Test Three Flashcards

1
Q

Chemical processes must stay isolated through

A

Membrane-enclosed compartments

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2
Q

How many compartments in prokaryotic cells

A

One compartment

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3
Q

Eukaryotic cells contain

A

Many organelles with specialized functions

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4
Q

What is the structure of the nucleus

A

Double membraned nuclear envelope with nuclear pores

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5
Q

Function of nuclear pores

A

Allow RNA to leave cell and bring raw materials into the cell

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6
Q

What is the structure of the ER

A

Flattened sacs

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7
Q

Where is the location of the ER

A

Extension of nuclear envelope

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8
Q

Rough ER function

A

Protein production

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9
Q

Smooth ER function

A

Production of lipids

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10
Q

What organelle is similar to ER

A

Sarcoplasmic reticulum

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11
Q

Function of sarcoplasmic reticulum

A

Stores calcium

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12
Q

Function of golgi

A

Modified proteins and lipids for transport (modify and package)

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13
Q

Structure of golgi

A

Contains cisternae that stacks of compartments

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14
Q

Function of lysosomes

A

Breakdown endocytosed molecules such as macromolecules and old, nonfunctioning organelles

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15
Q

Function of peroxisomes

A

Breakdown toxins to the cell and breakdown lipids and uses oxidative reaction

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16
Q

Function of endosomes

A

Sort endocytosed material coming into cell

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17
Q

Structure of mitochondria and chloroplasts

A

Double membrane

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18
Q

Function of chloroplasts

A

ATP production through photosynthesis

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19
Q

Function of mitochondria

A

ATP production through oxidative phosphorylation

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20
Q

Function of cytoskeleton

A

Hold organelles in place, moving vesicles through the cell, provide structure and support

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21
Q

What are the two theories of organelle evolution theories

A

Invagination and eukaryotic engulfing

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22
Q

When the cell divides what else divides

A

Organelles such as the nuclear envelope, ER and golgi

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23
Q

What is invagination

A

Plasma membrane enfolded to surround and protect the DNA

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24
Q

What is engulfing

A

Organelles such as a mitochondria were engulfed by an ancient eukaryotic cell and once inside split into two different mitochondria organelles

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25
Q

New lipids come from

A

Smooth ER

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26
Q

During cell division what organs divide as well

A

Nuclear envelope, ER and golgi

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27
Q

What happens to proteins in the cell

A

Formed constantly, sorted and delivered

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28
Q

Why are proteins formed constantly

A

Need for general maintenance

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29
Q

What is a sorting signal

A

Amino acid sequence that is part of protein telling where to go

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30
Q

Where are some end destinations of proteins

A

Mitochondria, chloroplasts, peroxisomes

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31
Q

What are the three types of protein transport

A

Gated, transmembrane and vesicular

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32
Q

Gated transport occurs only through

A

Nucleus

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33
Q

Where is nucleus does proteins go through for gated transport

A

Nuclear pores

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34
Q

Describe type of molecules that go through gated transport

A

Specific for larger molecules, specific sequence in protein, folded proteins only

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35
Q

Transmembrane transport is what for proteins

A

Protein translocators

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36
Q

What is protein translocators

A

Locate proteins across the membrane

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37
Q

Where are transmembrane transports found

A

ER, mitochondria, chloroplasts, and peroxisomes

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38
Q

Transmembrane transport requires

A

Unfolding of the protein

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39
Q

Vesicular transport contains vesicles that bud from

A

ER and take part of membrane with them

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40
Q

Where do vesicles in vesicular transport go

A

Go to golgi, lysosome, or cell membrane and fuse with their membrane

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41
Q

Vesicles in vesicular transport carry what

A

Deliver lipids and proteins

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42
Q

What are signal sequences

A

Sorting signals of 15 to 60 amino acids that get the protein where it needs to go

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43
Q

Signal sequences are cleaved by

A

Signal peptidases

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44
Q

What happens to protein when signal sequence is cleaved

A

Protein can now fold correctly once at its new location

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45
Q

What are signal patches

A

Sorting signal is the 3D conformation that is recognized by sorting receptors

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46
Q

What in nucleus regulates what is going in and out

A

Inner membrane that contains binding sites

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47
Q

The outer nuclear membrane is similar to what organelle

A

ER

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48
Q

Function of outer nuclear membrane

A

Structural support

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49
Q

Outer nuclear membrane is continuous with what

A

ER

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50
Q

Nuclear pore transport goes through

A

Nucleoporins

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51
Q

What is the movement of nuclear pore transport

A

Both in and out

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52
Q

What goes in nucleoporins

A

Proteins

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53
Q

What goes out of nucleoporins

A

RNA and ribosome subunits

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54
Q

What channels in nucleus allow for small water soluble molecules to pass through

A

Water channels

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55
Q

Larger molecules need to have what to be directed into the nucleus in nuclear transport

A

Nuclear localizing signal (NLS)

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56
Q

What is a nuclear transport receptor

A

Mediate interaction between cytosol located on the nuclear protein and nuclear pore

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57
Q

How do nuclear transport receptors work

A

Receptors bind signal on the protein and move through the pore of the nucleus

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58
Q

What is needed for nuclear transport receptor to work

A

GTP hydrolysis

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59
Q

Proteins being transported into the mitochondria have to be

A

Unfolded

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60
Q

What is in the mitochondria to help refold the protein

A

Chaperones

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61
Q

Lipids bound for organelles are transported how

A

Vesicular transport

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62
Q

Proteins transported to ER need to be

A

Unfolded

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63
Q

Proteins leave the ER in what

A

Transport vesicles

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64
Q

What types of proteins can enter into ER

A

Water soluble proteins

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65
Q

What proteins are membrane bound with ER transmembrane transport

A

Potential transmembrane proteins

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66
Q

What directs the protein to the ER

A

ER signal sequences

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67
Q

Can proteins be partially formed before they cross the ER membrane

A

Yes

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68
Q

What are the three types of ribosomes in the ER

A

Membrane bound ribosomes, free ribosomes and polyribosomes

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69
Q

Membrane bound ribosomes go where in the ER

A

Attached to the cytosolic side of the ER

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70
Q

Where are free ribosomes in the ER

A

Unattached, they will make proteins from other nuclear DNA that’s out in the cytosol

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71
Q

What are the polyribosomes in the ER

A

1 long mRNA with the ribosomes bound to it

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72
Q

What are the components required to direct a protein into the ER

A

Signal recognition particle (SRP) and SRP receptor

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73
Q

What a re signal recognition particle (SRP)

A

Bind to signal sequence of protein in the cytosol

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74
Q

Where is the SRP receptor located for protein transport into ER

A

Membrane bound on ER

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75
Q

Binding of SRP to protein results in

A

Slowing of synthesis

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76
Q

Does synthesis of protein occur after SRP binds to it

A

Yes

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77
Q

What cleaves an SRP

A

Signal peptidases

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78
Q

What is transmembrane transport into ER membrane

A

The protein remains partially in the membrane

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79
Q

What is a single pass protein

A

Protein that has only one portion spanning the membrane

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80
Q

What occurs during single pass protein transport into ER membrane

A

Signal sequence assists the protein getting into membrane till it hits the stop transfer sequence (hydrophobic A.A.) and will stop the protein from entering any further

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81
Q

What is a multi pass protein

A

Protein the spans the membrane multiple times

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82
Q

How does a multi-pass protein transport into the ER membrane

A

Contains internal signal sequence (start sequence) in the middle of the protein then contains several stop-signal sequences

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83
Q

What is vesicular transport

A

Protein goes from ER to Golgi apparatus through transport vesicles

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84
Q

In order for protein to leave ER what must happen

A

It must be protected/ stabilized with chemical modifications such as carbohydrates added or disulfide bonds added

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85
Q

Secretory pathway of vesicular transport AKA

A

Exocytosis

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86
Q

What is secretory pathway of vesicular transport

A

Transport proteins to cell surface or lysosomes

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87
Q

What is endocytic pathway of vesicular transport

A

It’s an internal pathway that uses selective transport, taking something from outside in

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88
Q

Coated vesicles have what type of coat

A

Protein

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89
Q

Vesicle coat functions

A

Forms the membrane into a bud and captures selected molecules, helps develop membrane of vesicle, select molecule interested in carrying. NOT USED FOR PROTECTION!

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90
Q

What is the structure of clathrin-coated vesicles

A

Triskelion

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91
Q

Clathrin coated vesicles move from

A

Golgi outward or plasma membrane inward

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92
Q

If a clathrin-coated vesicle is being created, what is needed

A

Dynamin to help form a ring that contracts and helps pinch off the vesicle from membrane

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93
Q

Function of adaptin

A

Mediate interaction between clathrin, select molecules for transport, secure clathrin to plasma membrane

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94
Q

What are the two types of adaptin types

A

Bind cargo receptors in plasma membrane to pull things in or bind cargo receptors in Golgi apparatus to pull things out

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95
Q

COP coated vesicles go to

A

Golgi and ER

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96
Q

In vesicle docking, transport vesicles have what surface marker

A

Rab

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97
Q

What is Rab

A

Surface marker of transport vesicles directing vesicle that are recognized by and binds to tether proteins

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98
Q

What are tether proteins

A

Help dock vesicle by being the receptor for surface markers, grab hold of Rab

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99
Q

What are the two types of SNAREs

A

V-SNARE( vesicle) and t-SNARE (target)

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100
Q

What is exocytosis

A

Proteins exit the cell and this specific and has directed routes

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101
Q

How do SNARE’s interact

A

Remove water from vesicle to allow for merging and draw membranes together through chemically intertwined snares

102
Q

What are the two protein modifications in the ER

A

Formation of disulfide bonds and glycosylation

103
Q

The formation of disulfide bonds on proteins in the ER help what

A

Stabilize proteins and protect them

104
Q

Where do disulfide bonds occur in proteins in ER modification

A

At cysteine residues

105
Q

What occurs during glycosylation of proteins in ER modifications

A

Oligosaccharides side chains attach to proteins and become glycoproteins

106
Q

What is the function of oligosaccharides in ER modifications

A

Protects from degredation outside of cell, chaperoning for proper folding, directing to correct location, assisting in INTERCELLULAR recognition between cells.

107
Q

How does oligosaccharide processing occur in ER modification

A

Add 14 sugars at a time using oligosaccharide transferase and dolichol to anchor the sugar

108
Q

What occurs when protein is leaving the ER

A

Transport vesicle begins to bud, proteins have to be folded correctly and if not chaperones will keep protein in ER.

109
Q

What occurs with cystic fibrosis mutation and protein exiting the ER

A

Chaperones wont let the protein out due to a problem with the chloride transport protein

110
Q

What is the unfolded protein response in the ER

A

When the ER and chaperones become overwhelmed it triggers a response causing the ER to grow and more chaperones grow but the chaperones can not keep up and causes apoptosis

111
Q

What is an example of unfolded protein response in the ER

A

Diabetes

112
Q

Vesicles from the ER enter where in the golgi

A

Cis side

113
Q

What happens if proteins from the ER have ER retention signal

A

Receptors on the Cis of golgi will see signal and send the protein back to the ER

114
Q

What occurs when the protein is in the golgi

A

Oligosaccharide removal and/or addition

115
Q

What are the two exocytosis pathways

A

Constitutive and regulated

116
Q

What is constitutive exocytosis pathway

A

Default pathway that has no direction specificity

117
Q

What is regulated exocytosis pathway

A

Secretion that is specific loading of molecules and specific transport

118
Q

Where are the destinations for the proteins in exocytosis

A

Adhesion to cell surface, incorporation into extracellular matrix, diffusion into extracellular fluid

119
Q

What is not needed for constitutive pathway

A

No signal sequence necessary

120
Q

What are the secretory products in regulated exocytosis pathway

A

Hormones, mucus, digestive enzymes, neurotransmitters

121
Q

Describe secretory vesicles of regulated exocytosis pathway

A

Packaged with only one type of molecule

122
Q

Where are the vesicles located in regulated exocytosis pathway

A

Near the plasma membrane but will wait for signal to unload

123
Q

How does the vesicle prepare itself

A

Gets concentration of aggregated proteins for export and vesicle pinches off

124
Q

The fusion of membranes is a

A

Temporary membrane combination

125
Q

What are the two types of endocytosis

A

Pinocytosis and phagocytosis

126
Q

What is pinocytosis

A

Cellular drinking, taking in fluids but also small molecules

127
Q

What is phagocytosis

A

Cellular eating, taking in cellular debris, microorganisms

128
Q

What endocytosis do all cells use

A

Pinocytosis

129
Q

What are phagocytic cells

A

Macrophages and neutrophils

130
Q

What is the target material of phagocytes

A

Dead RBC’s

131
Q

Function of phagocytes

A

Digest phagocytosed materials and destroying it with lysosomes

132
Q

What is the phagocytic process

A

Materials bind to phagocytic cell through specific surface receptors then the pseudopods extend from plasma membrane and pull pathogen into cell then the phagosome and lysosome fuse and digestion occurs

133
Q

What are the two surface receptors of phagocytes

A

Antibody based receptors (specific) and receptors specific for common proteins (general)

134
Q

What pathogen escapes phagocytic process

A

Tuberculosis bc want to be eaten by macrophage and prevent phagosome and lysosome from fusing

135
Q

What materials are engulfed in pinocytosis

A

Lipids and fluids

136
Q

What occurs to the plasma membrane components when engulfed through pinocytosis

A

Returned to cell

137
Q

Pinocytosis macrophages ingest how much fluid volume in one hour

A

25%

138
Q

What is located in smaller vesicle of pinocytosis cell vesicle goes to

A

Endosomes

139
Q

Function of endosomes

A

Where sorting takes place, determine where things are going to

140
Q

What makes pinocytosis specific

A

When clathrin coated pits are added

141
Q

Example of pinocytosis

A

Cholesterol is taken up specifically by bringing cholesterol into cell then digested by lysosome. If LDL receptor is missing, then there is a build up then you have cholesterol building up in vessels and cant be digested

142
Q

What are examples of misuse of endocytic pathways

A

HIV and influenza

143
Q

What is the structure of endosomes

A

Contain ends that are called early and late which contains a network of tubes and vesicles

144
Q

What happens to the receptors on the endosome

A

Recycled or degraded

145
Q

How do endosomes sort

A

Transcytosis

146
Q

What is transcytosis

A

Moving the loaded receptor with molecule to another side of the membrane

147
Q

Structure of lysosome

A

Stacks of very strong digestive enzymes

148
Q

What enzyme is used in lysosomal digestion

A

Acid hydrolases

149
Q

What is the lysosomal environment and how maintained

A

Acidic for better function of enzymes and is maintained by H+ pump

150
Q

What occurs after lysosomal digestion

A

Membrane proteins allow particles to be exported

151
Q

What is the inner surface of lysosomal membrane like

A

Highly glycosylated

152
Q

What occurs to vesicles that are heading to lysosome

A

Tagged with sugar called M6P

153
Q

Purpose of M6P tag on vesicles

A

Keep them from binding to everyone else

154
Q

What are autophagosomes

A

Engulf non-functional organelles and form a vesicle from own membrane and deliver to lysosomes

155
Q

What is a signal transduction

A

Sending information into cells in language they understand

156
Q

What are signaling molecules

A

Neurotransmitters, one receptor and another coming together

157
Q

An intracellular response causes

A

Cell signaling

158
Q

What are the five types of signaling

A

Endocrine, paracrine, neuronal, contact and autocrine

159
Q

Endocrine signaling goes where

A

Whole body signaling

160
Q

What are the signaling molecules in endocrine signaling

A

Hormones secreted in bloodstream

161
Q

What are the signaling cells in the endocrine signaling

A

Endocrine cells

162
Q

Example of endocrine signaling

A

Pancreas secreting insulin

163
Q

Paracrine signaling location

A

Local diffusion in extracellular matrix

164
Q

What are the signaling molecules in paracrine signaling

A

Local mediators, cytokines

165
Q

What are the signaling cells in paracrine signaling

A

Immune cells or injured cells

166
Q

Example of paracrine signaling

A

Inflammation and wound healing

167
Q

Location of neuronal signaling

A

CNS

168
Q

Signaling molecules of neuronal signaling

A

Neurotransmitters

169
Q

Signaling cells of neuronal signaling

A

Neurons

170
Q

Example of neuronal signaling

A

Crossing synapses to target tissues

171
Q

Location of contact dependent signaling

A

Between cells, intimate, short range

172
Q

Signaling molecules of contact dependent signaling

A

Receptor binding to ligand

173
Q

Signaling cells of contact dependent signaling

A

Any cell because all have receptors

174
Q

Example of contact dependent signaling

A

Embryonic development

175
Q

What is autocrine signaling

A

Cell will signal to itself

176
Q

Cell signaling is a selective response and how

A

Choosing the signals that apply since they are hit from all sides by different signals

177
Q

What limit what signals the cell receives

A

Cellular receptors

178
Q

Cellular receptors have what type of response and due to what

A

Complex response and due to result of receptor binding

179
Q

What is an example of a complex response with cellular receptors

A

Acetylcholine binding to pacemaker to slow down rate or salivary gland causing secretion

180
Q

What are simultaneous receptor stimulation

A

Collection of receptors, intracellular signaling yields larger cellular response

181
Q

How does it take for multiple receptors simultaneously

A

Longer response due to cell dividing, differentiating or programmed cell death

182
Q

Single receptor can include what in the signal

A

Change in cell shape, movement, metabolism or gene expression. This is fast

183
Q

Large molecules rely on what type of receptor

A

Extracellular receptor

184
Q

Small molecules (hydrophobic) can pass directly through membrane and affect what

A

Enzymes by turning them on or off

185
Q

Small molecules that pass directly through the membrane bind to what receptor

A

Intracellular

186
Q

Example of small hydrophobic molecule that passes through membrane

A

Hormones

187
Q

Hormones target what receptors

A

Intracellular receptors

188
Q

Examples of hormones

A

Cortisol, estradiol, testosterone, and thyroxine

189
Q

When hormones bind to intracellular receptors what happens to them

A

Conformational change occurs which changes in gene expression

190
Q

Is nitric oxide a hormone

A

No

191
Q

What is the half life of NO

A

5 to 10 seconds before converted to nitrate

192
Q

How does NO work

A

Enters cell directly to activate intracellular enzymes

193
Q

Example of NO

A

Endothelial cells NO to relax blood vessels when they are constricted

194
Q

What enzyme does NO activate

A

Guanylyl Cyclase to form GMP

195
Q

What is in a signaling cascade

A

Primary transduction step, intracellular signal and signaling cascade

196
Q

What is the primary transduction step

A

First binding of ligand to receptor

197
Q

Bind of a ligand to receptor in signaling cascade causes

A

Intracellular signal leading to multiple intracellular signals (cascade)

198
Q

What are the steps in functions of signaling cascades

A

Transforming external signal into intracellular molecule for signaling, relaying signal to cellular response, amplify signal, distributing signal, integration of signal (lead to other pathways)

199
Q

What are the two types of receptors for molecular switch

A

G protein coupled receptors and enzyme receptors

200
Q

How do molecular switches work

A

Molecular switches are activated when signaled and then turn on other protein and then turn off in response to another signal

201
Q

molecular switches are

A

Chemical transducers or signaling messengers

202
Q

What are the two types a of molecular switches

A

Phosphorylation activated and GTP binding activated

203
Q

What is phosphorylation activated and inactivated switches

A

Kinase adds phosphate to turn on and removes to turn off

204
Q

What kinases are used in phosphorylation activation switches

A

Serine threonine kinase and tyrosine kinase

205
Q

GTP binding activated switch works how

A

Add entire GTP and is activated, loses phosphate to GDP and becomes inactivate

206
Q

What are the three classes of receptors

A

Ion channel coupled, G protein coupled, and enzyme coupled

207
Q

What are ion channel coupled receptors

A

Ions bind to channels, open channels and ions enter

208
Q

What are G protein coupled receptors

A

Ligand bind to receptor, activates G protein, G protein can then activate enzyme

209
Q

How do enzyme coupled receptors work

A

Ligand binds them to enzyme and they become activated or they can bind to ligand that then binds to enzyme and binds to another enzyme to activate it

210
Q

Ion channel coupled receptors use what type of channel

A

Transmitter gated ion channel and act between synapses

211
Q

How do transmitter gated ion channels work

A

Turn chemical signal into electrical signal and changes membrane potential causing receptor to change conformation

212
Q

What is the largest family of receptors

A

G protein coupled receptors

213
Q

What is the structure of G protein coupled receptor

A

Weaves through membrane 7 times (transmembrane receptor protein)

214
Q

Example of G protein coupled receptor

A

Photo receptor, olfactory receptor, yeast mating receptor

215
Q

How is a G protein coupled receptor stimulated

A

Binds to a ligand, G protein becomes activated intracellularly

216
Q

Structure of G protein

A

Contains three subunits (alpha, beta and gamma)

217
Q

Inactivate form of G protein contains

A

GDP

218
Q

Active form of G protein contains

A

GTP

219
Q

When GTP removed on G protein what else separates

A

A subunit

220
Q

How is a G protein stimulated

A

Activation of receptor, alpha-GTP and gammabeta subunit bind together and interact with intracellular targets to trigger cascade

221
Q

How to inactivate G protein

A

Remove phosphate to become GDP

222
Q

G protein inactivation example

A

Cholera toxin changes the alpha subunit preventing the conversion of GTP to GDP, G protein always active

223
Q

What inactive protein causes G protein to always be off

A

Whooping cough, keep alpha subunit in inactive state

224
Q

What activates ion channel

A

Subunits of G proteins activate ion channels or enzymes

225
Q

Example of activation of ion channel

A

Acetylcholine binds to G protein receptor causes alpha subunit to activate that then causes gammabeta subunit bind to K+ channel to open it, to close it lose phosphate

226
Q

How are enzymes activated in G protein coupled receptors

A

Target adenylyl cyclase which then produces cAMP that then could activate phospholipase C to produce IP3 and DAG

227
Q

What activates second messengers

A

Stimulation of G proteins

228
Q

How is cyclic AMP stimulated

A

Ligand binds to receptor to activate G protein and the alpha subunit turns of adenylyl cyclase and then activates and increase in cyclic AMP

229
Q

How to inactivate cyclic AMP

A

Phosphodiesterase turns cAMP to AMP making it difficult to move through cell

230
Q

Pathway of cAMP

A

CAMP binds to cAMP-dependent protein kinase to activate it so that it can phosphorylate intracellular proteins such as PKA

231
Q

What causes PKA to change conformation

A

CAMP

232
Q

What us calmodulin

A

Calcium binding protein that response to increase Ca2+, it will change conformation and wrap itself around target protein

233
Q

What are the target proteins of calmodulin

A

CaM kinases

234
Q

Where is the domain in the enzyme coupled receptors

A

Intracellular domain that is the enzyme

235
Q

Enzyme coupled receptors are involved in changes in the

A

Cytoskeleton

236
Q

Structure of RTKs (receptor tyrosine kinases)

A

Single pass protein with an alpha helix

237
Q

How to RTKs become activate

A

Two RTKs come together to form a dimer active at the intracellular tails and the tails phosphorylate each other and act like a kinase

238
Q

What are the stopping signal of RTKs

A

Protein tyrosine phosphotases that remove receptor

239
Q

Where do you see Ras pathway in real life

A

Cancer which is overreaction of Ras and causes cell division

240
Q

RTKS activating Ras causes phosphorylation cascade resulting in

A

Change in gene expression

241
Q

Activated Ras protein can cause

A

Activation of MAP kinase cascade

242
Q

What inhibits Ras

A

Antibodies in pathway grab Ras, cell cant respond to extracellular signals

243
Q

What happens with overstimulation of Ras

A

Continuous cell proliferation, 30% of all cancer has Ras defect

244
Q

PI 3-kinase promotes

A

Cell growth and survival

245
Q

PI 3-Kinase phosphorylate s

A

Inositol phospholipids

246
Q

AKT inactivate

A

Bad to promote cell survival

247
Q

Akt activates what

A

Tor to promote cell growth

248
Q

Cytokines activate

A

Gene regulatory proteins

249
Q

Cytokine receptors associate with

A

JAKs

250
Q

JAKs phosphorylate what gene regulatory proteins

A

STATs

251
Q

Cellular receptors induce

A

Gene expression and cellular response