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Translation: Making Protein Synthesis Possible

One of the most important activities of a cell is the production of proteins that fulfill major roles in the cell--structural, enzymatic, hormonal, and more. Chromosomes never leave the nucleus of the cell. However, protein synthesis is carried out by the , small structures which either float freely in the cytoplasm or are attached to membrane networks that snake their way through the cell—both outside the nucleus.

This section will explain briefly and superficially the way the instructions reach the ribosomes and how they are translated into the language of proteins. This information is not critical for understanding the use of DNA for genealogy but does form a foundation for understanding the way genetic mutations are expressed and a basis for understanding genetic differences.

A protein is a chainlike molecule built of subunits of smaller molecules called amino acids. We obtain most of our amino acids by digesting proteins taken in with our food. The digestive process breaks the protein chains down into individual amino acid molecules which are then absorbed by the blood and transported to the individual body cells. Human cells can also manufacture some amino acids. However, eight of the amino acids that are essential to building human proteins must be acquired from food. They eight essential amino acids are phenylalanine, valine, leucine, isoleucine, lysine, threonine, tryptophan and methionine. Histidine is essential for infants but not for adults.

The rough ER has ribosomes attached to it, and is the site for protein synthesis.

72. Perey L, Hayes DF, Maimonis P, Abe M, O'Hara C, Kufe DW. Tumor selective reactivity of a monoclonal antibody prepared against a recombinant peptide derived from the DF3 human breast carcinomaassociated antigen. 1992;52:2563-8

Labeled Parts Of A Protein - Wiring And Parts Diagram

Smooth ER is devoid of ribosomes, and is the site for lipid synthesis and protein transport.

Medarova . synthesized a breast tumor-targeted nanodrug designed to specifically shuttle siRNA to human breast cancer while simultaneously allowing for the noninvasive monitoring of the siRNA delivery process []. The nanodrug consisted of SPIONs for MRI monitoring, Cy5.5 fluorescence dye for near-infrared (IR) optical imaging, and siRNA to target the tumor-specific antiapoptotic gene . Magnetic iron oxide nanoparticles are extensively used as multimodal imaging probes in combination with optical fluorescence dyes to obtain the benefits of optical imaging, such as rapid screening and high sensitivity. Because tumor-associated underglycosylated mucin-1 (uMUC-1) antigen is overexpressed in >90% of breast cancers and in >50% of all cancers in humans [], researchers have decorated nanodrugs with uMUC-1-targeting EPPT synthetic peptides for selective tumor targeting. As shown in Figure A, amine-functionalized superparamagnetic iron oxide nanoparticles with a cross-linked dextran coating (MN) have been prepared, and a Cy5.5 dye was conjugated to the surface of nanoparticles to produce MN-Cy5.5. Subsequently, thiol-modified, FITC-labeled EPPT peptides and siRNA were coupled to MN-Cy5.5 via a heterofunctional cross-linker, -succinimidyl 3-(2-pyridyldithio) propionate (SPDP). The resulting therapeutic and diagnostic nanodrug (MN-EPPT-siBIRC5) exhibited superparamagnetic and fluorescence properties. After intravenous injection of the nanodrugs into mice with BT-20 breast tumors, the tumors were clearly imaged, as verified simultaneously by T2 MRI and near-IR optical imaging (Figure B). Systemic administration of the nanodrug once a week over 2 weeks induced considerable levels of necrosis and apoptosis in the tumors as a result of the siBIRC5-mediated inhibition of the antiapoptotic survivin protooncogene, translating into a significant decrease in tumor growth rate (Figure C). This tumor-targeted, imaging-capable nanodrug highlights the potential of MRI-guided tumor treatment, which can be used to quantify changes in the tumor volume over the treatment schedule as well as to guide selection of an optimal treatment time course.

Lee decorated liposomal Dox with a lung tumor targeted peptide []. Lung cancer is the leading cause of death due to cancer, and its high mortality rate appears to derive from a low therapeutic index for chemotherapy and late detection due to a lack of sensitive diagnostic biomarkers []. The identification of novel biomarkers for early lung cancer detection remains a challenge. In this study, a novel peptide (CSNIDARAC) with a high binding affinity for lung tumors was identified by screening of a phage display peptide library, and CSNIDARAC peptide-conjugated liposomal Dox (Lipo-Dox) was synthesized. The tumor targeting capabilities and the therapeutic efficacy were evaluated in the H460 tumor xenograft mice. To minimize the interactions between the targeted peptide and the surface of the liposome, the amount of PEG on the surface of the liposome was reduced from 5-20 mol% (general use) to 1.3 mol% of total lipids. Tumor growth inhibition of the peptide-targeted Lipo-Dox was superior to that of the untargeted Lipo-Dox or free Dox administered at an equivalent dose, and this result was consistent with the levels of apoptosis measured by TUNEL staining. Near-IR Cy7.5 dye-labeled peptide-conjugated Lipo-Dox also showed a distinct fluorescence signal at the tumor, whereas untargeted Lipo-Dox did not show such a strong signal intensity, suggesting the potential utility of this lung tumor-targeting peptide as a diagnostic agent.

Mar 12, 2014 · In protein synthesis the ..

This is site of synthesis for proteins destined for secretion, lysosomes, or membranes.

Cell wall: Protects the cell from the outside environment and maintains the shape of the cell. It also prevents the cell from bursting if internal pressure rises.

Plasma membrane: Semi-permeable membrane that controls the substances moving into and out of the cell. It contains integral and peripheral proteins. Substances pass through by either active or passive transport.

Cytoplasm: Contains many enzymes used to catalyze chemical reactions of metabolism and it also contains the DNA in a region called the nucleoid. Ribosomes are also found in the cytoplasm.

Pili: Help bacteria adhere to each other for the exchange of genetic material.

Flagella (singular flagellum): Made of a protein called flagellin. Helps bacteria move around by the use of a motor protein that spins the flagellum like a propeller.

Ribosomes: They are the site of protein synthesis. Contributes to protein synthesis by translating messenger RNA.

Nucleoid: Region containing naked DNA which stores the hereditary material (genetic information) that controls the cell and will be passed on to daughter cells.

BIO 301
Human Physiology
Physiology - science that describes how organisms FUNCTION andsurvive in continually changing environments
Levels of Organization:CHEMICAL LEVEL - includes all chemical substances necessary for life(see, for example, a small portion - a - of a hemoglobin molecule); together form the next higher levelCELLULAR LEVEL - cells are the basic structural and functional unitsof the human body & there are many different types of cells (e.g.,muscle, nerve, blood, and so on)LEVEL - a tissue is a group of cells that perform a specific function andthe basic types of tissues in the human body include epithelial, muscle,nervous, and connective tissuesORGAN LEVEL - an organ consists of 2 or more tissues that perform aparticular function (e.g., heart, liver, stomach, and so on)SYSTEM LEVEL - an association of organs that have a common function;the major systems in the human body include ,,,,,,and .

This video about protein synthesis looks like an excellent tool for exam preparation. There are nice review slides at the end.
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Protein synthesis takes place in the direction 5' → 3'.

Dispersed in the cytoplasm, and also present in conjunction with the rough ER, they are responsible for synthesizing the proteins required for various cellular processes.

Gene Expression | Protein Synthesis

The nucleus is surrounded by the nuclear membrane.
ribosome - small organelles composed of RNA-rich cytoplasmic granules that are sites of protein synthesis.
rough endoplasmic reticulum - (rough ER) a vast system of interconnected, membranous, infolded and convoluted sacks that are located in the cell's cytoplasm (the ER is continuous with the outer nuclear membrane).

Ribosome plays a vital role in protein synthesis as they ..

You must understand this to make sense of what is to come. Control of protein exit from the ER.Some proteins are retained in the ER (for example, the enzymes that make the oligosaccharides that are added to proteins) These proteins carry an ER retention signal (KDEL or MDEL sequence) at their carboxyl ends.

They are the site of protein synthesis.

They often require theexpenditure of energy to help compounds move across the membraneCells, cytoplasm, and : - controls cell function via transcriptionand translation (in other words, by controlling protein synthesis in acell)- DNA is used to produce mRNA- mRNA then moves from the nucleus into the cytoplasm & is usedto produce a protein

by controlling protein synthesis in a cell) ..

Nanoporous silica offers a higher surface area and binding capacity for therapeutic and diagnostic agents compared to similarly sized liposomes, and, therefore, provides an attractive drug delivery system. Multicomponent cargos are easily loaded onto nanoporous silica cores, and the resultant nanocarriers can potentially be used for targeted multicomponent delivery. Ashley . developed porous silica nanoparticle-supported lipid bilayers (protocells, 100-150 nm in diameter) that synergistically combined the features of mesoporous silica particles and liposomes to address the multiple challenges of targeted delivery (Figure ) []. Protocells were modified with an SP94-targeted peptide that binds to human hepatocellular carcinoma and a histidine-rich fusogenic peptide that promotes endosomal escape of the protocells and cytosolic dispersion of the encapsulated cargos. The nanoporous support resulted in greater stability and enhanced lateral bilayer fluidity compared with both liposomes and non-porous particles, thereby promoting multivalent interactions between the protocell and the target cancer cell using a minimal number of targeting peptides via peptide recruitment to the cell surface. The high surface area and porosity of their nanoporous cores conveyed a one-thousand-fold higher capacity of the protocells for Dox than the similarly sized liposomes. The unique properties of protocells solve the problem of simultaneously achieving high targeting specificity, high cytotoxicity toward the target cell, and low collateral damage to non-cancerous cells. Cell viability tests indicated that Dox-loaded protocell treatment maintained greater than 90% normal hepatocyte viability while killing nearly 97% MDR1+ hepatocellular carcinoma (Hep3B). In contrast, Dox-loaded liposomes or protocells without fluidity on their surface were less efficient at killing Hep3B and caused considerable cytotoxicity to non-cancerous cells. The Dox-loaded protocells demonstrated good therapeutic ability compared to both free Dox and Dox-loaded liposomes.

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