Essay On Indomethacin

As discussed, galectin-8 is has different functions such as cell growth and apoptosis. When galectin-8 interacts with different integrins, high affinity interactions are formed. When galectin-8 is soluble, it inhibits the cell cycle and prompts the arrest of cell growth [6]. This is caused by a 4-5-fold increase in p21, which is a cyclin-dependent kinase inhibitor [6]. An increase in c-Junc-n-terminal kinases (JNK) and protein kinase B (PKB) activities cause an increase in the levels of p21. When galectin-8 cDNA is transfected into cells of human lung carcinoma, the inhibition of colon formation is noticed; this suggests that when galectin-8 is overexpressed, it may inhibit cell growth [6]. An experiment was done to examine the effects of galectin-8. There were multiple procedures that took place in this experiment; the generation of antibodies against galectin-8, the creation of cell cultures with human carcinoma cells, generation of GFP-galectin-8, generation of GHO cells overexpressing a mutant form of SEK1, the preparation of cell extracts, the binding of galectin-8 to Lactosyl-Agarose beads, Thymidine incorporation, apoptosis, PCR, and a Northern Blot Analysis.

Two of the main functions of galectin-8 are cell adhesion and cell growth. These functions also occur in the protease-resistant form of galectin-8. Galectin-8 is a type of protein that is secreted. When it is secreted, is serves a modulator for cell adhesion [3]. When the protein is stopped, it promotes cell adhesion. This occurs by ligation and gathering of a select group of integrin receptors [3]. Recall that galectin-8 is a sugar binding protein. Therefore, when there is a formation between galectin-8 and integrins, it activates integrin-mediated signaling [3]. When there are large amounts of galectin-8 present, it negative regulates cell adhesion with it forms a complex with integrins. Cell adhesion depends on the interactions between galectin-8

Certain drugs that are engaged in protein synthesis, differentiate between prokaryotic and eukaryotic ribosomes. (Streptomycin, Gentamicin, Chloramphenicol, Tetracycline, Erythromycin, Clindamycin, and Fusidic) Their therapeutic index is fairly high, but not as favorable as that of cell wall synthesis inhibitors. Streptomycin Binds with the 30S subunit of the bacterial ribosome to inhibit protein synthesis and causes misreading of mRNA. Chloramphenicol binds to the 50S ribosomal subunit and blocks peptide bond formation through inhibition of peptidyl transferase. Tetracycline bind to the 30S ribosomal subunit and interfere with aminoacyl-tRNA binding. Erythromycin and Clindamycin bind to the 50S ribosomal subunit and inhibit peptide chain elongation. Fusidic acid binds to EF-G and blocks translocation.

With modern advances to genome sequencing, whole genomes can now be used to rapidly identify protein encoding sequences from a small amount of amino acid sequences. This has led to a field of study called proteomics, which encompasses the study of proteins, protein complexes, and protein-protein interactions. As an example when one isolated protein is found to interact with a complex of proteins known to be part of an enzyme complex, it could be inferred that the isolated protein may be part of the enzyme complex as well. Some of the techniques involved for studying proteomics are interaction assays that allow for the rapid identification and purification of proteins.

Following phagocytosis, the transportation, uncoating and fusion of the phagosome vesicle are achieved by the recruitment of GTPase Rab proteins. Mtb blocks the conversion of Rab5 to Rab7, a fundamental process for phagosome maturation. Rab5 is found in early phagosomes, stimulating receptor-mediated endocytosis and clathrin-vesicle formation while Rab7 is associated with endosomal membrane trafficking of the late phagosome. Rab5 recruits the early endosomal autoantigen 1(EEA1) and hepatocyte growth factor-regulated tyrosine kinase(Hrs) which can bind to phosphatidylinositol-3-phosphate(PI3P) to promote phagosome maturation. PI3P is a lipid intermediate produced by Type III phosphatidylinositol-3-kinase(PI3K) on early endosomal and phagosomal membranes, significant for the recruitment of the vacuole GTPases. Mtb produces the lipid LAM and a PI3P phosphatase known as SapM, both targeting PI3P (Mario C.R., 2010). LAM was suggested that inhibits generation of PI3P by affecting the calcium/calmodulin pathway, important for recruitment of PI3K, while SapM degrades any remaining PI3P. As a result, EEA1 and Hrs cannot bind to PI3P, prohibiting phagosome maturation, hence Mtb resides in a phagosome with an abnormally high pH and limited fusion (Vojo D.,et al, 2006).

Proteases are categorised in six different groups. The first one is known as Serine Proteases which help digest food in the body and kill unwanted bacteria, they also assist the sperm penetrate the egg.

Chemists are seeking to learn about proteins and how they function not only together, but with other molecules. They are studying the fluctuation of these structures. They are questioning how proteins look when they merge with other proteins. The studies of how distinct proteins and other substances act together in the cell is called proteomics. This field of research is new, and

The de-ubiquitinase (DUB) will cleave this precursor into free monomer ubiquitin molecules and can be activated and attached to the target protein through ATP dependent process called ubiquitination with the help of activating enzyme E1, conjugating enzyme E2, and ligase E3. Through forming (iso)-peptide, thioester, or ester bond between carboxyl groups of C-terminal glycine 76 on ubiquitin and the ε-amino group of the lysine, cysteine, serine/threonine on the substrate, respectively, the poly-ubiquitin chain is formed [3]. Based on the different internal Lysine (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, and Lys63) and on the proximal ubiquitin, the (iso)-peptide bond can be form with another ubiquitin, distal mono-ubiquitin [4, 5]. Consequently, seven conventional poly-ubiquitin chains resulting in different 3-dimentional shapes explaining its different characteristics inherited upon binding to the target protein [5, 6]. With ranging more than 500 putative E3 ligases exist in human, the E3 ligase will tag the poly-ubiquitin chain to the target protein with high specificity

Gentamicin binds to specific DNA/RNA proteins and. specifically gentamicin binds to four proteins this leads to interference with the initiation complex, misreading of mRNA so the wrong amino acids sub groups are inserted into the polypeptide leading to Broken or toxic peptides and the breakup the

Ubiquitin is composed of 3 enzyme units, which facilitate the breakdown of proteins into amino acids, these are E1: ubiquitin activating enzyme, E2: ubiquitin-conjugating enzyme and E3: ubiquitin-protein ligase. Once targeted proteins are marked by ubiquitin for degradation, a proteasome will digest the protein and break it down into its constituent amino acids, while the ubiquitin is cleaved off and recycled for future use.

The crosslinked telopeptides that are released from type I collagen degradation by proteases during bone resorption generate neoepitopes (CTX-I, ICTP, NTX-I). The C-terminal telopeptide, CTX-I, as well the N-terminal telopeptide, NTX-I, when compared with ICTP, reflect different enzymatic pathways of bone breakdown, by cathepsin K or matrix metalloptoteinase-1 (MMP-1) cleavage of collagen type I, respectively.13

Previous studies have suggested that K63 ubiquitination is associated with anti-apoptotic protein trafficking pathways. Figure 1 addresses whether K63 ubiquitination is accomplished by the TRAF6 E3 ligase. An immunoblot of p53 was used for U2SO cells in a Ni-NTA assay to determine if K63-linked ubiquitination of p53 was associated with TRAF6. U2SO cells were used because of their high proliferation rates. Flag-TRAF6 and p53 were included in the western blot as controls for this assay. Ubiquitin was tagged with histidine and TRAF6 was tagged with the Flag antibody to assess protein to protein interactions. This assay shows ubiquitination of p53 in the presence of His-Ub and Flag-TRAF6 indicating that K63 linked ubiquitination of p53 depends on TRAF6. To determine if specifically, K63-linked ubiquitination occurs through TRAF6 the authors assessed whether TRAF6 promotes K48-linked ubiquitination of p53 and proteasomal degradation. An immunoblot for HA in a Ni-NTA pull-down assay was generated to assess if ubiquitination and proteasomal degradation occurs at K48 and K63 by TRAF6. HA-p53 and Flag-TRAF6 in U2SO cells were used to show protein-protein interaction. A

It (proteasome inhibitor) has been shown to have an effect on the growth in ATC cell lines alone and in combination with other drugs [40]. Combretastatin A4 phosphate (CA4P) It is a tubulin-binding compound. It is a vascular disrupting agent, resulting in reduced central blood flow to the tumor.

Mannose binding lectin is a member of a family of proteins called collectins (CLs), which

This alarm anti-protease is secreted at the site of injury in response to primary cytokines like interleukin-1 (IL-1) and tumour necrosis factor (TNF), making them possibly the first line of defence in the anti-proteinase network (Sallenave, 2000). Elafin is produced mainly by epithelia in the skin, upper gastrointestinal tract, female reproductive tract, lungs and in low levels in serum. Its secretion is upregulated in the presence of inflammatory stimuli or conditions such as psoriasis and acute respiratory distress syndrome (Shaw, 2011), although some research have shown that uncontrolled protease activity may lead to its proteolytic cleavage (Small, 2015). This was confirmed in a study by Guyot et al which demonstrated that the involvement of purified NE in