Physiology-Endterm Flashcards
Function of cellular junctions
- Mechanical stability
- Sepration of membrane domains
- Signal conduction between cells
- Maintaining integrity during contraction
- Binding growth factors together (ex: neurons growth core guidance)
- Help in cell migration, wound healing, phagocytosis
Tight junction (occluding junctions)
Separates 2 things in epithelial cells
- Different compartments of fluids from each other
- Apical and basolateral surface
Tight junctions are located below the apical surface
Makes sure nothing unregulated enters or exits the cell
Tight junction proteins
Claudius and occludens
Each claudin connects to another claudin and the same for occludens
Claudin
Major part of the tight junctions
Occludens
Don’t know the function of it
Tight junctions and role in glucose transport
Need to bring glucose from the lumen to the blood. So have glucose transporters that are secondary active transporters that bring glucose from the lumen to the cell. Have glucose carriers that work by facilitated diffusion to bring glucose to the blood. Have high glucose in cell and low in lumen.
Tight junctions make sure that the glucose transporters and the glucose carriers stay in their respective side
Heregulin
Secreted by epithelial cells. Helps stimulate cell repair during injury. Heregulin is located in the apical surface while while it’s receptors are located in the basolateral surface.
Tight junctions and heregulin
Tight junctions make sure that heregulin and its receptors stay on their respective side during normal times.
When the cell is injured, tight junctions will disappear allowing heregulin to bind to its receptor and heal the cell. This is an autocrine process
Desmosomes
Maintains the integrity of the cell. Found in places that are exposed to mechanical stress. Is an adhering junction.
Has an attachment plaque
Attachment plaque
Make of desmoplakin, plakoglobins, and plakophikin. Plakophikin connected desmoplakin and plakoglobins together.
The attachment plaque is connected to keratin which then connects it to the cytoskeleton
Extracellular side of desmosomes
Connected by adhering proteins such as cadherins to connect attachment plaques to each other
If no desmosomes…
Cells are transformed to metastatic cancer cells that can move around freely
Anchoring junction
Anchor between
- Other cells
- Basolateral surface to the basal lamina
Has intracellular attachment proteins and transmembrane adhesion proteins
Transmembrane adhesion proteins
The proteins that connect to the surfaces
Intracellular attachment proteins
Binds to the transmembrane adhesion proteins
Gap junctions
Channels that allow ions and small molecules to pass through. Made of connexons
Connexons
Hexagonal tubes that are make of 6 connexins
Advantages of gap junctions
Are really fast
A lot of insects have them as their main signaling mechanism which is why there are so fast
Disadvantages of gap junctions
The signal is bidirectional
Function of gap junctions
- Allows cells to work all together since if one cell is depolarized, the next cell will be as well (In smooth and cardiac muscle)
- Helps in signal transduction pathways
Integrins
Connects the cytoskeleton to the ECM by ECM proteins and the adaptor protein
Helps in cells migration, wound healing, and macrophages
Adaptor proteins
Interacts with keratin and actin filaments of the cytoskeleton
ECM proteins
Collagen, laminin, and fibronectin
Mechanism of Integrins
- Integrins are in the inactive or bent form
- Signal transduction pathway will phosporlate talon and talon will activate Integrins by getting rid of the mask on the ECM binding side and dimerizing the integrins together
- Ingegrins bind to the specific ECM protein
- Focal-adhesion molecules will recruit intracellular proteins to hold the integrin in place (vincillin and actin)
Cytoskeleton
Made of actin and myosin
Actin
Small protein that has 2 forms
- G-actin: monomer
- F-actin: polymer
Can work by itself or with myosin
Myosin II
Most abundant type and found in muscle cells
Myosin I and V
Found in non-muscle cells
Microfilaments
Made of F-actin and bound proteins
Thinnest filaments of the cytoskeleton
Polymerization of actin (nucleation)
G monomer has clefts to which ATP binds. Mg is needed as a cofactor (ATP binds here). Binding of ATP leads the G monomer to be converted to F-actin which is a double helical form
Equilibrium between…
G actin and F actin forms
Part of actin
Has 2 parts:
- Positive end
- Negative end
Positive end
Activated G actin can easily be attached and elongate the actin filaments
Negative end
Depolymerization happens here and stabilizes the structure
Cytochalasins
Inhibit polymerization and activate depolymerization
Bad since the cell doesn’t have any support so is weak
Phalloidans
Inhibit depolymerization and activates polymerization
Bad since the cell doesn’t need that much actin
Actin location
Located at the peripheral regions of the cell since this is where the cell moves
Actin function
- Stabilize periphery of cell
- Responsible for cell shape
- Allows cell movement
- Can generate force with myosin
Cell movement by actin
- Integrin-shuttle movement: cell rolls on its membrane due to actin and integrin is inserted through the front of the cell
- Transcytosis: actin helps move the materials through the cell
- Elongation of membrane: actin helps vesicles fuse into the membrane to elongate it
Myosin I
Small motor protein that works with actin
Has 2 domains:
- TH1 domain
- Motor domain
Motor domain
Binds to actin
Has nucleotide binding pockets where ATP and ADP bind
TH1 domain
Binds to the vesicle/organlelle
Neck region
In between the two domains
Myosin I function
- Membrane cytoskeleton adhesion: provides integrity to the cell
- Endocytosis/exocytosis: in endocytosis, myosin pulls the material inwards
- Vesicle shedding: myosin helps move cell membrane parts out of the cell (ex: mammary glands)
- Channel gating/adaptation: helps in signal transduction (ex: hair cells)
Myosin V
Helps transport organelles and vesicles
Myosin V mechanism
ADP is bound the to the two motor domains so it’s in the waiting state. When an ATP replaces the ADP, the motor domain moves and takes a step forward and lands in the 13th actin unit. This process is repeated until finally, ATP is hydrolyzed and myosin V goes back to the waiting state
Microtubules
Made of alpha and beta tubulin.
Alpha and beta tubulin form a row called a protofilament with the help of GTP
13 protofilaments together will form a tubulin structure and this structure is tubular
Parts of microtubules
Have two ends
- Positive end: beta tubulin on this side and GTP tubulin is added so elongation on this side
- Negative end: alpha tubulin and GDP tubulin is here so it falls apart. Need a GTP molecule to be added here in order to keep the molecule together. This is known as catastrophe and rescue
Function of microtubules
- Transport (this is really fast and done by microtubules since actin and myosin are too slow)
- Helps in mitosis (organized in centrosomes)
- Helps in cell shape
Microtubules associated proteins (MAPs)
Can be divided into:
- Non-motor proteins
- Motor proteins
Nonmotor proteins
Helps organize the microtubules
Have MAPI(MAPS1 and MAPS1B) and MAPS II (MAPS2 and MAPS 4 and tau)
MAPSII
Attach vesicles to the ER
Motor MAPS
Have kinesin and dyenin
Have a similar walking mechanism to myosin V and walk in opposite directions
Dyenin
Retrograde transport so goes from cell membrane to ER
Kinesin
Is anterograde transport so goes from ER to cell membrane
Cilia
Microtubules that help remove cilia in the respiratory tract. Turns like a propeller to expel material
Organized into 9+2 and have A and B tubules and connected by dyenin
Dyenin helps the cilia move very slowly in a clockwise manner
Flagellum
A long cilia that has one turning to move and the other turning in the opposite direction to move things out of the way
Intermediate microfilaments
Very string microfilaments and part of the cytoskeleton
Provide mechanical support and shape maintenance
Help connect desmosomes together
Structure of intermediate microfilaments
IFs are intertwined into a dimer to form a double helix.
2 dimers come together to form a tetramer
8 tetramers make an IF
Myosin
Anisotropic so doesn’t allow light pass through and this is why the A band is dark
Main component of thick filaments
Has three parts:
- Head: attaches to actin
- Neck
- Tail
H zone
No intersection between actin and myosin so that’s why it’s light
Thin filaments
Have actin, troponin, and tropomyosin
Held in place by the Z disc