Cell Interactions Flashcards

0
Q

What are the three main domains of Cell adhesion molecules (CAMs)?
What are the three main families of CAMs?

A

The extracellular domain, the transmembrane domain and the cytoplasmic domain.
The three families are: Cadherins, immunoglobulins and selectins.

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1
Q

Interactions in multicellular organisms are mediated by what?
What enables interactions between cells?

A

Direct cell-cell contacts and indirect extracellular matrix-cell interactions.
Cell adhesion molecules enable the contacts.

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2
Q

What is the most prevalent CAM found in vertebrates?
What type of binding are they involved in with what other CAM molecule?
What is this binding dependent on?
What is the cytoplasmic domain linked to?

A

Cadherins are the most prevalent CAM. They are involved in homotypic binding with the same type of Cadherin molecule. This binding is dependent on calcium ion concentrations with high concentrations leading to binding and cell association. The cytoplasmic domain is linked to the actin cytoskeleton.

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3
Q

What are the characteristics of immunoglobulin-like CAMs?

Describe the PSA region of these CAMs and what they modulate.

A

They have immunoglobulin-like repeats and are involved in homophilic interactions with other N-CAMs. Finally these interactions are calcium ion independent.
The polysialic acid region (PSA) comprises of three carbohydrate chains with a negative charge. They modulate cell adhesion as large PSA regions repel cells and short PSA regions may bind to cells.

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4
Q

What do selectins/lectins bind to and what type of interaction is it?

A

Selectins bind weakly to olligosaccharides, these interactions being heterotypic interactions.

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5
Q

How are stable cellular adhesions formed?

What are the interactions between CAMs and what are the interactions between ligand-receptors?

A

Stable cellular adhesions are formed through clustering of multiple receptors. CAM interactions are cis interactions compared to the trans interactions of ligand-receptors.

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6
Q

What are the four types of cell-cell interactions?

A

Tight junctions,
Adherens junctions,
Desmosomes,
Gap junctions.

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7
Q

What are tight junctions?

A

These are a type of cell-cell interaction. They result in tight linkages between two membranes and the linkage between the actin cytoskeletons of both cells.

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8
Q

What are adherens junctions?

A

These are mediated by cadherins which makes the interactions calcium ion dependent. The two cells are linked by their actin cytoskeletons.

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9
Q

What are desmosomes?

A

These cell-cell interactions are associated with the intermediate filament network. Keratin filaments connect the cytoskeletons of two cells via linked desmosomes. The cell-cell membranes are linked through desmosomal proteins making the interaction indirect.

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10
Q

What are the three protein families involved in desmosomal linkage?

A

Desmosomal cadherins,
Armadillo family proteins,
Plakin family of cytolinker.

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11
Q

What are gap junctions?

A

These are formed from members of the protein connexin. These aggregate into hemi-channels which then interact to form channels 1.4nm in diameter, allowing for the selective transit of molecules.
They are found in most animal tissues such as epithelial cells and muscle cells. They can be opened and closed in response to extracellular signals.

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12
Q

What are the cell-cell junctions in plants called?

A

There are cytoplasmic links called the plasmodesmata. The ER are connected through these junctions. They allow ions and small molecules to pass through.

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13
Q

What is the main function of the extracellular matrix?

What are the three fundamental components of the ECM?

A

To provide structural and biochemical support to surrounding cells.
Collagens, glycoproteins and proteoglycans are the three main components.

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14
Q

What are the monomers of collagens and how are they arranged?
What are collagens characterised by?

A

The monomers are α-chains. Three α-chains form and triple helix.
Collagens are characterised by repetitions of specific sequences, and the conversion of prolines and lysines to hydroxyproline and hydroxylysine respectfully through post translational modification.

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15
Q

What are the different types of collagen aggregates?

A
Fibril-forming collagens,
Fibril-associated collagens,
2D network-forming collagens,
Filament-forming collagens,
Specialised structures.
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16
Q

What are some diseases associated with collagen?

A

Mutations in fibrillar collagens can result in Ehlers-Danlos syndrome and Osteogenesis imperfecta.
Defects of collagen processing can result in scurvy which is caused by a lack of vitamin C.

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17
Q

What are glycoproteins?

A

They are diverse group of proteins which play a major role in ECM. They have a variable protein core. Attached to the peptide is a olligosaccharide. Olligosaccharides bound to serine or threonine in the peptide are called O-linked Olligosaccharides. If they are linked to asparagine they are N-linked Olligosaccharides.

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18
Q

What is fibronectin and what are its functions?

A

Fibronectin is a glycoprotein. It’s functions are to interact with multiple ECM components and it is involved in cell adhesion. It also increases the stretchability of polymers.

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19
Q

What are laminins?

A

These are a family of glycoproteins and are an integral part of the structural scaffolding in almost every tissue of an organism. They are secreted and incorporated into the ECM. They are heterotrimers, containing a α-chain, β-chain and a γ-chain. There subunits are glycoproteins and they are found in the basal lamina.

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20
Q

What are proteoglycans?

A

Like glycoproteins, they have a central protein core. They have long glycosaminoglycan side chains and N-linked oligosaccharides. They are multi domain proteins, and if they’re on the cell surface they can interact with growth factors, ECM components and CAMs.

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21
Q

Name four examples of tissue specific ECMs.

A

Basement membranes, bone, cartilage and elastic tissues.

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22
Q

Most cells need to be able to bind to substrates as this is essential for what cellular functions?

A

Stable anchoring, differentiation, proliferation, migration, signalling and survival.

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23
Q

The loss of cell matrix contact can cause what?

A

Cell death, anoikis.

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24
Q

How can cell adhesion be tested for?

What can cell spreading result in?

A

It can be tested for via a cell attachment assay.
Cell spreading can result in the attachment of large areas of cell surface to the substrate and the flattening of cell bodies.

25
Q

How do cells interact with the 3-dimensional matrix?
What is cell adhesion dependent on?
What are the two major adhesive cell surface structures?

A

Contact with collagen fibrils, adhesion to ECM elements, modification of the matrix by cells and migration.
Cell adhesion is dependent on specific ligands/receptors.
Focal adhesions and hemidesmosomes are the two surface structures.

26
Q

What are the three classes of receptors?

A

Integrins, dystrophin-dystroglycan complexes, cell-surface proteoglycans.

27
Q

What are integrins?

A

Integrins are membrane bound receptors which function for ECM molecules. They all possess a extracellular domain, a transmembrane domain and a intracellular domain which is linked to the cytoskeleton. They are heterodimers with α and β subunits.

28
Q

What defines the specificity of the ligand binding domain on integrins?
What are the two ways binding can occur?

A

An alpha subunit.
In one both the α and β subunits are involved with the ligand binding in the cleft region between the beta propellor domain and the N-terminal domain.
In the other binding mechanism the α-subunit is not involved and an extra domain αA is involved.

29
Q

What defines families of integrins?
Similar ligands may be recognised by what?
Multiple ligands may be recognised by what and what motif in ligands allows for recognition?

A

Common subunits defines families of integrins.
Similar ligands may be recognised by multiple receptors.
Multiple ligands may be recognised by a single receptor, with the RGD motif allowing for recognition as it is present in many ligands.

30
Q

What integrin structure is the low affinity structure and what one is the high affinity structure?

A

The blended structure is the low affinity structure and the extended structure is the high affinity structure.

31
Q

What are integrins focused in?

What are these adhesion structures found in?

A

Integrins are focused in focal contacts. Focal contacts are found in motile cells and cells in tissues.

32
Q

Describe intracellular signalling caused by integrins?

A

Ligand binding causes conformational changes to occur which have affects on adaptor proteins and signalling kinases. Consequently signal pathways are activated which can have numerous effects on the cell.

33
Q

What are hemidesmosomes?

A

These are electron dense areas found on the basal side of epithelial cells. They are complex anchoring structures and possess a basal connection to the underlying basement membrane.

34
Q

What are dystrophin-dystroglycan complexes?

A

Hesse are multi-protein cell matrix receptor complexes constructed from dystrophin and dystroglycan α and β subunits. They form essential connections between basement membranes and actin cytoskeletons.

35
Q

What are cell-surface proteoglycans?

A

They possess a protein core domain and often have intracellular and extracellular domains. They possess a glycosaminoglycan side chain. These interact with ECM proteins such as collagens, Fibronectin etc.

36
Q

What is the main structure of flagella?

A

Two microtubules surrounded by nine doublet microtubules which are connected by different structures. They are anchored in the cell body by a specialised basal body which is comprised of nine triplet microtubules.

37
Q

What causes movement of the microtubules in the flagella/cilia?

A

Dynein binds to the microtubules and its movement causes a relative shift in the microtubules. Bridging structures limit the sliding of microtubules and cause bending of the flagellum.

38
Q

Cell migration can be measured in what ways?

A

In vitro wound healing assay.
Video time lapse microscopy-cells observed by a video camera, images taken at regular time intervals and the cell migration speed measured.

39
Q

What are the two ways cells can migrate?

A

Random movement-there is no preferred direction of migration.
Chemotaxis-in the presence of a gradient of a chemo-attractant substance, cells migrate preferentially in a defined direction.

40
Q

Migration is dependent on cellular adhesion, elaborate on this.

A

Receptors (integrins) are connected to focal contacts which are in turn linked to the cytoskeleton. Force produced from the actin cytoskeleton when contracting is translated to the substrate via focal contacts.

41
Q

Most cells need to be able to bind to substrates as this is essential for what cellular functions?

A

Stable anchoring, differentiation, proliferation, migration, signalling and survival.

42
Q

The loss of cell matrix contact can cause what?

A

Cell death, anoikis.

43
Q

How can cell adhesion be tested for?

What can cell spreading result in?

A

It can be tested for via a cell attachment assay.
Cell spreading can result in the attachment of large areas of cell surface to the substrate and the flattening of cell bodies.

44
Q

How do cells interact with the 3-dimensional matrix?
What is cell adhesion dependent on?
What are the two major adhesive cell surface structures?

A

Contact with collagen fibrils, adhesion to ECM elements, modification of the matrix by cells and migration.
Cell adhesion is dependent on specific ligands/receptors.
Focal adhesions and hemidesmosomes are the two surface structures.

45
Q

What are the three classes of receptors?

A

Integrins, dystrophin-dystroglycan complexes, cell-surface proteoglycans.

46
Q

What are integrins?

A

Integrins are membrane bound receptors which function for ECM molecules. They all possess a extracellular domain, a transmembrane domain and a intracellular domain which is linked to the cytoskeleton. They are heterodimers with α and β subunits.

47
Q

What defines the specificity of the ligand binding domain on integrins?
What are the two ways binding can occur?

A

An alpha subunit.
In one both the α and β subunits are involved with the ligand binding in the cleft region between the beta propellor domain and the N-terminal domain.
In the other binding mechanism the α-subunit is not involved and an extra domain αA is involved.

48
Q

What defines families of integrins?
Similar ligands may be recognised by what?
Multiple ligands may be recognised by what and what motif in ligands allows for recognition?

A

Common subunits defines families of integrins.
Similar ligands may be recognised by multiple receptors.
Multiple ligands may be recognised by a single receptor, with the RGD motif allowing for recognition as it is present in many ligands.

49
Q

What integrin structure is the low affinity structure and what one is the high affinity structure?

A

The blended structure is the low affinity structure and the extended structure is the high affinity structure.

50
Q

What are integrins focused in?

What are these adhesion structures found in?

A

Integrins are focused in focal contacts. Focal contacts are found in motile cells and cells in tissues.

51
Q

Describe intracellular signalling caused by integrins?

A

Ligand binding causes conformational changes to occur which have affects on adaptor proteins and signalling kinases. Consequently signal pathways are activated which can have numerous effects on the cell.

52
Q

What are hemidesmosomes?

A

These are electron dense areas found on the basal side of epithelial cells. They are complex anchoring structures and possess a basal connection to the underlying basement membrane.

53
Q

What are dystrophin-dystroglycan complexes?

A

Hesse are multi-protein cell matrix receptor complexes constructed from dystrophin and dystroglycan α and β subunits. They form essential connections between basement membranes and actin cytoskeletons.

54
Q

What are cell-surface proteoglycans?

A

They possess a protein core domain and often have intracellular and extracellular domains. They possess a glycosaminoglycan side chain. These interact with ECM proteins such as collagens, Fibronectin etc.

55
Q

What is the main structure of flagella?

A

Two microtubules surrounded by nine doublet microtubules which are connected by different structures. They are anchored in the cell body by a specialised basal body which is comprised of nine triplet microtubules.

56
Q

What causes movement of the microtubules in the flagella/cilia?

A

Dynein binds to the microtubules and its movement causes a relative shift in the microtubules. Bridging structures limit the sliding of microtubules and cause bending of the flagellum.

57
Q

Cell migration can be measured in what ways?

A

In vitro wound healing assay.
Video time lapse microscopy-cells observed by a video camera, images taken at regular time intervals and the cell migration speed measured.

58
Q

What are the two ways cells can migrate?

A

Random movement-there is no preferred direction of migration.
Chemotaxis-in the presence of a gradient of a chemo-attractant substance, cells migrate preferentially in a defined direction.

59
Q

Migration is dependent on cellular adhesion, elaborate on this.

A

Receptors (integrins) are connected to focal contacts which are in turn linked to the cytoskeleton. Force produced from the actin cytoskeleton when contracting is translated to the substrate via focal contacts.