1. tissues Flashcards
summarise the lipid distribution in the plasma membrane
extracellular half;
phospholipid choline (PC), glycolipids
intracellular half;
Phosphatidylserine (PS), Phosphatidylethanolamine (PE) and Phosphatidylinositol (PI)
*cholesterol is distributed evenly between the two halves
phospholipids are a class of lipids containing a hydrophilic head (phosphate group) and two hydrophobic tails (fatty acids)
*heads face outwards.
uneven distribution of phospholipids (3 in the intracellular and 1 extracellular)
**lots of proteins associated with membrane
FRAP
Fluorescence recovery after photobleaching (FRAP) is a standard technique used to study the diffusion properties of biomolecules in artificial or cell membranes.
what does it mean that the proteins associated with the membrane are dynamic?
Dynamic Regulation of Plasma Membrane Protein Organization
Protein function is often directly coupled to lateral organization by clustering proteins in functional membrane domains or separating them in different domains. The formation of protein domains occurs over a broad range of length scales and is highly dynamic.
the “dynamic” nature of membrane-associated proteins means that they are constantly in motion, adjusting their positions, structures, and interactions to enable proper cellular responses and functions.
what type of adult cell does not generally replicate?
neurons
what is the nucleus of a cell important for?
for protein synthesis
what are some common components of an animal cell?
endosome
peroxisome
free polyribosomes
plasma membrane
nucleus
endoplasmic reticulum with membrane-bound polyribosomes
mitochondrion
golgi apparatus
lysosomes
cytosol
function of ER
The ER is the largest organelle in the cell and is a major site of protein synthesis and transport, protein folding, lipid and steroid synthesis, carbohydrate metabolism and calcium storage
golgi apparatus function
a factory in which proteins received from the ER are further processed and sorted for transport to their eventual destinations: lysosomes, the plasma membrane, or secretion.
spectrin and ankyrin
Spectrin and ankyrin are membrane skeletal proteins that contribute to mechanical support of plasma membranes and micron-scale organization of diverse membrane-spanning proteins.
summarise glucose uptake in the gut
epithelial tissue lines the gut with microvillus for increased surface area and therefore increased absorption.
Na+/K+ ATPase is important for maintaining the Na+ gradient, which drives the apical absorption of glucose in SGLT1.
Glucose enters the epithelial cells by a process catalyzed by the cotransporter SGLT-1. Intracellular cAMP activates the transepithelial transport by a mechanism possibly involving phosphorylation of SGLT-1. The glucose accumulated intracellularly can diffuse out of the cells by facilitated diffusion through GLUT2 into the blood stream.
*significantly more glucose transporters in apical membrane vs basal
[Sodium/glucose cotransporter 1]
Na+/K+ ATPase
The sodium-potassium pump system moves sodium and potassium ions against large concentration gradients. It moves two potassium ions into the cell where potassium levels are high, and pumps three sodium ions out of the cell and into the extracellular fluid.
3Na+ out
2K+ in
apical vs basal membrane
The membrane facing the lumen or free surface is known as the apical membrane, while the membrane oriented away from the lumen, contacting the extracellular matrix, is known as the basal membrane and the sides of the cell contacting the neighbouring cells form the lateral membrane
The Apical surface faces lumens or outside environments, showcasing Specialised systems for features including absorption or secretion. Contrastingly, the basal surface adheres to the basement membrane, offering structural help and anchorage to underlying tissues.
*significantly more glucose transporters in apical membrane vs basal in epithelial cells lining lumen of small intestine
mechanisms of protein transport
Protein sorting occurs through three mechanisms: gated transport, transmembrane transport, and vesicle transport, all utilizing sorting signals—short. Gated transport involves nuclear localization signals (NLS) allowing proteins to enter the nucleus via nuclear pores.
From the endoplasmic reticulum, proteins are transported in vesicles to the Golgi apparatus, where they are further processed and sorted for transport to lysosomes, the plasma membrane, or secretion from the cell.
secretory pathway of proteins
The secretory pathway ensures the transport of proteins from the endoplasmic reticulum (ER) via the Golgi complex to their destination compartment, such as the cell surface, the endosomes or the lysosomes
rough ER → Golgi → secretory vesicles → cell exterior
TIM/TOM complex mitochondria
The TIM/TOM complex is a protein complex in cellular biochemistry which translocates proteins produced from nuclear DNA through the mitochondrial membrane
TOM complex is outer membrane. TIM is inner membrane. TOM allows precursor protein to move through mitochondrial membrane. It then passes through TIM complex to pass into the mitochondrial matrix. (proteins within matrix will cleave signal peptide)
precursor protein
A protein precursor, also called a pro-protein or pro-peptide, is an inactive protein (or peptide) that can be turned into an active form by post-translational modification, such as breaking off a piece of the molecule or adding on another molecule.
Signal sequences are N-terminal extensions of nascent polypeptide chains that mediate protein targeting to the membrane of the endoplasmic reticulum (ER).
transcription vs translation
The process by which DNA is copied to RNA is called transcription, and that by which RNA is used to produce proteins is called translation.
translation
The process through which information encoded in messenger RNA (mRNA) directs the addition of amino acids during protein synthesis
- mRNA binds to the ribosome. mRNA binds to the ribosome. This binding is helped by the 5’ cap of the mRNA, which the ribosomes recognise and bind to. The poly-A tail of the mRNA also binds to the ribosome in order to increase translational efficiency.
- The ribosome reads the first codons. The ribosome reads the codons on the mRNA, beginning with the start codon “AUG”.
- A tRNA will bring the complementary amino acid for the first codon. Amino acids are found in the cytoplasm. Each specific tRNA has a complementary amino acid, and can bring it over. This is an ATP driven process (it requires the hydrolysis of ATP). As the start codon is “AUG”, the first amino acid will be methionine, brought by a tRNA with the anti-codon “UAC”.
- Another tRNA brings the second amino acid. The ribosome continues to read the next codon, and another tRNA brings the correct amino acid.
- The first tRNA leaves. The first tRNA is then released from the ribosome, and the second tRNA takes its place. This process is repeated for each codon that the ribosome reads.
- A peptide bond forms. A peptide bond forms between the two amino acids. An enzyme called aminoacyl transferase catalyses this.
- The process continues until a stop codon is reached. Ribosomes continue this process until they reach a stop codon on the mRNA. Stop codons are either “UAA”, “UGA”, or “UAG”. tRNAs do not have anti-codons for stop codons. Once the ribosome recognises the stop codon, a terminating factor catalyses the hydrolysis of the bonds between the final tRNA and the amino acid chain, which then releases the polypeptide chain.
- After translation, the polypeptide chains are folded. This folding is a spontaneous process but is also guided along by specialised proteins.
- Polypeptides can also undergo post-translational modifications. Modifications can occur. For example, carbohydrate chains can be added onto proteins, depending on the type of protein and its function. Also, all polypeptide chains start with methionine, but in some proteins this starting methionine can be cleaved off following translation.
- Proteins destined to leave the cell go to the rough ER. Proteins that need to be secreted from the cell are translated and folded in the rough endoplasmic reticulum. Ribosomes can recognise if a protein is meant to be secreted. If this is the case, the ribosomes will attach themselves to the rough endoplasmic reticulum, and the translated polypeptide chain will be released into the lumen of the endoplasmic reticulum where it will be folded and packaged for secretion and sent to the Golgi apparatus.
- Proteins destined to stay in the cell go to the cytoplasm. Proteins meant for use inside of the cell are synthesised and released into the cytoplasm.
SRP
The signal recognition particle (SRP) is a ribonucleoprotein particle essential for the targeting of signal peptide-bearing proteins to the prokaryotic plasma membrane or the eukaryotic endoplasmic reticulum membrane for secretion or membrane insertion.
SRP locks to ribosome and signal complex of protein. Whole protein SRP complex binds to receptor protein which omits opening of translocator and docking of translocator.
vesicles and protein transport
A vesicular transport protein, or vesicular transporter, is a membrane protein that regulates or facilitates the movement of specific molecules across a vesicle’s membrane. As a result, vesicular transporters govern the concentration of molecules within a vesicle.
The finished new proteins end up in the trans Golgi network, which packages them in transport vesicles and dispatches them to their specific destinations in the cell.
Newly formed protein buds off from vesicle when it fuses with plasma membrane. Secretory vesicle fuses with plasma membrane and protein is released through exocytosis.
which neurotransmitter does not get processed in ER?
acetyl choline
acetylcholine
neurotransmitter (released by neuron )
acetylcholine is released from nerve cells at the neuromuscular junction via calcium mediated exocytosis.
acetylcholine binds to receptors on skeletal muscle to cause contraction.
botox can block this muscle relaxation.
causes muscle contraction; botox prevents muscle contraction so can be used medically to prevent issues like muscle stiffness/excessive swearing but is now more often used for aesthetic purposes.
how does botox work?
SNARE- soluble NSF attachment protein receptor
v-SNAREs- found on vesicles
t-SNAREs located in the target membrane
botox cleaves SNARE proteins
fusing of vesicle to membrane for release of acetylcholine at the neuromuscular junction but botox cleaves this so acetylcholine is not released.
Botulinum Neurotoxin causes functional damage to SNARE proteins, which has significant physiological and medical implications. By damaging SNARE proteins, the toxin prevents synaptic vesicles from fusing to the synaptic membrane and releasing their neurotransmitters into the synaptic cleft.
function and main components of the cytoskeleton
cell shape
mechanical support for the cell and tissues
cellular locomotion
intracellular movements of cytoplasm, organelles and chromosomes
microfilaments
microtubules
intermediate filaments
*gives cell distinctive shape and is vital for movement of cells