-
When was sulfonamide introduced?
1935
-
What was introduce in 1935 ?
sulfanamide, it a antibacterial agent prontosil
-
When was penecilin created ?
1940's by Florey and Chain
-
Who developed the cell theory of immunity
Metchnikoff
-
what did Metchnikoff do ?
created the cell theory of immunity
-
Who developed the concept of the magic bullet ?
Paul Ehrlich
-
Who is Paul Ehrlich ?
He created the magic bullet and He is the forerunern for antitoxins and compound 6060 which is used to treat syphilis
-
If you do a OMM tenet to relieve a problem which tenet is it ?
If right after performing the technique the patient feel better it is structure and function.
-
Where are problem facets
they are only in type II not in type one
-
ERS
- Extension dysfuction. E is equal and the problem facet is on the same side as the dysfunction.
- the problem facet is on the right side
- Ers means that ot wants to extends
- STUCK closed
- ERS right the right facet is stuck closed and does not want to open
-
FRS right
- means that the left facet is stuck open That will cause it rotate and side-bend to the right side
- STUCK OPEN
-
Type I dysfunction
- it is a scoliosis
- like side bend to the rigth and rotated to the left
- you would feel ribs more posterior
-
Type II dysfuction looks like
Hard to see because it is such small sigments
-
What is PFK-1
- rate limiting step
- it is actvated with fructose 2,6-bisphosphate F@^BP
- F2,6BP is a positive regulator
-
Wha does Glucogan do ?
- activates protein kinase-1 which is used to adds a phosphate group
- Glucagin phosphorylates pyruvate kinase and thus inactivates it
-
What is Epidemiology ?
- What determines and distributes health disease in human
- WHO what where when and why of any disease
-
what is a tandem enzyme ?
- Ask michelle or preet
- Fructose-2,6-bisphosphate
-
Communicable diseases
oraganism multiply on or in the body and make the body infection to others directly or indirectly after developing a living vector
-
Examples of communicable diseases invclude
-
Endemic
low and constant level of disease in a population
-
Epidemic
level of infection found above that which is usually found in the population
-
Pandemic disease examples
AIDS, cholera (1980's), ZIKA ( 2016 ) COVID
-
reservoirs
only mammilian carriers od the infectious agent
-
virulence
The # of fatalities over the total cases
-
Incidence
New cases/specific population over a specified time period
-
Prevalence
Total # of cases exiting in a given population
-
Measles
- human to human
- respiratory droplets
- The virus has ss RNA
- very communicable
- MMR vaccination
-
Black Plague
- Pathogen Yersinia pestis
- gram neg
- from rats to fleas to humans
- epidemic of the 1th centrury in Europe
-
Noscomial Epidemics
Hospital acquired infections most commonly inolving opportunitistic organism
-
What is the difference btw a nucleoside and a nucleotide
- A base linked to a sugar
- Side just got the SUGAR
-
Heterochromatin
- The heterosexual is always tight because they never express themselves
- Densely packed chromatin that does not express usually
-
Define the term gene and gene mutation
DNA that has a start and a stop point that specifies a protein
-
How do you do an AP Xray and why is it relevant?
- It is the most accurate
- You have to put the back closest to the image detector.
- That way the X-ray passes from Anterior to posteror hence AP
-
Mutation in which gene lead to Marfan's Syndrome
Fibrin-1 protein mutation would lead to this aliment
-
What do statin drugs do ?
The are competitive inhibitors that compete for thebinding of HMG CoA eductase
-
ERS
- When patient flexes the problem facet is stuck closed
- and the vertebra rotate to the SAME SIDE
- e.g. T4 ERS Right
- this means that the right facet is stuck closed
-
Open ended question Skills
Some Nuns Never really reach Sex
- silence
- Non verbal encouragment
- neutral utterance
- Reflection
- Request
- summarizing \
-
On the Cage questionnaire
- Cut down
- Annoyed by people about you habit
- Guilty about your drinking
- Eye-Opener- do you have a drink first thing in the morning
-
Dna Pol III
- found in prokaryotic cells
- places the RNA primer so DNA can be synthesized from 5' to 3' on a ss dna template
-
DNA Pol I
- Found in Prokaryotic DNA
- mainly to repair DNA.
- it also replaces RNA primer on the lagging strand and replacing them with DNA
-
How is prokaryotic replication different from Eurkayrotic replication ?
- Prokaryotes need:
- DNA gyrase
- circular chromosome not sister chromatids
- it is fast
- large okazaki fragments
- needs DNA polymerase I and II
- single origin of replication
- Dna replicates in the cytoplasm
- circular and double stranded DNA
-
Who is gregor mendel ?
he used the pea plants to understand inheritance
-
Avery MacLoed McCarty
That DNA is what makes up genes
-
Rosaline Franklin
She discovered that DNA is a double stranded helix
-
Collagen
- Fibrous proteins
- linking of GXY which is usually
- Glycine, Proline, and Hydroxyproline or hydroxylysine
-
In euraryotic cells
- DNA alpha
- DNA beta
- and OMEGa
-
Telomerase
- When primer is removed from the end of our DNA there is a gap because we can only add bases in the 5' to 3' directiojn
- expressed in germ cell and live forever because it prevents us from losing information at the end of our genes.
- usually when we replicate information we lose information at the end
-
How to do you make a Collagen fiber
- Repeats of GXY that create a alpha chain
- 3 alpha chains create collagen molecule
- collagen moelcules come together to make collagen fibrils \collagen fibrils come together to make a collagen fiber
-
How do you differentiate RNA and DNA
- This is based on the sugar .
- If the 2' carbon the sugar has an oxygen then it is RNA
- if not it is DNA because it does not have a Oxygen , hence deoxy.
-
How do you correctly name nucleoside when they are attached to the different sugars?
- adenosine
- cytidine
- uridine
- guanosine
- thymidine
-
DNA helicase
unwinds the DNA by breaking the hydrogen bonds that exist between the nitrogenous bases of each DNA strand.
-
DNa Primase
dds a small primer to the existing DNA (since DNA polymerase is unable to start making DNA without a primer first).
-
DNA ligase
seals the gap by building a bond between the phosphate group and the sugar.
-
DNA alpha
- Makes initiator DNA attach to primer
- this cause lagging strand synthese
-
DNA pol. delta
Leading strand synthesis
-
DNA pol. episolon
Lagging strand repair
-
How to detect MI from blood test
- increase in Cardiac Troponin I and T .
- 2-4 hours to release and peaks after a day or two
- CK-MB ( slower indicator)
-
what does Creatine Kinase/Creatine Phosphokinase 1 CK-BB indicate ?
some damage to the brain seeing that it is mostly found in the brain
-
CK2
CK-MB
shows when cardiac muscle is damaged
-
CK3
shows when cardiac muscles and skeletal muscle is damaged.
-
What enzyme is secreted by the level for blood coagulation
-
ALT & AST
- alanine aminotransferase and Aspartate aminotransferase
- elevation in blood could mean liver damage
-
Alkaline Phosphatase
- Could mean cholestatsus
- elevation of this serum enzyme means that bile flow from the liver is blocked or slowed.
Also bones tumor , in the case of Rickets
-
What serum enzyme indicate muscle damage ?
- AST ALT : just like with the liver
- creatine kinase
- Aldolase
-
Pancreas serum enzyme
Amylase in blood indicative of pancrease damage
-
Lacatae dehydrogenase
- made up of 4 subunits
- isofroms separated using chromatography and electrophoresis
- the subunit types are H (heart0 and m(muscle)
-
LDH 2 & 3
- Found in acute leukemia
- H3M
- H2M2
-
LDH 1
- The pure heart LDH 1 HHHH is in the myocardium
- Fasting moving
- Heat Stable
-
LDH 4
HM3 HMMM is in the liver and muscle
-
LDH 5
- M4 MMMM Occur in muscle liver
- anaerobic tissue in liver disease
-
Competitive inhibitor
- Km :increases
- Vmax: stays the same
-
Non-competitive Inhibition
- Decrease in Apparent Vmax
- Does not affect Km
-
-
-
Dna polymerase III
found only in prokaryotes and sythesizes both lagging and leading strand
-
Phosphodiester bond
link nucleotide together in the Dna back bone
-
What are histones
- in eurkaryotic cells.
- proteins that Dna wraps themselves around to organize itself
-
Nucleosome
nucleosome - the unit of histones with Dna wraps about it 2 times
-
GATC
This is the place where metyolation occurs in DNA
-
CpG island
places where there are repeated CG's
-
what is different about the parent and new strand ?
The parent strand is usually methaylated for a time period that the new strand is not
-
Heimethylation
- when the parent dna strand is methylated and the new strand is not
- This is to help with mismatch proofreading
- DAM methylase will know to repaire the new unmethylated strand then metylate at the A
-
Chromatin Remodeling
make sure that the chromatin is accessible for replication
-
DNA gyrase
- only found in Prokaryotes
- quinones such as nalidixic acid and cirpoflocin inhibit DNA gyrase and will kill bacter gram -
-
Osteogensis imperfecta
- Glycine in the amino triple repeat in collagen G-X-Y has point mutation
- results in pooor collagen packing
- Fibril forming collagen type I
-
Stickler Syndrome
- mutation in collagen gene
- Firbril forming and Type I
-
Network forming collagen
- Type II
- Under this is types 4,8,and 10
-
Collagen type II
- fibril associated
- interruption in triple helices
- types 9 and 12
-
How is collagen made
- formed in ER with N-glycosylated residue and 3 alpha helicies twine to form pro collagen
- after N-residue is cleaved procollagen is offical collagen and stacks with other collagen to make collagen fibrils
-
What does lysyl oxidase do?
form covalenbt cross links between collogen to make collagen fibrils
-
why is glycosylation of the hydroxylysine or proline important in collagen
- This is where the cleavage of proalpha chain collagen is made
- if not down it result in faulty collagen or none
-
what is the cofactor of hydroxylases
Vitamin C, Fe2+ and O2
-
EDS
- Ehlers Danlos Syndrome
- defective collagen processing enxyme ( lysl oxidase)
- mutation in fibril forming colloagen
- type I II or V
-
what hold the triple helix of pro alpgha chains together
- cysteines
- that form disulfide interchain
- links h
-
What changes the pyruvate made in glycolysis to acetyl coA?
PDh pyruvate dehydrogenase
-
PDH complex
- an alpha-keto acid dehydrogenase
- Makes a 2 carbon product from a 3 carbon substrate
- There are 3 enzymes in PDH
- - pyruvate dehydrogenase, Dihydrolipoyl transacetykase and Dihydrolipoyl dehydrogenase
-
How is Pyruvate changed to Acetyl coA
- Loses Co2
- Oxidized by lipoic aicd
- Acetyl group is transferred to coA
-
what are the coenzymes of PDH complex
- 1. thamine Vitamin B1 pyrophosphate TPP : E1
- 2. Lipoic Acid E2
- 3. Coenzyme A E3
- 4. FAD E3
- NAD E3
-
Elastin
- nonpolar residues
- hyproxyproline
- dense hydrophobiv globules
- rich in val pro gly
- crossed linked ( desmosine cross-link)
- lysly oxidase helps with cross linking
- when it is relaxed it is compressed
-
what do elastin fiber consists of
Elastin consists of Elastin and Glycoprotein micrfibrils ( Fribin 1, fibrin 2 etc.
-
Marfan syndrome
- Mutationi n Fibrin-1
- elongated limbs and skeltal deformation
- hands and bodies are marfed
-
Where is Elastin found
- in the lungs
- wall of arteries
- elastic ligaments
-
How to remember the two disease spoke about in regards to Elastin
- Elastin is all about me :
- MARFAN and Emphysema
-
Emphysema
- Alpha 1 antitrypsin is a protease inhbitor
- preserve elastin
- stop elastase
- People with Emphysema are deficientin AAT or α1- antitrypsin have their elastin in their lungs destroyed
-
what is M358
- helps protease bind to AAT so that the protease can be =in hibited
- smoking oxidizes this enzyme
-
What division of the PNS is the ANS
The visceral motor divison
-
Somatic sensory Neuron travel to the dorsal ganglia via ?
the peripheal axon proesses
-
How do the somatic sensory get to the spinal cord?
via the central process of the sensory axon
-
what are the names of the 5 plexuses in the body
- cervial C1-C4
- Brachial C5-T1
- Intercostal n T1-T11
- subcostal T12
- Lumbar L1 -L4
- Sacral plexus L5-S3
-
Pyruvate dehydrogenase deficency E1
- Since there is not PDH to crease Acetyl CoA pyruvate becomes lactate and results in lactic acidosis
- it is x-linked w. no treatment
-
arsenic poisoining
- arsenic inhibits enzymes that require lipoic acid suc as PDH, α-ketoblutarate dehydrogenase
- from complex with thio group on lipoic acid
- affect brain
-
Part 1 of TCA
- oxidative decarboxylation to for Co2 and 2 NADH
- from Citrate to α-ketoglutarate
-
PArt 2 of TCA
- oxidative and recreated oxa,oacetate
- creates 1 NADH and 1 FADH2
-
TCA products
Can I Keep selling sec for money, officer?
-
palpation
adding pressure to the surface of the body to determine size, shape, health, consistency, and motility beneath
-
TCA step 1
- acetyl CoA + oxaloacetate =citrate
- through the use of citrate synthase
- it is negative feedback
- succinyl coa
- NADH
-
TCA Step 2
- Aconitase
- what a con first you take out the water then you add it back
- Fe-S protein
- inhibited by fluoroacetate
-
TCA step 3
- Isocitrate dehydrogenase
- oxidative decarboxylation
- RATE LIMITING STEP first NADH
- release CO2
-
what activate the step 3 rate limiting enzyme isocitrate dehydrogenase ?
-
What inhibits isocitrate dehydrogenase?
- ATP
- NADH
- sufficent energyu signals
-
Mnemonic to remeber enzymes of TCA
- Cindy is kinky so she fuck more often
- Citrate
- Cindy And I Know Some Sexy Fucking Mothers!
- Citrate synthase, Aconitase, Isocitrate dehydrogenase , α-ketoglutarate dehydrogenase, succinate thiokinase, Succinate dehydrogenase, Fumarase, and malate dehydrogenase
-
TCA step 4
- oxidative decarboxylation
- 2nd NADH
- 2nd Co2
- the productsuccinykt coA contain a high energu bond
-
what are the coenzymes of alpha-ketoglutarate dehydrogenase
thamine, lipoic acid, CoA, FAD, NAd
-
what inhibits a-ketoglutarate dehydrogenase ?
ATP, GTP, NADH , and succinyl coA
-
what activates a-ketoglutarate dehydrogenase ?
CA2+ from muscle contraction
-
Step 5 TCA
succinate thiokinase
- produces one GTp --> ATP
- from the high ebergy bond of CoA
- substrate level phosphorylation
-
TCa step 6
- makes 1 FADh2
- part of the ETC
-
TCA step 7
- Fumarase
- adde H2o to the doubel bond of the fumarate
- reversible
-
TCA Step 8
- malate dehydrogenase
- produces 3rd and final NADH
-
how many ATP are created from the TCA cycle
- 10
- assuming 1NADH= 2.5 ATP
- 1FADH2=1.5ATP
-
TCa cycle created how many reducing equivalents?
-
After all of the metabolic process how many ATP are made>
36 -38 from 1 molecule of glucose
-
what are the most important enzymatic steps in TCA
-
Layer of palpation
- Skin connective tissue
- muscle and tendon
- Visceral organs
- BOne,ligament,and joints
-
what is the palpate method?
- p- postion of comfort
- a- anatomy= study and visualize
- l- level of tissue
- p- understanding the purpose behind feeling
- a-ascertain movement
- t- tweaking you feeling to see what feels better and what s better
- e-evaluate what has changed
-
cartilage
- 3 types
- Hyaline
- Firbro cartilage
- Elastic Cartilage
-
what kind of cartilage lines synovial joints
hyaline lines the articular surface
-
what are the components a synovial joint ?
- Firbous joint capsule
- synovial membrane 9 produces synovial fluid)
- synovial fluid ( lubrication )
- Hyaline cartilage ( absorbs shock)
-
what are the types of synovial joints?
- 7 types
- pivot
- hinge
- ball and socket
- plane
- Trochoginglymus
- saddle
- condyloid
-
what are the action of the trochoginglymus?
Flex, extend, and rotate the knee
-
what type of synovial joint is in the phalanges ?
- condyloid
- allows for flexion and extexion
- abduction and adduction
- circumduction
-
what type of synovial joint is the caprometacarpal joint ?
- saddle
- allow movement in two different planes
-
pivot synovial joints
Permit rotation like the atlas and the axis
-
contraction
activating muscle fibers that result in tension
-
when muscle create movement it is referred to as ?
isotonic -muscle length changes that create motion
-
what are the types of istonic contractions?
- two types :
- Concentric and Eccentric
-
concentric contraction
- shortening of the muscles
- like to concentrate is to make smaller
- overpowering gravity
-
eccentric
- resisting gravity and controlling motion at a specific rate
- gravity overpower muscle
- elongation of muscle s
-
TCa intermediates are precursors to the biosynthesis pathways
- amino acids
- fatty acids
- Prophyrins
- gluconeogenesis
- bases for nucleotide synthesis
-
anaplerotic reaction
- Pyruvate carboxylase
- replensihes the intermediate of the TCA Cycle
- contain Acetyl coA
-
Pyruvate carboxylase
- other than serving as an anaplerotic
- it contain biotin and requires ATP and Mg2+
-
What does Pyruvate carboxylase catayze ?
the first step of glucneogensis
-
what activates pyruvate carboxylase ?
Acetyl coA
-
anaplerotic reaction
amino acid degradation can create fumarate, oxaloacetate , a-ketoglutarate
-
Leigh syndromes
- PDH deficiency
- PC deficency
-
BeriBeri disease & wernicke-Korsakoff
vitamin B1 deficiency
-
cofactor of PDH
5 coenzymes
- Take Large cock and fuck Nathan
- thamine ( vitamin B1)
- Lipoic Acid
- Coenzyme A
- FAD
- NAD
-
prokaryotes vs Eurkaryotes
- E:
- one promoter
- monocistronic mRNA
- Pro:
- multiple genes controlled by the same promoter (e.g. lactose ; lac operon )
- poly cistronic MRna
-
mRna
becomes the sequence to make proteins
-
how are Rna and Dna related
dna is transcripted to RNA
-
regulatory rNA
they turn rna on and off
-
mature RNa
eventually become the sequence to make proteins
-
RNA
they have secondary and primary structure
-
Rna polymerase
- copies Dna and turns it into RNA
- it does not have any repairing function- this is the reason why they mutate so often
-
RNA polymerase II
most of the protein coding genes
-
Rna Polymerase I
ribosomal RNa
-
RNa polymerase II
transfer Rnas, snrna and small Rna
-
α-amanitin
- comes form the death cap mushroom
- this enzyme binds to RNA pol II
- can stop transcrition and replication in prokaryotes
-
How does transciption start for eukaryotes?
- at the promoter around -25bp
- TATA box
-
How does transciption start for prokaryotes?
at the promter at -35 -10 bp region
-
how Rna polymerase recognizes transcription start region on eurakaryotes ?
- they have transcription factors
- Rna polymerase II ( Eukaryotes ) has 6 different transciption factors
- they all bind with Rna polymerase II
-
how Rna polymerase recognizes transcription start region on prokaryotes ?
- Rna polymerase is made up of 4 different subunits ; the σ subunit recognizes the transcription start site
- sigma falls off of the promoter and then Rna polymerase continues transcritption
-
How is transcription terminationed>
RHo dependent or rho independent
-
Rho dependent
a hair bin loop ( areas of base homo logy ) where rho comes and dissociates the complex
-
Rho independent
- more common
- there is a hair pin loop that is followed by a a series of u's are created and after that there are is AU and they form very weak hydrogen bonds that are not strong enough to hold
- A and U interaction there are only two hydrogen bonds that are not strong enough to hold and destablizes the DNA and teseult sin termination
-
House keeping genes
- are not regulated (e.g. RNa polymerase)
- we need to have it on all the time because we are constantly translating DNA
- always turned on
-
how are gene regulated ?
BY activator and respressors
-
The lac operon is a study of Gene replication how?
- code for proteins that allow cellt o use lactose as energy
- LACZ
- LacY
- and LacA are
-
how to repress lac operon ?
Lac I sit on the promter so that the lactose utilizing enzymes cannot be made and when lactose is present it binds to lac I that removes it from the promoter region
-
how do ecoli cells know to use glucose over other sugars like lactose
- Camp can bind cap and they can bind to sugar operons on the Cap site
- It is necessary for Rna polymerase to bind to the promter
- they untangle the promoter so transcription can take place
-
what does CAP mean
Catabolite activator protein
-
what controls the lac operon globally and locally
Glucose and lactose, respectively.
-
what happens if we mutate the promoter sequence of eukaryotes (TATA)?
it can either weaken or strengthen it reaction with the mutation
-
what are the Post transcritional modifications?
- 5'capping
- 3’-polyadenylation
- Exonal splicing
- Abs to snRNPs very specific to SLE
- Abs to U1 RNP (MCTD)
-
5' capping
a modified guanine residue is added and protect the rna from being degraded in the cell
-
3' polyadenylation
a series of adenines that are added to the 3' end
-
-
prugeria
- a disease that result from the mutation of an exons .
- there is a splice site made in an exon
- results in the removal or distruption of the gene that is used to make a cyotskeltal protein
-
what do spliceosome do?
remove exons from introns an but them together
-
what do antibodies to snRNps do?
help treat mixed contention tissue disease and SLE diseases because it stop snrps
-
sNrps
rna molecules responsible for spliceosomes
-
Translation
- three main components:
- rRNA
- tRna
- mRNA
-
-
What are the ribsome protein for prokaryotes ?
30s and 50s which make 70s
-
when is glucagon high
starving and fasting
-
What are the ribsome protein for eukaryotes ?
30s and 60s to make 80s
-
For transcription how are Prokaryotes different?
- holoenzyme ( 5 subunits)
- no transcriptoon factors
- polycitronis mrna
- promter at -35bp t -10 bp
- no post transitional modification
- coupled transcription and translation
-
how do mRNA's work
- They need a start codon (AUG: methyanine) and a
- stop codon
-
how do we know which AUG is the start codon ?
- before the start codon is the ribosomal binding site and they move and wait for the first aug they encounter and this is the start
- This rna binding site is also called the SHine-Dalgarno sequence
-
ribosome composition
rRNa and protein
-
tRNA
- has 3 loops and attached to it is the amino acid
- on one end there is a section called the anticodon
- on the other section is the amino acid
- carries the anticodon that corresponds to the codon from the mRNA
-
how many codon do we have and what is relevant about them?
There are 64 and they are universal
-
nonsense mutation
creates a immature stop codon
-
how many stop codons are there?
3
-
E P A
- in ribosome that they have 3 site
- exits
- peptid
- accept or site ) where a new TRNA is accepted
-
Ribosomes
- create peptide bond between amino acids
- it has the EPA sites
- move one codon at a time
- there are initiation factors, elongation factor, and releae factors
-
examples of prokaryote antibotics
- targets protein synthesis in prokaryotic
- Aminoglycosides ( bind to 30 s leadin to misread mrna)
- Tetracyclines ( bind 30s)
- Macrolides: bind 50s
- chloramphenicol ( bind 50s)
-
what is a missense mutation
changing one condon to the other
-
What is shown in the bottom image ? what is special about it ?
- pneumoccous
- lancet shapped diplococci
-
what is shown in the image below :
gram negative Legionella or Klebsiella
-
-
what's in the image below:
- gonocossua
- gram neg.
- round shaped
-
- spirochetal bacterium
- Treponema pallidium
-
-
-
histoplasma capsulatum in yeast
-
-
-
- schitosomes
- type of helminths
-
-
- lyme ticks
- Lyme spirochetes (Borrelia )
-
cheif complaint
in the word of the patient and is short and sweet
-
HPI
more structure and detailed with demogrphics
-
what are the OPQRST
- Onset
- palliation/provoking
- Progression
- quality
- radiation
- Severity/Site
- Timing
-
Review of systems
- GU urinary disturances
- GYn vaginal symptoms
- MSK joint and muscle issues
- Neurologicl: dizziness, tremors, headaches, etc
- endocrine
- Pscyh: Depressed/anxious concentration
-
For family history
obtain the age of the pesrons that have disease
-
what are the 5 domains of PARS
- establish rapport
- demonstrate empathy
- instill confidence
- use appropriate verbal communication
- elicit clearly and effectively
-
culture
system of belief shared among memebers of a particular group p
-
what does glucagon activate
- activate PKA
- protein kinase A
- it adds a phosphate group on the target
- the phosphate
-
what is a cofactor
- it is a necessary part of the catalysis of a reaction
- proteins cannot work without their cofactors
-
how to develope consistent cultural humitilty
- ASSES
- Ask Q's
- Seek self awareness
- Suspend judgement
- Express kindness and compassion
- Support safe space
- Start where the patient is
-
uncouplers
- the proton gradient is leaking out
- meaning that you proton gradient gets disrupted
- proton gradient is used by complex 5.
- respiration increase because we are trying to restore our proton gradient
-
malate aspartate shuttle
- oxaloacetate is oxidized to malate via NADH when it get into the mitchodria the maladehydrogenase is reduces to oxaloacteate and the NADH is remade
- in the cell asparate and a-ketoglutarate made from oxaloacetate to get out of the mitochondria
- no energy loss
-
what happens when there is complex 3 inhibitor
- Atp will decrease
- proton gradient decreases
-
if a co factor is an organic molecule?
it can be called a coenzyme
-
how do you remember the difference between transcription and translation ?
- translation happen late in the cycle
- DNa-> RNa->Rna
-
Gene structure
has promoters because they promote transcription
-
Gene mutation
any alteration of DNA (genetic material ); they will have little or no significant effect
-
how are chromosomal mutations different from gene mutatiopns
chromosomal mutations are much larger
-
wild type vs mutant
wild type if the most common
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mutation in germ cell results in
inherent disease
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mutation in somatic cell results in
result in cancer
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What are the 2 types of mutations
Induced and Spontaneous
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name some spontaneous mutations
- erros in DNa polymerase
- base tautomerization
- Ap sites ( ROS)
- deamination
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name some induced mutation
- this is the most common:
- chemical
- radiation
- heat
- - dimerization 9 two thymine residue bond)
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what is a Ap mutation
- lost of a purine or pyridimine
- adenine or guanine or C or t (u)
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Deamination
- remove amino group like going from
- cytosine to a uracil
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Base tautomerization
- different ensomers get switched
- instead of AT it would be AG resulting in shift in
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what are some chemical that can cause induced mutations ?
- alkylating agents
- bromouracil
- acridine orange
- cisplatin
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base substitution mutation
- point ( transitio/ transversion)
- missense/nonsense
- insertions/deletion, frameshift
- inversion, translocation, and duplication
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what is a point mutation
a base subsitutionm mutation
- two type
- transition ( the dna base is changed to the same base)
- transversion ( the dna base is changed to a different one )
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Null/ knock out gene mutation
- the gene no longer can make the protein
- the gene can no longer be transcribed
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Silent gene mutation
mutation does not cause any change in the protein
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Pyrimidine dimers
- pyridimine get bonded by a covalent bond
- lethal because the polymerase can no longer copy the DNA
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Mismatch repair system
- MutSHL system this sis what remove the mismatch
- recognizes himimethylated DNA
- this is to fix and bases that were miss matched
- it happens during G2 of the cell cycle
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what happen when the mutSHLy system is faulty
this will lead to Lynch syndrome which is a type of colorectal cancer ( hereditary)
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Nucleotide excision repair
- happens in G1 stage of cell cycle
- has a more diverse range of
- it is resistant to UV radiation
- pyridimine dimer
-
mutation in the mucleotide repair system will lead to whcih disease
Xeroderma pigmentosum
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uvrABCD
- the proteins that exist in nucletotide excision repair
- they remove 10-12 bases total and dna polymerase fills the gap
- mutation result in Xeroderma pigmentosum ( high susceptible to sun )
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Base excision repair
- happens throughout cell cycle
- repair damaged bases
- ap sites and dss breaks
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homologous recombination
- typically ds breaks
- seen in breast and ovarian tumars
- uses BRCA1/BRCA2 require for this repair.
- use one chromosome to repair the other
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Non homologous end joining
- there is a ds break and no sister chromosome to copy and help to fix the break
- error prone
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Translesional synthesis
- during replication the DNA polymerase skips the error
- polymerase eta
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cell cycle
- G- growth prepare for division
- s dna synthesis
- G2 growth
- M- mitosis
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p53
- tumor supressor gene
- control G1 to S phase
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CDK
check point in the cell cycle to make sure that errors are addressed and are not replicated
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when do oocytes get suspended and start again
they stop mitoses at prophase I at birth and Meiosis II does not happen until fertilization
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what important even happens in Prophase I
- chiasmata formation and crossing over
- that way that genes can be recombinated and give rise to alot of diversity
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what is chromosomal non dis junction
- when chromsomes do not split properly leading to mutation
- in sex cells this can lead to downs syndrome
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cultural competemility
cultural competency + cultural humility
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cultural awareness
self examination and recognition of biases / paradoigm
-
cultural competency
impacts care though service delivery ; respectful and responsive to health belief practices and cultural needs
-
cultures affect with health
- health care seeking behavior
- perceived causes of illness
- understand of disease process
- treatment decisions
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[perceive benefits
pt's opinion of desirable behavioral helath beliefs that need to be thought out
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what are the steps of the cultural proficiency continuum
- cultural:
- destructiveness
- Incapability
- Blindness
- precompetnece
- competence
- proficiency
-
philoshy
inquiry into the nature of things
-
precept
general instruction for action
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corollary principles of OMM
- disease= when self maintence is overcome
- movement is fluids is essential
- nervous system is essential in controlling the body
- somatic component are present and contribute to diseased state
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