IMMS Flashcards

1
Q

Mitochondria

A
o	double membrane
o	cristae
o	matrix (Kreb’s cycle)
o	inner membrane (oxidative phosphorylation
o	produces ATP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Endoplasmic reticulum

A

o rough – ribosomes for protein production

o smooth - lipid production

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Golgi apparatus

A

o receives proteins and lipids from endoplasmic reticulum

o modifies and packages them into vesicles for transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Vesicles

A

o lipid bilayer

o 3 types – lysosome, secretory and transport vesicles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Cytoskeleton

A
o	Function - keeps cell shape and organises parts of cell
o	Structure:
▪	Microtubules
▪	microfilaments (actin)
▪	intermediate filaments
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Cell energy storage

A

o lipofuscin is droplet deposits around nucleus (increase with age)
o lipid droplets found mainly in adipose tissue
o glycogen is main cell storage of glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Cell membrane

A
o	phospholipid bilayer
o	interspersed with proteins, carbohydrates and cholesterol
o	function:
▪	protects the cell from outside,
▪	selectively permeable to ions
▪	transport in and out of cell
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Transporter proteins

A

o Transmembrane
o move substances in and out of cell vie facilitated diffusion or active transport
● Desmosome:

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Desmosomes

A

o specialised for cell to cell adhesion

o protein complexes found in the cell membrane of epithelial cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Cell surface receptor

A

o bind to external ligand and convert extracellular information into intracellular information
o 3 types:
▪ ion channel - opens
▪ G protein - activates protein to open ion channel
▪ enzyme linked - receptor linked to intracellular enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Endocytosis

A

(movement into cell)

  1. Molecules bind to receptors in clathrin-coated pit in cell membrane
  2. pits bud to form clathrin-coated vesicles
  3. vesicle fuses with intracellular endosome
  4. contents are either transported to lysosome or recycled into cell membrane
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Exocytosis

A

out of cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Diffusion

A

movement of a molecule from an area of high concentration to an area of low concentration (down conc gradient)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Facilitated diffusion

A

normal diffusion through a transmembrane protein – useful for large/polar molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Active transport

A

movement of molecules against concentration gradient – requires ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Homeostasis

A

the maintenance of stable internal conditions within the body

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Cell communication

A

o autocrine - within same cell
o paracrine - signal affects nearby cells
o endocrine - signal secreted into blood

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Feedback

A

o positive = amplification of process – chain reaction)

o negative = result of action inhibits another action

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Water distribution within the body- 42kg

A

2/3 (28kg) Intracellular F
1/3 (14kg) ECF:
-3L= plasma
-11L= interstitial fluid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Osmoregulation

A
  1. low water levels detected by hypothalamic osmoreceptors
  2. Osmoreceptors sends signal to pituitary to release ADH
  3. ADH travels to kidney and causes increased fluid uptake
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Fluid loss

A

o sensible can be measured - urine, faeces, breathing

o insensible cannot - evaporation from skin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Osmolality -

A

concentration of solutes in plasma PER KG OF SOLVENT

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Osmolarity

A

concentration of solutes in plasma PER LITRE OF SOLUTION

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Osmotic pressure

CHECK!!!!!

A

how easily solution can take in water vs oncotic pressure: specific type of osmotic pressure concerning albumin
is a form of osmotic pressure induced by proteins, notably albumin, in a blood vessel’s plasma (blood/liquid) that displaces water molecules, thus creating a relative water molecule deficit with water molecules moving back into the circulatory system within the lower pressure venous end of capillaries.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Oedema
increased movement of fluid from plasma to interstitial space, or decrease in vice versa
26
Types of oedema
o normal - increased hydrostatic pressure forces fluid out of vessels o inflammatory - histamine increases blood vessel permeability o lymphatic - lymph system doesn’t remove fluid from extracellular space o hypoalbuminaemic - decreased albumin = decreased oncotic pressure
27
Carbohydrate
o made of monosaccharides - 6 carbon | o glycosidic bonds form between monosaccharaides to produce disaccharides/polysaccharides (condensation reaction)
28
Lipid
o hydrophobic | o triglyceride - glycerol head with 3 fatty acid tails
29
Nucleotide
o Structure: ▪ nitrogenous base ▪ pentose sugar ▪ phosphate group o Phosphodiester bonds form between adjacent nucleotides o Hydrogen bonds form between opposite nucleotides
30
Amino acids
``` o central carbon atom attached to: ▪ amine group ▪ carboxyl group ▪ hydrogen group ▪ variable group o Peptide bonds form between amino acids in condensation reaction ```
31
Protein structure
o primary - specific sequence of amino acids o secondary - alpha helix and beta pleated sheet o tertiary - folding into 3D shape (disulphide bridges, H bonds and polar regions) o quaternary - multiple tertiary proteins working together (haemoglobin)
32
Enzyme
o biological catalyst o protein and non-protein component o induced fit theory o coenzyme = non-protein component
33
Intermolecular forces | Weak to strong
Van der Waals -> permanent dipole -> hydrogen bonds
34
DNA and RNA:
pentose sugar (deoxyribose/ribose), phosphate group and nitrogenous base
35
● Base pairings:
o cytosine to guanine o adenine to thymine - replaced by uracil in RNA o hydrogen bonds between base pairings
36
● Semi-conservative replication
(1 original + 1 new DNA strand): 1. Topoisomerase unwinds DNA from supercoiled state 2. Helicase unzips DNA strand at replication fork 3. DNA polymerase synthesises new DNA – leading strand produced continuously, lagging strand produced in short Okazaki fragments (assisted by DNA primase) 4. New strands are joined up by ligase
37
● Transcription and translation:
1. RNA polymerase and transcription factors bind to promoter region on gene 2. DNA strand unwinds and RNA polymerase moves across active gene, producing strand of mRNA 3. Gene splicing – introns removed, exons reassembled in variable arrangement 4. Mature mRNA travels from nucleus and the 5’ end binds to the ribosome 5. tRNA with specific anticodon binds to corresponding codon on mRNA – amino acid is attached to tRNA 6. Stop codons – UAA, UGA, UAG
38
● Mis-sense:
single nucleotide polymorphism (SNP) = change in single nucleotide = potential change in amino acid
39
● Non-sense:
SNP causes stop codon to be translated = not fully formed amino acid chain = non-functioning protein
40
● Cell cycle:
1. G1 phase – cellular contents are replicated 2. S phase – chromosomes are replicated 3. G2 phase – replication is checked for errors and components are assembled/arranged 4. Mitosis – see below
41
● Mitosis:
1. Interphase: ▪ G1 -> S -> G2 phases (can’t see) 2. Prophase: ▪ chromatin condenses to visible chromosomes ▪ centrioles migrate to poles of cell 3. Prometaphase: ▪ nuclear membrane breaks down ▪ microtubules from centrioles bind to centromeres 4. Metaphase: ▪ chromosomes line up in middle of cell (metaphase plate) 5. Anaphase: ▪ Sister chromatids are pulled apart to opposite ends of cell by microtubules 6. Telophase: ▪ Nuclear membrane reforms ▪ chromosomes decondense to form chromatin 7. Cytokinesis: ▪ cytoplasm divides to form two daughter cells
42
● Meiosis:
1. Interphase – cell contents replicate (2n ->4n) 2. Meiosis 1 – mitosis, but crossing over and independent assortment occurs (4n -> 2n) 3. Meiosis 2 – daughter cells divide to form haploid cells (2n -> n)
43
● Numerical abnormalities:
o during meiosis 1 or 2 chromosomes are not divided up equally o Down’s Syndrome - genetic information missing???
44
● Structural abnormalities:
o chromosomes/parts of chromosomes swap places during meiosis 1 and 2 o different sized chromosomes o less serious than numerical because genetic information still present
45
● Gametogenesis
– meiosis to form gametes
46
● Mendel’s 2nd law
– the hereditary box crossover diagram (dominant and recessive alleles)
47
● Gonadal mosaicism –
epigenetics means that environmental factors (mainly age) causes sperm/egg to have different genetic information to father/mother
48
● Genotype - | ● phenotype
the genetic makeup of an individual | – observable characteristics of an individual (genes and environment working together)
49
● Inheritance:
o Mendelian - purely genes | o Multifactorial - combination of genes and environment
50
● Autosomal dominant
= condition presents in heterozygous state – polycystic kidney disease, Huntington’s disease
51
● Autosomal recessive
= condition only presents in homozygous state – cystic fibrosis, sickle cell anaemia
52
● Sex linked inheritance (X linked inheritance):
o genes carried on maternal X chromosome o transmitted through unaffected females and affects predominantly males o haemophilia, muscular dystrophy RECESSIVE + DOMINANT
53
● Lyonisation:
o one of the maternal X chromosomes are inactivated o in X linked inheritance, the X chromosome with the faulty gene could be active or inactive o random process
54
● Knudson’s two hit hypotheses –
cancer is a result of accumulated mutations to cell DNA, relates to discovery of cancer genes and carcinogenesis
55
● Multifactorial diseases =
combination of genes and environment, risk of condition is higher in people with relatives with condition – schizophrenia, cancer, Alzheimer’s
56
● Penetrance =
percentage of individuals with specific genotype that show expected phenotype
57
● Variable expression
= individuals with same genotype may have differing phenotypes
58
● Anticipation =
genetic defects affect successive generations early and more severely, due to repeat triplet sequences
59
● Metabolism definition
– chemical processes occurring within the body to maintain life
60
● Basal metabolic rate
– rate of energy use in the body for vital functions at rest
61
● Factors affecting BMR:
o Age o Gender o Body size + composition
62
● ATP – ADP cycle:
o ATP + water -> ADP + phosphate + H+ + heat energy o Energetically favourable – negative Gibbs free energy o Phosphate and H+ enter other metabolic pathways
63
● Generation of ATP:
o Glycolysis o Kreb’s cycle o Oxidative phosphorylation
64
● Glycolysis:
1. Glucose -> glucose-6-phosphate ▪ Requires 1 ATP ▪ Catalysed by hexokinase 2. Glucose-6-phosphate -> fructose-6-phosphate 3. Fructose-6-phosphate -> fructose-1,6-bisphosphate ▪ Requires 1 ATP ▪ Catalysed by phosphofructokinase ▪ Inhibited by ATP, activated by AMP 4. Fructose-1,6-bisphosphate -> glyceraldehyde-3-phosphate 5. Glyceraldehyde-3-phosphate -> 1,3-bisphosphoglycerate 6. 1,3-bisphosphoglycerate -> 3-phosphoglycerate ▪ Creates 2 ATP 7. 3-phosphoglycerate -> 2-phosphoglycerate 8. 2-phosphoglycerate -> phosphoenolpyruvate 9. Phosphoenolpyruvate -> pyruvate ▪ Creates 2 ATP
65
● Kreb cycle:
``` o Takes place in mitochondrial matrix o Pyruvate -> acetyl CoA via pyruvate dehydrogenase o Oxaloacetate + acetyl coA -> citrate ▪ Catalysed by citrate synthase o Citrate -> isocitrate ▪ Catalysed by aconitase o Isocitrate -> Alpha-keto glutarate ▪ Catalysed by isocitrate dehydrogenase ▪ Releases NADH and CO2 o Alpha-keto glutarate -> succinyl-coA ▪ Catalysed by alpha-ketoglutarate dehydrogenase ▪ Releases NADH and CO2 o Succinyl coA -> succinate ▪ Catalysed by succinyl coA thiokinase o Succinate -> fumarate -> malate ▪ Catalysed by fumarase and malase ▪ Releases FADH o Malate -> oxaloacetate ▪ Catalysed by malate dehydrogenase ▪ Releases NADH ```
66
● Glycolysis substrate mnemonic:
``` o Good – glucose o Girls – glucose-6-phosphate o Fuck – fructose-6-phosphate o Fine – fructose-1,6-bisphosphate o Gentlemen – glyceraldehyde-3-phosphate o But – 1,3-bisphosphoglycerate o Prohibit – 3-phosphoglycerate o Penile – 2-phosphoglycerate o Pooper – phosphoenolpyruvateu o Penetration – pyruvate ```
67
● Kreb’s cycle mnemonic:
``` o Can – citrate o Adam – aconitate o Intrigue – isocitrate o A – alpha-keto glutarate o Super – succinyl coA o Sexy – succinate o Foxy – fumarate o Momma – malate o Ok! - oxaloacetate ```