Cell Basics Flashcards

1
Q

Describe the properties of protoplasm and the tenets of the cell doctrine.

A

cell doctrine - all living organisms are made from cells and they are the basic/structural units of all organisms.

protoplasm - the cytoplasm in eukaryotes, contains ions, proteins, and nucleic acids.

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2
Q

Describe the relationship between cells, tissues, organs and systems of the body.

A

cells - basic unit of living organism

simple tissue - a collection of similar cells

compund tissue - a mix of cells and extracellular matrix

organ - a distinct group of several tissues

system - a group of organs with a distinct role

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3
Q

List the four basic tissue types.

A

epithelia: sheets of closely-packed cells derived from one of the 3 germ layers (ectoderm, mesoderm, endoderm) and which cover or line a surface of an organ.

connective tissues - cells derived from mesoderm and produce extracellular matrix of fibers and ground substance

muscular tissues: derived from mesoderm and composed of cells (or multinucleated syncytia) whose cytoplasm contains filaments made of contractile proteins (actin, myosin, etc)

Nervous tissues: develop from neurectoderm and consist of cells of which the main type possesses processes called neurites (axons and dendrites) which conduct impulses when stimulated

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4
Q

List the main membrane bounded organelles of the cell and state their functions.

A

mitochondria - responsible for respirationa and ATP production

nucleus - contains DNA which controls protein synthesis

endoplasmic reticulum - RER has ribosomes which are used for protein synthesis, SER is used for lipid synthesis

golgi - packs and sorts proteins from the ER

lysosome - membrane bound and contains digestive enzymes

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5
Q

Describe how the cell is divided into compartments.

A

the cell is divided into compartments via compartmentalisation. this is done via the phospholipid bilayer creating unique environments with specific conditions for organelles.

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6
Q

Discuss the process of secretion.

A

the secretion of materials from the cell is known as exocytosis, and it expels secretory vesicles which are produced by secretory cells. the secretory vesicle moves towards the cell surface membrane, and then fuses with it. the contents are then released. it is an active process.

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7
Q

Discuss the process of uptake of material by cells.

A

the uptake of materials in endocytosis. material from outside of the cell fuses with the cell surface membrane. the membrane then pinches off to form a vesicle which then travels inside of the cell. it is also an active process.

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8
Q

Be aware of the aims and purpose of personal and professional development.

A

to give the necessary knowledge, skills and
attitudes to enable you to assess patients and interact with colleagues in a professional manner at a level appropriate to your training and to stimulate and maintain enthusiasm for clinical medicine
early in the course

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9
Q

Understand how early clinical and professional development is assessed.

A

information governance training, mfqs, gp tutor sign off

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10
Q

Explain briefly how a microscope works.

A

a light microcope works by shinign light through a sample so that it can be seen in a microscope. the sample must be extremely thin for this to work.

a transmission electron microscope works by passing a beam of electrons through a specimen to produce an image

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11
Q

Describe how tissues are prepared for examination in the light microscope and become familiar with the appearance of the commonly used stains

A

in order to cut a thin section of a sample, it must first be impregnated with wax. the water in the cell is removed and replaced with something miscible between alcohol and wax. xylene is used to dewax.

the tissue is floated out in water bath to reverse compression. the tissue is transparent so stains are used. most common is haematoxylin and eosin. H stains acid components blue, E stains basic components pink

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12
Q

Give examples of other methods of tissue preparation e.g. cryostat sections, use of the electron microscope

A

a smaple can be freezed, and then dewaxing is not needed. tissue is mounted in OCT and sectioned with a cryostat.

preparation of a sample to use in a TEM is the same except different chemicals are used and a copper grid replaces the glass slide.

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13
Q

Consider the ways to interpret a 2D section of a 3D structure (plane of section)

A

sections of a sample will not always be cut perpendicularly, so care has to be taken when viewing slides and interpreting the 2D section of the structure

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14
Q

Understand the role and importance of epidemiology in medicine and public health

A

epidemiology is important as it shows the distribution of disease in a population. this allows chnages to be made to healthcare capactity

in medicine it allows doctors to consider how to prevent and treat disease, make sure best treatment is used, to work out amount of illness

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15
Q

Be able to explain what is meant by evidence-based medicine

A

using the best knowledge and treatments available for a patient. the volume of evidence can be unmanagable, statistically significant benefits may be marginal clinically

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16
Q

Understand the role of public health in improving health and preventing disease

A

public health is to reduce inequality and protecting and imporving population wellbeing. understanding health trends can help to understand the most effective way of preventing disease. improvement can be done through education, addressing soci-economic factors and through population interventions.

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17
Q

Explain the hierarchy of protein structure.

A

primary - the order of amino acids

secondary - chain of amino acids organised into alpha helix and beta pleats

teritary - the 3D packing of secondary structure elements

quaternary - number and position of polypeptide subunits.

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18
Q

Explain what is meant by the primary structure of proteins.

A

the primary structure is the sequence of the amino acids

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19
Q

Describe the nature of the peptide bond.

A

the bond is a resonance hybrid, and there is a delocalisation of electrons across the whole bond. it has a double bond character. a molecule of water is released when it is formed.

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20
Q

Explain what is meant by secondary and tertiary structure of proteins.

A

the alpha helix and beta pleat maximise hydrogen bonding and minimise steric repulsion. it is the localised organisation of the polypeptide backbone. beta side chains point alternatively up and down. they can be arranged in parallel and antiparallel strands.

polypeptides greater than 200 amino acids often have multiple teritary domains. the tertiary structure is a protein’s exact 3D structure.

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21
Q

Have a basic grasp of the relationship between genes and their expressed protein products.

A

genes determine the sequence of amino acids, which then determine the protein that is made.

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22
Q

Describe the key features of the basic building components of nucleic acids i.e. bases, sugar(s) and phosphate.

A

the bases are adenine, guanine (purines), cytosine, thymine and uracil (pyrimidines). the sugars are beta D deoxyribose and beta D ribose. the phosphate groups contain inorganic phosphate.

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23
Q

Understand and be able to explain the nature of a phosphodiester bond.

A

the phosphodiester bond is polar and asymmetric. it is the linkage between 3’ carbon and 5’ carbon.

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24
Q

Highlight the differences between DNA and RNA.

A

DNA contains deoxyribose whereas RNA contains only ribose. RNA contains uracil, not thymine. RNA is a single strand.

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25
Q

Describe what is meant when a nucleic acid is described as having polarity and explain why this is the case.

A

All the phosphodiester linkages in DNA and RNA strands have the same orientation along the chain, giving each linear nucleic acid strand a specific polarity and distinct 5’ and 3’ ends.

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26
Q

Give a brief overview of the DNA double-helix structure and how it is stabilised.

A

the DNA helix is two polynucleotide chains coiled around an axis. the chains are antiparallel and run 5’ to 3’ in oppositie directions. the bases are inside and the phophate is on the outside. hydrogen bonding between pairs and hydrophobic stacking forces.

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27
Q

Describe the Watson-Crick base-pairs.

A

A + T form a pair using two hydrogen bonds, C + G form a pair with 3 hydrogen bonds. T is replaced by U.

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28
Q

Understand what is meant by ‘genetic code’ and the relationship between genotype and phenotype.

A

genetic code - 3 nucleotides in a row (triplet) code for an amino acid.

genotype - individual’s collection of genes

phenotype - expression of geneotype, an organism’s observable characteristics.

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29
Q

Describe the initial competing models of DNA replication and which is, in fact, correct.

A

conservative replication - all of parental DNA conserved in one daughter molecule

semi-conservative replication - half of parental DNA conserved in each daughter molecule (correct)

30
Q

Briefly describe the process of DNA replication, including key features.

A
  • each strand is a template for the synthesis of new strand.
  • helicase unravels strand, HDP stops strands joining back together.
  • free nucleotides line up with complementary base pairs
  • okazaki fragments formed on lagging strand.
  • DNA polymerase closes the gap between fragments and DNA ligase joins them together.
31
Q

Name a drug that functions through the targeting of the DNA replication process.

A

Eukaryotic DNA replication requires topoisomerase enzymes, toposide is a topoisomerase II inhibitor and can be used as an anti cancer chemotherapeutic.

32
Q

List the typical RNA species in eukaryotic cells.

Describe the features of a eukaryotic mRNA and their functions, where appropriate.

A
- mRNA: 5’ cap
5’ UTR
Ribosome Binding Site (RBS) or Kozak sequence
Start/initiation codon
Coding sequence/open reading frame (ORF)
Termination/stop codon
3’ UTR
poly(A) addition consensus signal
poly(A) tail 
  • hnRNA
  • tRNA
  • rRNA
  • 7S RNA
  • snRNA
33
Q

Distinguish DNA, histones, chromatin coils and condensation and their contributions to chromosome structure and function.

A

DNA - two coiled polynucleotide chains

chromatin - made of DNA and protein. major proteins are histones. packs DNA into compact and dense structures.

histones - nuclear DNA is condensed and wrapped around histones in order to fit inside of the nucleus and take part in the formation of chromosomes.

34
Q

Understand the different types of cell population according to their rates of turnover.

A

continuously renewing - epidermis of skin, intestinal epithelium, blood-forming tissues

conditionally renewing - liver, kidney, endocrine glands

static or non-proliferative - cardiac, nerve cells

35
Q

Understand the phases in the life cycle of a cell.

A

the cell cycle is interphase, prophase, metaphase, anaphase, telophase and cytokenesis.

G1 - this is the growth phase.

S - DNA, RNA and protein replication occurs. There are multiple DNA sites known as replicons.

G2 - protein synthesis is taking place.

G0 - the cell leaves the cell cycle and does its differentiated function.

36
Q

Explain the stages of mitosis and the main events that occur.

A

Prophase - chromosomes formed, centrioles duplicate, act as microtubule organising centres (MTOCs). Microtubules form mitotic spindle apparatus

Prometaphase - nuclear membranes disassemble, chromosomes interact with microtubules. sister chromatids has an attachment site called the kinetochore and attaches to the spindle.

Metaphase - metaphase plate formed, and the chromosome arranged as two sister chromatids attached to centromeres, latter microtubules run to centromeres of sister chromatids and attach at the kinetochores.

Anaphase - the sister chromatids of each pair move apart to opposite poles of the cell, chromosomes are pulled along by microtubules.

Telophase - the chromosomes reach the pole and become less condensed, the nuclear membrane reassembles, cleavage furrow forms at the equator, the spindle disappears, and the nucleoli reappears.

37
Q

Explain how the cell cycle is regulated and why this is clinically important.

A

cyclins and cyclin dependant kinases regulate the cell cycle. they are proteins that coordinate the cells entry into the next phase of the cell cycle.

CDKs are activated when binding with cyclin, they then cause phosphorylation to acitvate/inactivate proteins.

inhibitors of these could stop the cell cycle and be used as tumour suppressors

38
Q

Describe the main events in meiosis and appreciate their significance in oogenesis, spermatogenesis and genetic variation. Be aware of the main chromosomal numerical abnormalities.

A

Prophase 1:

  • leptotene: chromatin condenses to form chromosomes, not split into sister chromatids. The chronometers are visible, DNA thread is locally coiled.
  • zygotene: homologous chromosomes pair to form bivalent tissue. Chromosomes split into sister chromatids. synapsids which develop between sister chromatids of homologous pairs.
  • pachytene: the synapsids complete, crossing over occurs via formation of chiasma.
  • diplotene: the chromatids held together by chiamata and centromeres. female foetus has 300-400 oocytes which go through the first stages of meiosis. Primary oocytes remain in the diplotene stage until the menstrual cycle.
  • diakinesis, the chiasmata appear to move towards the end of chromatids, this is known as terminalisation.
  • metaphase 1: genetic variation occurs as each bivalent to has two centromeres and they arrange themselves by chance.
  • anaphase 1: chromosomes move to opposite ends of the cell, each pole is a mixture of maternal and paternal chromosomes.
  • telophase 1: The nuclear membrane may be formed. In most female animals, asymmetrical meiosis has occurred, with one set of chromosomes moving to a small amount of cytoplasm to form secondary oocytes.
39
Q

Describe how cells respond to alterations in their environment

A

cells respond to alterations in the environment by adapting in order to maintain homeostasis. this is a reversible process.

40
Q

Explain the terms hypertrophy, atrophy, hyperplasia, involution and metaplasia

A

hypertropy - the size of cells increase

hyperplasia - the number of cells increase

atrophy - a decrease in the size of cells

involution - reduction in the number of functioning cells

metaplasia - a change in the type of cell

41
Q

Describe the mechanisms of cellular injury.

A

failure of ATP production, energy dependent processes fail, cell membrane more permeable to sodium so water moves in. lysosomal enzymes released and organelles destroyed, cell membrane fails and substances leak out. this leads to inflammation

42
Q

Outline the 2 main processes of cell death: Necrosis and apoptosis

A

Necrosis: Severe damage to cell membranes, enzymes leak from lysosomes into cytoplasm and digest the cell. Cellular contents leak out of the cell eliciting a local reaction. Pathologic

Apoptosis: cells kill themselves as a result of lack of growth hormones or damage to DNA/proteins. Active, energy dependant, regulated.

43
Q

Describe the terms ischaemia and infarction

A

ischaemia - the lack of an oxygen supply to a tissue or organ. can be reversible depending on different factors

infarction - necrosis of tissue as a result of ischaemia

44
Q

Explain quaternary structure.

A

polypeptide subunits associate with a specific geometry.

45
Q

Recognise haemoglobin as an example of quaternary structure and cooperativity.

A

haemoglobin has 4 globin subunits, 2 alpha and 2 beta. one haem group per subunit binds to oxygen.

cooperativity means that once one oxygen binds, it makes it easier for the rest to bind.

46
Q

Recognise some common protein types (globular, fibrous, membrane).

A

globular - spherical proteins that are water soluble, ie haemoglobin, regular secondary structure interspaced with stretches devoid of recognisable structure

fibrous - elongated shape, provide support for cells and tissues, ie alpha keratin (alpha helix colied) and collagen

membrane - receptor proteins relay signals between the cell’s internal and external environments. Transport proteins move molecules and ions across the membrane.

47
Q

Explain the role of some chemical modifications of proteins.

A

post transcription modifications can help to regulate protein activity and destination.

glycosylation (the attachment of carbohydrates), extracellular and cell surface to prevent digestion, aids folding of protein, can be N linked or O linked

48
Q

Recognise the role of mutations leading to altered proteins in some diseases.

A

protein function depends on its 3D structure, and a mutation can lead to a misfolding of protein, which will cause disease

49
Q

Explain how communication is central to effective medical care

A

clear communication means a patient will better understand what you’re saying, and you will also be able to take a better history.

50
Q

Describe the theme structure and goals for your communication skills for year 1

A

understand what good communication skills are and improve them with practice

51
Q

Explain the Calgary Cambridge Framework

A

initiate session, gather info, physical exam, explanation and planning, closing session

52
Q

Describe basic aspects of verbal and non-verbal communication.

A

verbal - structure the session, signpost what you’re saying/doing, open to closed model

non-verbal - conveys emotional info, body language, the way you speak, tone, pitch, speed, posture, touch, and eye contact.

53
Q

Describe techniques used in order to elicit the patient’s perspective during consultation.

A

ice framework - ideas, concerns and expectations

open questions, probing questions and then closed questions.

54
Q

Explain the importance of the contribution of the behavioural sciences to the medical curriculum.

A

behavioural sciences help us understand why patients and doctors behave in the ways they do. helps us to understand factors than influence decisions to seek help

55
Q

Identify factors influencing the patient’s decision to consult a doctor.

A

socialisation, gender, age, education, financial situation, ethnic group, severity of symptoms, convinience of appointment, previous experience with GP/doctor

56
Q

Describe the difference between observational and interventional studies.

A

observational - investigator passivley observes, used to find risk factors and outcomes

interventional - investigator manipulatrs participants, used to see if certain treatments work

57
Q

Understand the concept of the hierarchy of evidence

A

some evidence is better than others: systematic reviews and meta-analysis are the best, ecological studies are the worst.

58
Q

Understand the concepts of hypothesis testing, probability and statistical significance

A

hypothesis testing is used to see if there are associations between risk factors and disease.

probability is the chance of something happening, 0 means nulls hypothesis is definitely not true.

statisitical significance - p<0.05, statistically significant evidence against null hypothesis

59
Q

Differentiate between association and causation.

A

association - can be true with no cause and effect relationship, can be reult of chance, bias, confounding, reverse causality or simultaniety

causation - one variable makes the other happen, cause and effect relationship

60
Q

List Bradford Hill’s criteria for assessing causation.

A
  1. Strength of association
  2. Consistency
  3. Specificity
  4. Temporality
  5. Dose
  6. Plausibility
  7. Coherence
  8. Reversibility (experiment)
61
Q

Explain the importance of water and pH in biological systems.

A

water makes up 60% of the body, it is a solvent, forms hydrogen bonds which are weak but give water its properties. it dissociates to form hydroxyl and hydronium ions.

pH is the concentration of hydrogen ions in a solution. cellular reactions are pH sensitive, phosphate and carbonic acid are important intracellular buffers.

62
Q

Describe the scope of biochemistry.

A

biochemistry is the study of chemical processe within and relating to living things.

63
Q

Identify the macromolecules that biochemists study.

A

proteins, nucleic acids, complex carbohydrates, polymers of micromolecules

64
Q

Recognise that all proteins are composed of just 20 different units.

A

proteins are polymers of amino acids that come from diet or are made in the body, the sequence of amino acids determines a protein’s structure and function.

65
Q

Recognise that different amino acids have different chemical characteristics.

A

amino acids have different properties due to their unique side chains. R determines protein size, polarity and reactivity

66
Q

List the disciplines of clinical laboratory sciences.

Outline the functions of the different disciplines in clinical laboratory sciences.

A

diagnostic pathology - structural examination

diagnostic microbiology - characterisation of infective agents

diagnostic immunology - looking at immune response to disease

diagnostic genetics - genetic casues of disease

67
Q

Define the terms natural history and prognosis.

A

natural history - The course a disease takes in an individual. What will happen if treated/untreated: prognosis of disability, disease free survival and survival at a cost.

prognosis - the likely course of a medical condition

68
Q

Outline the main causes of disease and describe one example of each.

A

Aetiology: Finding the root cause of disease.

Congenital Defects: These are defects present at the time of birth, fetal development or birth process. It may be genetic or sporadic.

Genetic Defects: The onset of these defects can occur at any age, and there are a variety of genetic mechanisms.

Metabolic Defects: Can have genetic basis or be acquired by the environment.

Inflammatory Defects: These are usually conditions that end in ‘itis’. Indicates secondary tissue damage.

Neoplastic Defects: Involve tumours, which can be carcinomas or benign.

Environmental Defects: This can be caused by physical changes, chemical changes or radiation exposure.

Immune Defects: These can lead to allergies, immune deficiency, autoimmune conditions.

Infective Defects: These are viruses, bacterias, parasites and fungi.Vascular Defects: Examples of this are heart disease and atheroma (an abnormal accumulation of material in the inner layer of the wall of an artery).

Degenerative Defects: seen in different organ systems, wear and tear, aging, disease of the brain

Iatrogenic Defects: These are the result of medical interventions. Some patients develop autoimmune diseases after using a drug, or having surgery.

69
Q

Discuss the concepts of normal.

A

Normal is considered what is seen in 95% of individuals. can vary with a range of factors.

70
Q

Describe the difference between cell adaptation to physiological and pathological stimuli.

A

physiological stiumli can be hypotrophy in response to exercise, or hyperplasia during puberty. the response to pathological stimuli is usually necrosis.

71
Q

Outline the function of cell stress proteins.

A

Ubiquitin links to damaged proteins and flags them for elimination, the complex is then sent to the proteome system for the degradation of the protein

72
Q

Define the term agenesis.

A

the failure of an organ to develop during embryonic growth and development