the cell (b1- foundation) Flashcards
(56 cards)
cell is defined as… + what do all cells contain
the basic structural and functional unit of of life
- can live as its own or in another organism
all cells contain:
- surrounded by a plasma membrane
- have cytosol, containing the organelles
- contain chromosomes/genetic material
- have ribosomes
3 major differences between prokaryotic and eukaryotic cells
1. Size:
-prokaryotes: are smaller (typically 0.1-1.0 micron)
- eukaryotes: are much bigger (typically 10-100 microns in diameter)
2. Genetic Material:
- prokaryotes: genetic material is concentrated in the nucleoid
- eukaryotic cells: genetic material is in chromosomes in the nucleus
3. Cytoplasm:
- prokaryotes: all the material within the plasma membrane is cytoplasm
- eukaryotes: cytoplasm contained many membrane-bound organelles of specialized form and function
what is cytology?
study of cells, focusing on their structure and function
- uses process called subcellular fractionation to separate the cell components
- then, biomarker enzymes are used to identify each of the separated organelles
subcellular fractionation: first step and what the 3 processes used are
subcellular fractionation: process used to separate the cell components, involves 2 steps:
1. Tissue/cell homogenization: tissue is crushed by different methods and a homogenate is produce a homogenate
a. sonication: uses high-energy sound waves to rupture cell walls and membranes, releasing their contents. is effective for cell disruption and * highly suitable for protein extraction*.
b. chemical lysis: uses
- surfactants (dissolution of lipids)
- alkali (saponification- breaking down fats and oils into soap and alcohol- ex. NaOH)
- organic solvents: penetrate lipids and cause swelling of the cells (ex. toluene)
c. enzymatic lysis: enzymes are used to break down the cell. advantage is the specificity.
- enzymes used include: lysozyme, zymolase, cellulase, protease, glycanase (dont need to know all but maybe 1-2)
what are microsomal fractions
fragments of the endoplasmic reticulum that are obtained through centrifugation
(ER too fat to come out by itself so it comes out in bits and pieces)
subcellular fractionation: 2nd step and the steps used
2. centrifugation: used to separate the organelles based on different size, shape, and density. types of centrifugation:
a. differential centrifugation: means different times & speeds, so each step has a different time and speed (diff organelles come out at each)
order of organelles (1st to last): nuclei → mitochondria, chloroplasts, lysosomes, peroxisomes → plasma membrane, microsomal fragments, large ribosomes → small ribosomes → cytosol
b. density gradient centrifugation: all one big step and each of the organelle goes and settles at its density
- uses specific test tubes that have a pour at the bottom
what are the biomarker enzymes for the following structures:
- nucleus
- mitochondria
- lysosomes
- Golgi apparatus
- microsomes
- cytoplasm
- nucleus → DNA (microsatellite markers), RNA
- mitochondria → inner membrane: ATP synthase
- lysosomes → cathepsin
- Golgi apparatus → galactosyl transferase
- microsomes → glucose-6-phosphate
- cytoplasm → lactate dehydrogenase
structure of a nucleus
nuclear envelope: protective shell around the nucleus (made of 2 layers- inner and outer membrane), keeps DNA safe inside while separating it from the rest of the cell
nuclear pores (nucleoporins): tiny holes in the nuclear envelope, act like gates allowing important molecules (RNA and proteins) to move in and out of cell while keeping harmful substances out
nuclear lamina (jali like region): line inner part of the nuclear envelope, providing support and helps maintain shape of the nucleus
nucleolus: dense, round structure inside the nucleus, site where ribosomes are made
nucleoplasm: gel-like substance inside nucleus that surrounds the DNA and nucleolus (contains enzymes, proteins, and other molecules needed for the nucleus to function)
think nuclear EPL
karyopherins
special proteins that act like “transport workers” for the nucleus
- help move important molecules (like proteins and RNA) in and out of the nucleus through the nuclear pores
2 types: importins (carry into the cell) and exportins (carry out of the nucleus)
chromatin + 2 types + where is it located
chromatin are inside of the nucleus
functions of chromatin: primary protein components of chromatin are histones that compact the DNA and make nucleosomes, they prevent DNA damage, and control DNA replication and gene expression
2 types: euchromatin (loose & active - genes are on) & heterochromatin (tight & inactive- genes are off)
- euchromatin is less dense than heterochromatin and also looks lighter under a microscope
nucleosome
section of DNA that is wrapped around a core of proteins
(histone + DNA)
when chromatin is extended and viewed under a microscope, structure resembles beads on a string
biomedical importance of the nucleus
- controls hereditary characteristics of an organism & stores hereditary material in the form of DNA
- responsible for cell division, growth, and differentiation
- produces ribosomes (protein factories)
- site for transcription (mRNA are produced for protein synthesis*
- involved in DNA repair
why are there RBC’s the only type of cells without mitochondria? viva question
because their main job is to transport oxygen, and mitochondria would actually compete for that oxygen
- since mitochondria need oxygen to produce ATP so would take some of the oxygen
- also more space for hemoglobin and easier to squeeze through areas without organelles
- instead, rely on glycolysis with does not require oxygen, allowing them to function effectively (since all they need energy for is to maintain their membrane)
3 structures of a mitochondria
outer membrane: outermost layer of mitochondria, acts as protective barrier (allows free transportation of molecules), contains porins (special proteins that control what enters and exits)
inner mitochondrial membrane: site for electron transport chain (!!!), folded into structures called cristae (increase surface area for energy production)
- has protein complexes (I-V) that make up ETC to produce ATP (says you dont need to know names of each one yet)
matrix: inner fluid-filled space, contains enzymes, mitochondrial DNA, and ribosomes needed to make some of its proteins
- where the Krebs cycle (citric acid cycle) happens
- site for beta-oxidation of fatty acids
- ketone bodies production
- first 2 steps of the urea cycle
(memorize like 3-4 things from this list- matrix one)
mitochondrial cytochrome P450 system
group of enzymes in different mitochondria cells that help modify molecules using oxygen, work different in different organs
steroid hormone production (placenta, adrenal cortex, ovaries, testes): hydroxylates cholesterol (adds an -OH group) to convert it into steroid hormones (like cortisol, aldosterone, estrogen, and testosterone)
bile acid synthesis (liver): helps convert cholesterol into bile acids, which are needed to digest and absorb fats
vitamin D formation (kidney): activates vitamin D by hydroxylating it, allowing body to use it for calcium absorption and bone health
mitochondria DNA
is maternally inherited
- mutation rate is higher compared to nuclear DNA
- evolved from circular genome of bacteria that were engulfed by the early ancestor’s of today’s eukaryotic cell (she said this was wrong maybe though)
how mtDNA (mitochondrial DNA) contributes to the ETC (electron transport chain)
mitochondrial DNA contains 13 genes that make proteins for the ETC
breakdown:
7 genes make protein for → complex I
1 gene → complex III
3 genes → complex IV
2 genes → complex v (ATP synthase)
means mitochondria partially control their own energy production by making key proteins needed for the ETC
list some mitochondrial diseases
- fatal infantile mitochondrial myopathy and renal dysfunction (weak muscles, difficulty breathing, kidney problems)
- myoclonic epilepsy (seizures, nerve cells dont use energy right)
- ragged red fiber disease (muscle fibers appear “ragged” and red under microscope = muscle weakness)
- Alzheimer’s disease (nerve cell damage, memory loss and cognitive decline)
- diabetes mellitus (mitochondrial dysfunction in pancreatic cells, body has trouble using insulin)
functions of the rough endoplasmic reticulum
- covered with ribosomes giving it that “rough” appearance
- key role in processing proteins to send to right destination which will either be a) secreted, b) inserted into cell membrane, or c) sent to organelles like lysosomes
protein modification: newly made proteins are folded and processed before being sent to final destination
3 types of protein modifications:
- chaperone proteins help in protein folding
trimming by proteases: some proteins need some parts cut off before fully functional
- proteases are enzymes that cut unnecessary sections
protein glycosylation: RER adds carbohydrate (sugar) chains to proteins to help them function properly, stay stable, and reach the right location
glycation vs glycosylation
both are when sugars are attached to proteins BUT glycation can happen without enzymes whereas glycosylation needs proteins to happen
5 functions of smooth endoplasmic reticulum (SER) + microsomal cytochrome P450 monooxygenase system
think lipids are smooth
- has different functions depending on the type of cell it is in
1. Lipid Production (in intestinal epithelium): makes phospholipids, glycolipids, and cholesterol
2. Glycogen Breakdown (in liver and muscle cells): helps break down glycogen (a stored form of sugar) into glucose when the body needs energy
3. Steroid Hormone Synthesis (in adrenal gland cells): produces steroid hormones, like cortisol and sex hormones (like estrogen and testosterone).
4. Calcium Storage and Release (in muscle cells): stores calcium ions and releases them when needed, which is crucial for muscle contraction.
5. Detoxification (in liver cells): helps neutralize toxins from the body, including drugs and harmful substances
- uses cytochrome p450 enzyme system (plays key role in breaking down chemicals)
Golgi apparatus structure
- separated from nucleus by RER
- surface towards RER is called cis-golgi (“receiving” end of the Golgi apparatus- proteins from RER are sent here inside vesicles) screened and decided whether to keep or send back
- surface of last cistern of Golgi apparatus that is facing away from RER is called trans-golgi (is the “shipping” side of the Golgi apparatus- packs proteins into vesicles to send to target locations)
flow of proteins: RER → Vesicles → Cis-Golgi → Golgi Modification → Trans-Golgi → Final Destination
main function + 2 types of modifications done by the Golgi apparatus
main function: modify, sort, & package proteins
- receives vesicles from RER w/ newly synthesized proteins, screened by cis-golgi (if not good then sent back to RER), rest of proteins are passed onto network
types of modifications:
1. Glycosylation: attaches carbs (sugars) to proteins or lipids to help with cell recognition, signaling, and stability
- 2 types: N-Glycosylation (sugars added to -NH2 group (amide), mostly in membrane proteins and secreted proteins like antibodies) and O-Glycosylation (sugars are added to -OH (hydroxyl) group, mainly in mucus proteins)
2. Phosphorylation: adds phosphate groups to activate, deactivate, or direct them to right location
3 destinations of proteins after being packaged by the Golgi apparatus
- lysosomes
- secreted out of cell
- become part of the cell (cell membrane)