Caveolin-1 : Lab Analysis

The virus fuses with the cell’s plasma membrane. The capsid proteins are removed, releasing the viral proteins and RNA. Reverse transcriptase catalyzes the synthesis of a DNA strand complementary to the viral RNA. Reverse transcriptase catalyzes the synthesis of a second DNA strand complementary to the first. The double-stranded DNA is incorporated as a provirus into the cell’s DNA. Proviral genes are transcribed into RNA molecules, which serve as genomes for the next viral generation and as mRNAs for translation into viral proteins. The viral proteins include capsid proteins and reverse transcriptase (made in the cytosol) and envelope glycoproteins (made in the ER). Vesicles transport the glycoproteins from the ER to the cell’s plasma membrane. Capsids are assembled around viral genomes and reverse transcriptase molecules. New viruses bud off from the host cell.

Cin1 regulates growth and pathogenesis of Cn and its function is linked to the human WASp homolog Wsp1 and the GTPase Cdc42 that regulate actin dynamics. Cin1 contains multiple protein domains that share certain similarity, but not identical, to human intersectin ITSN1. In contrast, Cin1 exhibits limited protein domain conservation with Saccharomyces cerevisiae (Sc) endocytic protein Pan1. No Cin1 homolog was identified in Sc, likewise, a Pan1 homolog was also not found in Cn. However, several proteins that are homologous to Sc proteins and function in the Pan1 pathway were identified from Cn, including the Eps15 (EH) protein Ede1 that is a functional partner of Pan1 in Sc. We hypothesize that the Cn Ede1 homolog is a component of the Cin1 pathway and that its functional characterization will allow for a better understanding of intracellular trafficking in Cn. Importantly, we have generated an ede1 mutant and will characterize Ede1 in comparison with Cin1 using complementary genetic and proteomic

There are two types of Endoplasmic Reticulum the Smooth ER and the Rough ER. you can distinguish that both of the ER’s are different to each other, this is shown in the diagram above that one is smooth ER and the other is rough ER the rough ER has ribsomes attracted to it while the smooth ER does not have ribosomes attached to it. The two ER’s have different function to each other.

The body has two faces, the cis face which fuses with incoming transport vesicles, and the trans face which excretes the secretory vesicles. The cis face fuses with vesicles coming from the ER effectively from many directions due to its convex shape, whereas the concave trans face can direct the secretory vesicles to their destination. When fusing with the cis face, the transport vesicles release their proteins to be absorbed for modification. Each cisternal layer of the Golgi body holds different enzymes which each modify the passing proteins in separate ways. Between the layers the proteins are moved through the gaps by small vesicles. When a protein has been modified correctly, it leaves the Golgi body via secretory vesicles which then carry the modified proteins to the cell membrane or another organelle. The proteins that are transported to the cell membrane are either excreted from the cell, or absorbed into the membrane to aid with its function. Some of the secretory vesicles which hold hydrolytic enzymes stay within the cytoplasm and function as lysosomes.

Brennan K, Tateson R, Lewis K, Arias AM. A Functional Analysis of Notch Mutations in Drosophila. Genetics. 1997;147(1):177-188.

Sometimes, an electron dense thin line can be seen underneath hemidesmosomes, outside the cell and adjacent to the plasma membrane. This structure is referred to as the sub-basal dense plate. The hemidesmosome is composed of at least 5 distinict molecules: (1) bullous pemphigoid antigen 1 (BPAG1), (2) plectin, (3) integrins, (4) collagen XVII (BPAG2) (5) CD151. The first two molecules, BPAG1 and plectin, are found within the basal keratinocyte, and have been localized to the inner plaque of the hemidesmosome.[13]

3. A vesicle is formed at the end of the rER with the protein inside.

Notch signalling pathway mediate the cell-cell interactions that occur throughout C. elegans embryogenesis. These interactions are important in tissue morphogenesis and in specifying cell fates. In the C. elegans embryo, the REF-1 family of basic-helix-loop-helix(bHLH) transcription factors are the major targets of Notch signalling. According to Priess (2005), there are two closely-related proteins in Notch family of the transmembrane receptors in C. elegans known as GLP-1 and LIN-12.

Out of these 31 exons, there are exons known as CREB domains that manage different TFs. Domains include: nuclear receptor interaction domain (NRID), transactivation zinc domains (TAZ1&2-cystein regions), CREB and MYB interaction domain (KIX), the bromo domain (bromo), histone acetyltransferase domain (HAT), and nuclear coactivator binding domain (NCBD), essentially in that order on the CREBBP gene sequence. Mutations can occur at any of these exons, but the most notable mutations occur at the HAT domain. This is due largely because when the protein is not acetylated the promoter site cannot be accessed by TFs [5]. This results in essential proteins for development not being produced, thus causing developmental anomalies. One such anomaly is the Rubenstein-Taybi syndrome (RTS), which is associated directly with CREBBP mutations [8]. Mutations in CREBBP are also associated with Huntington’s disease and acute myeloid leukemia, due to chromosomal

Endocytosis is the capacity to disguise material from outside the cell is critical for a few cell forms including the ingestion of fundamental supplements, expulsion of dead or harmed cells from the body, and guard against microorganisms. Eukaryotic cells disguise liquid, extensive and little particles, and even different cells from their surroundings by a procedure called endocytosis. Amid endocytosis, the plasma layer of the cell frames a pocket around the material to be disguised. The pocket closes and afterward isolates from within surface of the plasma layer to shape a film encased air pocket, or vesicle, containing the ingested

Cytotoxin associated gene A contains a stored pattern at the C- terminus known as the conserved repeat responsible for phosphorylation independent activity (CRPIA) [34]. This motif interacts with β-catenin-E-cadherin complex [35-37], hepatocyte growth factor receptor (MET)[38, 39], phospholipase C gamma (PLC-γ)[40], and partitioning-defective 1b/microtubule affinity-regulating kinase 2 (PAR1b/MARK2) [41-43] [44, 45] It has also been associated with JAK/STAT3 [31]. These interactions lead to cellular responses that promote inflammation, uncontrolled replication, disruption of neighboring cells communication, loss of cell function, loss of cell shape and loss of cell structure [34]. Unphospoporylated Cytotoxin associated gene A also affects zonula occludens 1 (ZO-1) which are proteins essential for epithelial tight junction by dislocating it from its cellular location [46] [47]. It also interrupts the junctional adhesion molecule A (JAM-A), producing dysfunctional construction of cell junctions [48].A variety of studies suggest that Cytotoxin associated gene A interact with PAR1b/MARK2, a crucial regulator of cell function and structure. Cytotoxin associated gene A disrupts its activity by affecting the alignment of microtubule arrangement, in this way causing a loss of cell polarity [49] [22] [47]. PAR1b binds to the CM or CagA multimerization of CagA that is involve in the CagA dimerization [50]

James Rothman dissected the transport mechanism by purifying and identifying proteins used in transport. The NSF, SNAP and SNARE proteins act as docking sites to enable vesicles to fuse to specific target membranes. This explains the precision of transport; the proteins only combined with certain cargo. The ability to purify the NSF protein was made possible by the identification of the VSV-G protein. The VSV-G protein is labeled by a sugar when it comes in contact with the Golgi Apparatus, simplifying documentation. Genes code for proteins used in fusion, exemplified by how the sec18 gene relates to NSF. Sec17 relates to the SNAP protein in a similar manner. The discovery of the SNAP protein allowed for the revelation of SNARE proteins found in brain tissue. SNARE proteins are a gateway to the fusion and docking of vesicles in a very specific manner: only an exclusive number of target SNAREs (t-SNAREs) would bind to specific vesicle SNAREs, or v-SNAREs

To determine the total phenolic content using Folin-Ciocalteu (FC) reagent. Theory: Plants produce a diversity of phenolic metabolites with one or more acidic OH-groups attached to a phenyl ring. Phenolic compounds are excellent oxygen radical scavengers as the electron reduction potential of the phenolic radical is lower than the electron reduction potential of the oxygen radicals. Also phenoxyl radicals are generally less reactive than oxygen radicals.

Exosomes are membranous vesicles enclosed in lipid bilayers with diameter of 30-100nm and are responsible in carrying cytoplasmic proteins such as Rab proteins and actin-binding proteins and signal transduction molecules such as G-proteins and protein kinases, as well as some heat-shock proteins like Hsp70 and tetraspanins like CD9 [5-30]. Exosomal proteins can directly represent the specific profiles of their cells of origin, for

The endoplasmic reticulum (ER) is an essential organelle that is a major place for the biogenesis of cellular components including proteins, lipids, and carbohydrates and internal calcium storage. ER is primarily responsible for protein translocation, protein folding and protein post modification. Proper folding of protein in the ER is accomplished with the aid of ER resident proteins or enzymes such as chaperones. Binding of chaperones to