/0968-0004(87)90047-8.

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24

Leung, A. C., and E. E. McKee. "Mitochondrial protein synthesis during thyroxine-induced cardiac hypertrophy." American Journal of Physiology-Endocrinology and Metabolism 258, no. 3 (March 1, 1990): E511—E518. http://dx.doi.org/10.1152/ajpendo.1990.258.3.e511.

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The goal of this paper was to determine the effects of 3,5,3'-triiodothyronine (T3)-thyroxine-induced cardiac hypertrophy on the rates of synthesis of mitochondrial proteins by both the cytoplasmic and mitochondrial protein synthesis systems and to compare the results with total protein synthesis and cardiac enlargement. Daily injections of T3-thyroxine in the rat resulted in a 25% increase in the growth of the ventricle compared with controls. The cytoplasmic synthesis of both mitochondrial and total proteins as measured in the isolated perfused heart was stimulated by T3-thyroxine injection to a peak of 155 and 146%, respectively, of vehicle-injected controls after 3 days of hormone treatment. This peak was followed by a gradual decline in stimulation in total protein synthesis to 132% of control by 9 days of injection, whereas the decline in stimulation of cytoplasmic synthesis of mitochondrial proteins was significantly steeper, falling to 119% of vehicle control. The rate of protein synthesis within the mitochondrial compartment was also measured during the time course of T3-thyroxine-induced hypertrophy. These rates were measured in an isolated intact heart mitochondrial protein synthesis system described and characterized in the companion papers [E. E. McKee, B. L. Grier, G. S. Thompson, and J. D. McCourt. Am. J. Physiol. 258 (Endocrinol. Metab. 21): E492-E502, 1990; and E. E. McKee, B. L. Grier, G. S. Thompson, A. C. F. Leung, and J. D. McCourt. Am. J. Physiol. 258 (Endocrinol. Metab. 21): E503-E510, 1990]. Rates of mitochondrial protein synthesis were dramatically stimulated by T3-thyroxine injection.(ABSTRACT TRUNCATED AT 250 WORDS)
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25

Dash, Radha Charan, and Kyle Hadden. "Protein–Protein Interactions in Translesion Synthesis." Molecules 26, no. 18 (September 13, 2021): 5544. http://dx.doi.org/10.3390/molecules26185544.

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Translesion synthesis (TLS) is an error-prone DNA damage tolerance mechanism used by actively replicating cells to copy past DNA lesions and extend the primer strand. TLS ensures that cells continue replication in the presence of damaged DNA bases, albeit at the expense of an increased mutation rate. Recent studies have demonstrated a clear role for TLS in rescuing cancer cells treated with first-line genotoxic agents by allowing them to replicate and survive in the presence of chemotherapy-induced DNA lesions. The importance of TLS in both the initial response to chemotherapy and the long-term development of acquired resistance has allowed it to emerge as an interesting target for small molecule drug discovery. Proper TLS function is a complicated process involving a heteroprotein complex that mediates multiple attachment and switching steps through several protein–protein interactions (PPIs). In this review, we briefly describe the importance of TLS in cancer and provide an in-depth analysis of key TLS PPIs, focusing on key structural features at the PPI interface while also exploring the potential druggability of each key PPI.
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26

Walther, U. I., J. Schulze, and W. Forth. "Inhibition of protein synthesis by zinc: comparison between protein synthesis and RNA synthesis." Human & Experimental Toxicology 17, no. 12 (December 1, 1998): 661–67. http://dx.doi.org/10.1191/096032798678908116.

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27

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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28

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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29

Mendez, R., G. Kollmorgen, M. F. White, and R. E. Rhoads. "Requirement of protein kinase C zeta for stimulation of protein synthesis by insulin." Molecular and Cellular Biology 17, no. 9 (September 1997): 5184–92. http://dx.doi.org/10.1128/mcb.17.9.5184.

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The ability of insulin to stimulate protein synthesis and cellular growth is mediated through the insulin receptor (IR), which phosphorylates Tyr residues in the insulin receptor substrate-signaling proteins (IRS-1 and IRS-2), Gab-1, and Shc. These phosphorylated substrates directly bind and activate enzymes such as phosphatidylinositol 3'-kinase (PI3K) and the guanine nucleotide exchange factor for p21Ras (GRB-2/SOS), which are in turn required for insulin-stimulated protein synthesis, cell cycle progression, and prevention of apoptosis. We have now shown that one or more members of the atypical protein kinase C group, as exemplified by the zeta isoform (PKC zeta), are downstream of IRS-1 and P13K and mediate the effect of insulin on general protein synthesis. Ectopic expression of constitutively activated PKC zeta eliminates the requirement of IRS-1 for general protein synthesis but not for insulin-stimulated activation of 70-kDa S6 kinase (p70S6K), synthesis of growth-regulated proteins (e.g., c-Myc), or mitogenesis. The fact that PKC zeta stimulates general protein synthesis but not activation of p70S6K indicates that PKC zeta activation does not involve the proto-oncogene Akt, which is also activated by PI3K. Yet insulin is still required for the stimulation of general protein synthesis in the presence of constitutively active PKC zeta and in the absence of IRS-1, suggesting a requirement for the convergence of the IRS-1/PI3K/PKC zeta pathway with one or more additional pathways emanating from the IR, e.g., Shc/SOS/p21Ras/mitogen-activated protein kinase. Thus, PI3K appears to represent a bifurcation in the insulin signaling pathway, one branch leading through PKC zeta to general protein synthesis and one, through Akt and the target of rapamycin (mTOR), to growth-regulated protein synthesis and cell cycle progression.
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Gulve, E. A., and J. F. Dice. "Regulation of protein synthesis and degradation in L8 myotubes. Effects of serum, insulin and insulin-like growth factors." Biochemical Journal 260, no. 2 (June 1, 1989): 377–87. http://dx.doi.org/10.1042/bj2600377.

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We have examined the regulation of protein turnover in rat skeletal myotubes from the L8 cell line. We measured protein synthesis by the rates of incorporation of radiolabelled tyrosine into protein in the presence of a flooding dose of non-radioactive tyrosine. We monitored degradation of proteins labelled with radioactive tyrosine by the release of acid-soluble radioactivity into medium containing excess nonradioactive tyrosine. Extracellular tyrosine pools and intracellular tyrosyl-tRNA equilibrate rapidly during measurements of protein synthesis, and very little reutilization of the radiolabelled tyrosine occurs during degradation measurements. Measured rates of protein synthesis and degradation are constant for several hours, and changes in myotube protein content can be accurately predicted by the measured rates of protein synthesis and degradation. Most of the myotube proteins labelled with radioactive tyrosine for 2 days are degraded, with half-lives (t1/2) of approx. 50 h. A small proportion (less than 2.5%) of the radiolabelled proteins are degraded more rapidly (t1/2 less than 10 h), and, at most, a small proportion (less than 15%) are degraded more slowly (t1/2 greater than 50 h). A variety of agents commonly added to primary muscle cell cultures or to myoblast cell lines (18% Medium 199, 1% chick-embryo extract, antibiotics and antifungal agents) had no effect on rates of protein synthesis or degradation. Horse serum, fetal bovine serum and insulin stimulate protein synthesis and inhibit the degradation of long-lived proteins without affecting the degradation of short-lived proteins. Insulin-like growth factors (IGF)-1 and -2 also stimulate protein synthesis and inhibit protein degradation. The stimulation of protein synthesis and the inhibition of protein degradation are of similar magnitude (a maximum of approx. 2-fold) and display similar sensitivities to a particular anabolic agent. Insulin stimulates protein synthesis and inhibits protein degradation only at supraphysiological doses, whereas IGF-1 and -2 are effective at physiological concentrations. These and other findings suggest that IGFs may be important regulators of skeletal muscle growth during the fetal and early neonatal periods.
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Woo, David D. L., Ian Clark-Lewis, Brian T. Chait, and Stephen B. H. Kent. "Chemical synthesis in protein engineering: total synthesis, purification and covalent structural characterization of a mitogenic protein, human transforming growth factor-alpha." "Protein Engineering, Design and Selection" 3, no. 1 (1989): 29–37. http://dx.doi.org/10.1093/protein/3.1.29.

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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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Pinckaers, Philippe J. M., Michelle E. G. Weijzen, Lisanne H. P. Houben, Antoine H. Zorenc, Imre W. K. Kouw, Lisette CPGM de Groot, Lex B. Verdijk, Tim Snijders, and Luc JC van Loon. "The Muscle Protein Synthetic Response Following Ingestion of Corn Protein, Milk Protein and Their Protein Blend in Young Males." Current Developments in Nutrition 4, Supplement_2 (May 29, 2020): 651. http://dx.doi.org/10.1093/cdn/nzaa049_044.

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Abstract Objectives The muscle protein synthetic response to the ingestion of animal based proteins has been reported to be superior to the ingestion of plant based proteins. The lesser anabolic properties of plant based compared with animal based proteins has been attributed to differences in essential amino acid (EAA) contents and amino acid composition. This study compares post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein with the ingestion of 30 g corn protein or a blend of 30 g corn and milk protein in vivo, in young males. Methods In a randomized, double blind, parallel-group design, 36 healthy young males (26 ± 4 y) received a primed continuous infusion of L-[ring-13C6]-phenylalanine and ingested 30 g milk protein (MILK), 30 g corn protein (CORN), or a blend of 15 g corn protein plus 15 g milk protein (CORN + MILK) (n = 12 per group). Blood and muscle biopsies were collected for 5 h following protein ingestion to assess post-prandial plasma amino acid profiles and myofibrillar protein synthesis rates. Data were analyzed with 2-way repeated measures ANOVA and independent samples t-test. Data are expressed as mean ± SD. Results MILK increased plasma EAA concentrations more when compared to CORN (incremental area under curve (iAUC): 151 ± 31 vs 77 ± 19 mmol/L/300 min, respectively; P < 0.001). Both milk and corn protein ingestion increased myofibrillar protein synthesis rates (P < 0.001), with no differences between MILK and CORN (from 0.014 ± 0.014 to 0.053 ± 0.013 and from 0.017 ± 0.011 to 0.052 ± 0.013%/h, respectively; time*treatment P = 0.661). When MILK was compared to CORN + MILK, the iAUC for plasma EAA concentrations increased more in MILK when compared to CORN + MILK (151 ± 31 vs 126 ± 24 mmol/L/300 min, respectively; P = 0.036). Corn plus milk protein ingestion also increased myofibrillar protein synthesis rates (from 0.015 ± 0.015 to 0.052 ± 0.024%/h; P < 0.001), with no differences between MILK and CORN + MILK (time*treatment P = 0.823). Conclusions Ingestion of 30 g milk protein, 30 g corn protein, or a blend of 15 g corn plus 15 g milk protein increases muscle protein synthesis rates in vivo in young males. Post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein do not differ from rates observed after ingesting 30 g corn protein or a blend providing 15 g milk plus 15 g corn protein in vivo, in young males. Funding Sources TiFN.
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Skup, Małgorzata. "Dendrites as separate compartment – local protein synthesis [Review]." Acta Neurobiologiae Experimentalis 68, no. 2 (June 30, 2008): 305–21. http://dx.doi.org/10.55782/ane-2008-1697.

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The article summarizes the most meaningful studies which have provided evidence that protein synthesis in neurons can occur not only in cell perikarya but also locally in dendrites. The presence of the complete machinery required to synthesize cytoplasmic and integral membrane proteins in dendrites, identification of binding proteins known to mediate mRNA trafficking in dendrites and the ability to trigger “on-site” translation make it possible for the synthesis of particular proteins to be regulated by synaptic signals. Until now over 100 different mRNAs coding the proteins involved in neurotransmission and modulation of synaptic activity have been identified in dendrites. Local protein synthesis is postulated to provide the basic mechanism of fast changes in the strength of neuronal connections and to be an important factor in the molecular background of synaptic plasticity, giving rise to enduring changes in synaptic function, which in turn play a role in local homeostatic responses. Local protein synthesis points to some autonomy of dendrites which makes them “the brains of the neurons” (Jim Eberwine; from the interview with J. Eberwine – Barinaga 2000).
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Gessesse, Belay, Takashi Nagaike, Koji Nagata, Yoshihiro Shimizu, and Takuya Ueda. "G-Protein Coupled Receptor Protein Synthesis on a Lipid Bilayer Using a Reconstituted Cell-Free Protein Synthesis System." Life 8, no. 4 (November 2, 2018): 54. http://dx.doi.org/10.3390/life8040054.

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Membrane proteins are important drug targets which play a pivotal role in various cellular activities. However, unlike cytosolic proteins, most of them are difficult-to-express proteins. In this study, to synthesize and produce sufficient quantities of membrane proteins for functional and structural analysis, we used a bottom-up approach in a reconstituted cell-free synthesis system, the PURE system, supplemented with artificial lipid mimetics or micelles. Membrane proteins were synthesized by the cell-free system and integrated into lipid bilayers co-translationally. Membrane proteins such as the G-protein coupled receptors were expressed in the PURE system and a productivity ranging from 0.04 to 0.1 mg per mL of reaction was achieved with a correct secondary structure as predicted by circular dichroism spectrum. In addition, a ligand binding constant of 27.8 nM in lipid nanodisc and 39.4 nM in micelle was obtained by surface plasmon resonance and the membrane protein localization was confirmed by confocal microscopy in giant unilamellar vesicles. We found that our method is a promising approach to study the different classes of membrane proteins in their native-like artificial lipid bilayer environment for functional and structural studies.
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He, J., H. M. Cooper, A. Reyes, M. Di Re, H. Sembongi, T. R. Litwin, J. Gao, et al. "Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis." Nucleic Acids Research 40, no. 13 (March 27, 2012): 6109–21. http://dx.doi.org/10.1093/nar/gks266.

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Ozawa, Kiyoshi, Peter S. C. Wu, Nicholas E. Dixon, and Gottfried Otting. "15N-Labelled proteins by cell-free protein synthesis." FEBS Journal 273, no. 18 (September 2006): 4154–59. http://dx.doi.org/10.1111/j.1742-4658.2006.05433.x.

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38

Miller, Benjamin F., Christopher A. Wolff, Fredrick F. Peelor, Patrick D. Shipman, and Karyn L. Hamilton. "Modeling the contribution of individual proteins to mixed skeletal muscle protein synthetic rates over increasing periods of label incorporation." Journal of Applied Physiology 118, no. 6 (March 15, 2015): 655–61. http://dx.doi.org/10.1152/japplphysiol.00987.2014.

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Advances in stable isotope approaches, primarily the use of deuterium oxide (2H2O), allow for long-term measurements of protein synthesis, as well as the contribution of individual proteins to tissue measured protein synthesis rates. Here, we determined the influence of individual protein synthetic rates, individual protein content, and time of isotopic labeling on the measured synthesis rate of skeletal muscle proteins. To this end, we developed a mathematical model, applied the model to an established data set collected in vivo, and, to experimentally test the impact of different isotopic labeling periods, used 2H2O to measure protein synthesis in cultured myotubes over periods of 2, 4, and 7 days. We first demonstrated the influence of both relative protein content and individual protein synthesis rates on measured synthesis rates over time. When expanded to include 286 individual proteins, the model closely approximated protein synthetic rates measured in vivo. The model revealed a 29% difference in measured synthesis rates from the slowest period of measurement (20 min) to the longest period of measurement (6 wk). In support of these findings, culturing of C2C12 myotubes with isotopic labeling periods of 2, 4, or 7 days revealed up to a doubling of the measured synthesis rate in the shorter labeling period compared with the longer period of labeling. From our model, we conclude that a 4-wk period of labeling is ideal for considering all proteins in a mixed-tissue fraction, while minimizing the slowing effect of fully turned-over proteins. In addition, we advocate that careful consideration must be paid to the period of isotopic labeling when comparing mixed protein synthetic rates between studies.
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Vary, T. C., and S. R. Kimball. "Regulation of hepatic protein synthesis in chronic inflammation and sepsis." American Journal of Physiology-Cell Physiology 262, no. 2 (February 1, 1992): C445—C452. http://dx.doi.org/10.1152/ajpcell.1992.262.2.c445.

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The regulation of protein synthesis was determined in livers from control, sterile inflammatory, and septic animals. Total liver protein was increased in both sterile inflammation and sepsis. The rate of protein synthesis in vivo was measured by the incorporation of [3H]phenylalanine into liver proteins in a chronic (5 day) intra-abdominal abscess model. Both sterile inflammation and sepsis increased total hepatic protein synthesis approximately twofold. Perfused liver studies demonstrated that the increased protein synthesis rate in vivo resulted from a stimulation in the synthesis of both secreted and nonsecreted proteins. The total hepatic RNA content was increased 40% only in sterile inflammation, whereas the translational efficiency was increased twofold only in sepsis. The increase in translational efficiency was accompanied by decreases in the amount of free 40S and 60S ribosomal subunits in sepsis. Rates of peptide-chain elongation in vivo were increased 40% in both sterile inflammation and sepsis. These results demonstrate that sepsis induces changes in the regulation of hepatic protein synthesis that are independent of the general inflammatory response. In sterile inflammation, the increase in protein synthesis occurs by a combination of increased capacity and translational efficiency, while in sepsis, the mechanism responsible for accelerated protein synthesis is an increased translational efficiency.
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Fiorotto, Marta L., Teresa A. Davis, and Peter J. Reeds. "Regulation of myofibrillar protein turnover during maturation in normal and undernourished rat pups." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 278, no. 4 (April 1, 2000): R845—R854. http://dx.doi.org/10.1152/ajpregu.2000.278.4.r845.

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The study tested the hypothesis that a higher rate of myofibrillar than sarcoplasmic protein synthesis is responsible for the rapid postdifferentiation accumulation of myofibrils and that an inadequate nutrient intake will compromise primarily myofibrillar protein synthesis. Myofibrillar (total and individual) and sarcoplasmic protein synthesis, accretion, and degradation rates were measured in vivo in well-nourished (C) rat pups at 6, 15, and 28 days of age and compared at 6 and 15 days of age with pups undernourished (UN) from birth. In 6-day-old C pups, a higher myofibrillar than sarcoplasmic protein synthesis rate accounted for the greater deposition of myofibrillar than sarcoplasmic proteins. The fractional synthesis rates of both protein compartments decreased with age, but to a greater degree for myofibrillar proteins (−54 vs. −42%). These decreases in synthesis rates were partially offset by reductions in degradation rates, and from 15 days, myofibrillar and sarcoplasmic proteins were deposited in constant proportion to one another. Undernutrition reduced both myofibrillar and sarcoplasmic protein synthesis rates, and the effect was greater at 6 (−25%) than 15 days (−15%). Decreases in their respective degradation rates minimized the effect of undernutrition on sarcoplasmic protein accretion from 4 to 8 days and on myofibrillar proteins from 13 to 17 days. Although these adaptations in protein turnover reduced overall growth of muscle mass, they mitigated the effects of undernutrition on the normal maturational changes in myofibrillar protein concentration.
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Duncan, R. F., and J. W. Hershey. "Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation." Journal of Cell Biology 109, no. 4 (October 1, 1989): 1467–81. http://dx.doi.org/10.1083/jcb.109.4.1467.

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Incubating cells at elevated temperatures causes an inhibition of protein synthesis. Mild heat stress at 41-42 degrees C inhibits the fraction of active, polysomal ribosomes from greater than 60% (preheating) to less than 30%. A return to 37 degrees C leads to an increase in protein synthesis, termed "recovery." Continuous incubation at 41-42 degrees C also leads to a gradual restoration of protein synthesis (greater than 70% of ribosomes reactivated by 2-4 h), termed "adaptation". Protein synthesis inhibition and reactivation is prestressed, recovered cells that contain elevated levels of the heat stress proteins occur to the same extent and at the same rate as in "naive" cells. The adaptation response requires transcription of new RNA whereas recovery does not. A large number of phosphorylation changes are induced by severe heat stress and occur with kinetics similar to the inhibition of protein synthesis. These include phosphorylation of eukaryotic protein synthesis initiation factor (eIF)-2 alpha and dephosphorylation of eIF-4B and eIF-4Fp25 (eIF-4E). However, the extent to which the modification occurs is proportional to the severity of the stress, and, under mild (41-42 degrees C) heat stress conditions, these initiation factor phosphorylation changes do not occur. Similarly, under conditions of severe heat stress eIF-2 alpha and eIF-4B frequently recover to their prestress phosphorylation state before the recovery of protein synthesis. eIF-4E dephosphorylation likewise does not occur under mild heat stress conditions. Therefore, these changes in phosphorylation states, which are thought to be sufficient cause, are not necessary for the inhibition of protein synthesis observed.
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LaMorte, Joseph, Kaitlin Pensabene, Amanda Allender, and Aimee Eggler. "Oxidative Stress Suppresses Nrf2 Protein Synthesis through Global Protein Synthesis Inhibition." Free Radical Biology and Medicine 180 (February 2022): s62. http://dx.doi.org/10.1016/j.freeradbiomed.2021.12.141.

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43

Kimball, S. R. "The role of nutrition in stimulating muscle protein accretion at the molecular level." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 1298–301. http://dx.doi.org/10.1042/bst0351298.

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Nutrients act both directly and indirectly to modulate muscle protein accretion through changes in protein synthesis and degradation. For example, glucose, amino acids and fatty acids can all be metabolized to produce energy in the form of ATP that can be utilized for protein synthesis. In addition, amino acids are used directly for the synthesis of new proteins. Nutrients also regulate protein synthesis through activation of a signalling pathway involving the protein kinase, mTOR [mammalian TOR (target of rapamycin)]. Together with several regulatory proteins, mTOR forms a complex referred to as TORC1 (TOR complex 1). Because of its central role in controlling cell growth, TORC1 is an integral component of the mechanism through which nutrients modulate protein synthesis. Herein, the mechanism(s) through which nutrients, and in particular amino acids, regulate signalling through TORC1 will be discussed. In addition, downstream effectors of TORC1 action on mRNA translation will be briefly presented. Finally, a previously unrecognized effector of TORC1 signalling in regulating protein synthesis will be described.
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44

Rao, U. J., N. D. Denslow, and E. R. Block. "Hypoxia induces the synthesis of tropomyosin in cultured porcine pulmonary artery endothelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 267, no. 3 (September 1, 1994): L271—L281. http://dx.doi.org/10.1152/ajplung.1994.267.3.l271.

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The present study examined the effect of hypoxia on protein synthesis by porcine pulmonary artery endothelial cells (PAEC). Hypoxia decreased protein synthesis in PAEC, but two-dimensional gel electrophoresis of [35S]methionine-labeled PAEC proteins demonstrated the increased synthesis of a set of proteins having molecular masses (M(r)) of 35, 36.5, 45, 116, and 205 kDa. The synthesis of the 35-, 36.5-, and 45-kDa proteins was increased in preconfluent and postconfluent cells. The 35- and 45-kDa proteins were not induced by hyperthermia, whereas the 36.5-kDa protein was induced slightly by hyperthermia. Induction of the 36.5- and 45-kDa proteins required a minimum of 8 h of hypoxia, whereas induction of the 35-kDa protein required only 4 h of exposure to hypoxia. The upregulated synthesis of the 35-, 36.5-, and 45-kDa proteins was reversible with return to normoxia. Actinomycin D, an inhibitor of transcription, did not block the hypoxic induction of the 35- and 36.5-kDa proteins but did block induction of the 45-kDa protein. The partial amino acid sequence of the 35-kDa protein obtained from cyanogen bromide cleavage of the molecule was Asp-Ala-Ile-Lys-Lys-Lys-Met-Gln-Met-Leu-Lys-Leu-Asp-Lys-Glu. This partial sequence of the 35-kDa protein identically matches the sequence of tropomyosin. Amino acid composition data and the isoelectric point (4.8) were also typical of tropomyosin. Finally, specific cross-reactivity was detected between the 35-kDa protein and a monoclonal antibody to chicken gizzard tropomyosin on immunoblot. Thus hypoxia induces the synthesis of tropomyosin, a major microfilament-associated protein, in porcine PAEC in monolayer culture.
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45

Schreurs, V. V. A. M., G. Mensink, H. A. Boekholt, and R. E. Koopmanschap. "Relation of protein synthesis and amino acid oxidation: effects of protein deprivation." Netherlands Journal of Agricultural Science 33, no. 3 (August 1, 1985): 328–31. http://dx.doi.org/10.18174/njas.v33i3.16853.

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For up to 3 weeks 10 male rats weighing about 300 g were given diets which had 20% protein or were free from protein but supplied similar amounts of energy. The rats were killed at intervals; the last 2 were given L-[U-14C]tyrosine by infusion 4 h before they were killed. The deprived rats showed restricted amino acid oxidation and a decreased rate of protein synthesis. Amino acid oxidation continued by an uneven loss of proteins from the tissues. In muscle the composition and relative synthesis rate of the constituent proteins were not affected. Liver and kidney, compared with other tissues tended to maintain a relatively high rate of protein turnover. (Abstract retrieved from CAB Abstracts by CABI’s permission)
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46

Meuler, Debbie Crise, and GEORGE M. Malacinski. "An analysis of protein synthesis patterns during early embryogenesis of the urodele - Ambystoma mexicanum." Development 89, no. 1 (October 1, 1985): 71–92. http://dx.doi.org/10.1242/dev.89.1.71.

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Changes in protein synthesis during early Ambystoma mexicanum (axolotl) embryogenesis were monitored using two-dimensional (2-D) polyacrylamide gel electrophoresis. No change in synthesis patterns during progesterone-induced oocyte maturation was detected. In oocytes matured in vivo (unfertilized eggs), however, the synthesis of several oogenetic proteins ceased, only to be resumed later in development. At fertilization, one novel non-oogenetic protein was found. A cleavage-specific protein was also detected. Dramatic changes in protein synthesis patterns were detected at gastrulation in axolotl embryos. About 10% of the proteins synthesized at earlier stages ceased synthesis at gastrulation. Another 10% of the proteins synthesized during gastrulation were novel. A gastrulation-specific protein was also detected. After gastrulation additional novel nonoogenetic proteins were synthesized for most stages examined. A pronounced increase in the number of novel proteins synthesized was observed at the onset of neurulation and during neural fold fusion. Some of those proteins were specific to dorsal or axial structure tissue (AST) and some were specific to ventral or non-axial structure tissue (NAST). Actin and tubulin synthesis was also monitored during axolotl development. While the cytoplasmic γ- and β-actins were synthesized at all stages, muscle-specific α-actin synthesis began at the head-process stage (stage 23/25).
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47

Bowman, L. H. "The synthesis of ribosomal proteins S16 and L32 is not autogenously regulated during mouse myoblast differentiation." Molecular and Cellular Biology 7, no. 12 (December 1987): 4464–71. http://dx.doi.org/10.1128/mcb.7.12.4464-4471.1987.

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A series of mouse myoblast cell lines was constructed that contain 1 to 34 extra copies of either the S16 or the L32 ribosomal protein (r-protein) gene. The metabolism of the S16 and L32 r-proteins and mRNAs was examined in myoblasts and fibers of these cell lines to determine whether the synthesis of these r-proteins is autogenously regulated. The incorporation of extra copies of these r-protein genes into the genome resulted in the accumulation of the corresponding mRNAs to levels that were directly proportional to the gene copy number. The levels of the overproduced mRNAs decreased after the differentiation of mouse myoblasts into fibers in parallel to the decrease in the levels of the endogenous r-protein mRNAs. These results indicate that the synthesis of these r-proteins is not autogenously regulated at the level of transcription, RNA processing, or mRNA stability. To determine whether the synthesis of these r-proteins is regulated at the level of translation, the translational efficiencies of the overproduced mRNAs were inferred from their distribution in polysomal gradients. The translational efficiencies of these overproduced r-protein mRNAs in myoblasts are similar to those of the endogenous r-protein mRNAs. After myoblast differentiation, the translational efficiencies of the overproduced r-protein mRNAs decrease exactly like those of the endogenous r-protein mRNAs. Examination of the synthesis and stability of r-proteins in one of the L32-overproducing cell lines demonstrated that the overproduced L32 r-protein degrades shortly after its synthesis. The synthesis and stability of the other r-proteins were unaffected in this cell line. Thus, the synthesis of S16 and L32 r-proteins is not autogenously regulated at any level in either myoblasts or fibers.
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48

Bowman, L. H. "The synthesis of ribosomal proteins S16 and L32 is not autogenously regulated during mouse myoblast differentiation." Molecular and Cellular Biology 7, no. 12 (December 1987): 4464–71. http://dx.doi.org/10.1128/mcb.7.12.4464.

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A series of mouse myoblast cell lines was constructed that contain 1 to 34 extra copies of either the S16 or the L32 ribosomal protein (r-protein) gene. The metabolism of the S16 and L32 r-proteins and mRNAs was examined in myoblasts and fibers of these cell lines to determine whether the synthesis of these r-proteins is autogenously regulated. The incorporation of extra copies of these r-protein genes into the genome resulted in the accumulation of the corresponding mRNAs to levels that were directly proportional to the gene copy number. The levels of the overproduced mRNAs decreased after the differentiation of mouse myoblasts into fibers in parallel to the decrease in the levels of the endogenous r-protein mRNAs. These results indicate that the synthesis of these r-proteins is not autogenously regulated at the level of transcription, RNA processing, or mRNA stability. To determine whether the synthesis of these r-proteins is regulated at the level of translation, the translational efficiencies of the overproduced mRNAs were inferred from their distribution in polysomal gradients. The translational efficiencies of these overproduced r-protein mRNAs in myoblasts are similar to those of the endogenous r-protein mRNAs. After myoblast differentiation, the translational efficiencies of the overproduced r-protein mRNAs decrease exactly like those of the endogenous r-protein mRNAs. Examination of the synthesis and stability of r-proteins in one of the L32-overproducing cell lines demonstrated that the overproduced L32 r-protein degrades shortly after its synthesis. The synthesis and stability of the other r-proteins were unaffected in this cell line. Thus, the synthesis of S16 and L32 r-proteins is not autogenously regulated at any level in either myoblasts or fibers.
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Frare, Erica, Patrizia Polverino de Laureto, Elena Scaramella, Fiorella Tonello, Oriano Marin, Renzo Deana, and Angelo Fontana. "Chemical synthesis of the RGD-protein decorsin: Pro→Ala replacement reduces protein thermostability." Protein Engineering, Design and Selection 18, no. 10 (September 9, 2005): 487–95. http://dx.doi.org/10.1093/protein/gzi054.

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Watson, Emma E., and Nicolas Winssinger. "Synthesis of Protein-Oligonucleotide Conjugates." Biomolecules 12, no. 10 (October 20, 2022): 1523. http://dx.doi.org/10.3390/biom12101523.

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Nucleic acids and proteins form two of the key classes of functional biomolecules. Through the ability to access specific protein-oligonucleotide conjugates, a broader range of functional molecules becomes accessible which leverages both the programmability and recognition potential of nucleic acids and the structural, chemical and functional diversity of proteins. Herein, we summarize the available conjugation strategies to access such chimeric molecules and highlight some key case study examples within the field to showcase the power and utility of such technology.
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