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Physiology Dr. Aka's class > The cell > Flashcards

The cell Flashcards

1
Q

What are the properties of the cell membrane?

A

Support- mechanical and chemical
Response to signals
Amphipathic
Fluidity

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2
Q

What are the membrane lipids?

A

Phospholipids
Glycolipids
Steroids

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3
Q

What do glycolipids do?

A

Provide membrane strength and a structural framework for the cell.

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4
Q

Gangliosidosis

A

Inappropriate development of the optic nerve due to the concentration of gangliosides not decreasing. This often is due to ineffective hexosamidases.

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5
Q

Scrambliosides

A

First step in apoptosis where enzymes redistribute the asymmetrical distribution of phosphoglycerides in the cell membrane.

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6
Q

What are the inner lipid players in the cell membrane?

A

Phosphatidylserine

Phosphotidyletholamine

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7
Q

What are the outer lipid players in the phospholipid bilayer?

A

Phosphatidylcholine

Sphingomyelin

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8
Q

What molecule has a hydroxyl head and a steroid ring that act to stabilize the lipid bilayer of a cell membrane despite temperature changes fluxuations?

A

Cholesterol

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9
Q

This component of cholesterol cements the phosphate head of the phospholipid.

A

The Hydroxyl component.

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10
Q

This disperses the hydrophobic tails of the phospholipid membrane.

A

The steroid ring of cholesterol.

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11
Q

This is in the external monolayer of the cell.

A

Glycocalyx

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12
Q

Covalently bonded with olgiosacchrides on the outer surface of the cell membrane to form a portion of the glycocalyx.

A

Glycolipids

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13
Q

Negatively charged to repel the negative charge of most bacteria.

A

Glycolipids

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14
Q

Characterized by lipid proteins caveolin and flotilin.

A

Lipid rafts

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15
Q

Nonpolar membrane protein

A

Glycine

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16
Q

Nonpolar lipid membrane

A

Alanine

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17
Q

Nonpolar lipid protein

A

Valine

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18
Q

Nonpolar lipid membrane

A

Leucine

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19
Q

Nonpolar membrane protein

A

Isoleucine

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20
Q

Nonpolar lipid protein

A

Methionine

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21
Q

Nonpolar membrane protein

A

Phenylalanine

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22
Q

Nonpolar membrane protein

A

Tryptophan

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23
Q

Nonpolar lipid protein

A

Proline

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24
Q

These proteins are hydrophobic and anchor the protein to into the cell membrane

A

Nonpolar lipid proteins

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25
Q

These proteins are hydrophilic and are located on the outer surface of the cell membrane interacting with the cytosol.

A

Polar lipid proteins

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26
Q

Polar lipid protein

A

Serine

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27
Q

Polar lipid protein

A

Threonine

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28
Q

Polar lipid protein

A

Threonine

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29
Q

Polar lipid protein

A

Tyrosine

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30
Q

Polar lipid protein

A

Tyrosine

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31
Q

Polar lipid protein

A

Asparagine

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32
Q

Polar lipid protein

A

Asparagine

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33
Q

Polar lipid protein

A

Glutamine

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34
Q

Characteristics of integral proteins

A

Folded
Well anchored
Found on the protoplasmic surface
Will leave impressions on the efface of the cell membrane

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35
Q

Arrhythmogenic Right Ventricular Cardiomyopathy

A

Genetic disorder characterized by distorted cell attachments within the desmosomes of cardiac cell muscle. This is typically a gradual unnoticed onset and diagnosed after death.

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36
Q

These cell membrane proteins are amphipathic with hydrophylic areas in an irregular coil and hydrophobic areas in a helix.

A

Integral proteins

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37
Q

Create pores to allow movement of water soluble substances

A

Integral proteins

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38
Q

Characteristics of peripheral proteins

A 
More localized on the inner monolayer
Associated with integral proteins
Electron carriers
Form part of the cytoskeleton
Contribute as second messengers
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39
Q

Three types of lipid movements

A

Rotational
Lateral
Flip flop

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40
Q

Diffusion type that is restricted by association with the cytoskeleton

A

Lateral

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41
Q

This holds the cell membrane in place

A

Cytoskeleton

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42
Q

Main players in the cytoskeleton

A

Actin and Filament

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43
Q

Main players in the cytoskeleton

A

Actin and Filament

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44
Q

RBC protein that facilitates chloride/bicarb exchange

A

Band 3 proteins

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45
Q

RBC protein that provides mechanical support

A

Band 4.1 proteins

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46
Q

RBC protein that acts a stabilizer

A

Spectrin

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47
Q

RBC protein in the cytoskeleton

A

Actin

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48
Q

RBC protein that anchors Band 3 and Band 4.1

A

Ankrin Bridge

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49
Q

Functions of the gylcocalyx

A

Cell protection and insulation
Receptor sites for cell signaling
Cell attachment
Cell immunity

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50
Q

Interacts with the extracellular matrix to form the gylcocalyx

A

Glycolipids
Glycoproteins
Proteoglycans

51
Q

Ig A protects cells

A

It is attracted to glycolipids and glycoproteins and it’s attachment increases the negative charge of the cell.

52
Q

Proteins involved in cell attachment

A

Selectin
Integrin
Cadherin
Immunoglobulin super family

53
Q

Junctions that significantly limit movement but can allow a very small amount of substances through based on size and charge (leaky).

A

Tight junctions

54
Q

Anchoring junctions that are desmosomes or hemidesmosomes

A

Adherent junctions

55
Q

These junctions form between cells, between the cell and the extra cellular matrix and both.

A

Anchorage junctions

56
Q

These attachments can be heterophilic or homophilic

A

Stable cell attachments

57
Q

These junctions are typically homophilic and use intermediate junctions and cadherins to connect cells and the extracellular matrix.

A

Desmosomes

58
Q

Characteristics of desmosomes

A

Visualized as rivets
Cystoskeleton: actin
CAM: cadherin

Note a homophilic desmosome would involve cadherin to cadherin interactions

59
Q

Characteristics of hemidesmosomes

A

Connect the cytoskeleton to the extra cellular matrix
Cytoskeleton: actin
CAM: Integrin

60
Q

Characteristics of adherin junctions

A 
Combination of hemidesmosome and desmosome
Provide morphological diversity
Can be seen as streaks, spots or bands
Cell to cell: cadherin
Cell to extracellular matrix: integrin
61
Q

This protein is not involved in adherin junctions

A

Actin

62
Q

Communication/GAP junction

A

This junction facilitates spontaneous impulses in individual cells so they will act as a unit.

63
Q

Communicating/GAP junxtion

A

These junctions allow cells to share cytoplasmic contents- not organelles, but ions and electrical current.

64
Q

Examples of Communicating/GAP junctions

A

Brain, heart, smooth muscle and highly proliferating cells

65
Q

Type of communicating/GAP junction

A

Intercalated disk- allow the heart cells to behave as a functional syncytium.

66
Q

Composition of intercalated disk

A

Macula adherins- desmosome, fascia adherins and a communicating GAP junction

67
Q

Protein involved in a communicating or GAP junction

A

Connexin

68
Q

Structure of connexins

A

Connexon (Communicating or GAP junction)

69
Q

Example of cells that use connexins to make connections for their communicating or GAP junction

A

Interstitial Cells of Cajal

70
Q

Interstitial Cells of Cajal

A

Highly proliferating cells located in the GI tract

71
Q

These toxins can destroy a tight junction

A

E coli, Staph, C. dif, parasites and hook worms

72
Q

Functions of tight junctions

A

Barrier to each body compartment
Act as a barrier
Regulate the amount of water and solute movement

73
Q

Proteins found in tight junctions

A

Occludens

74
Q

Property is limited by tight junctions

A

Osmosis

75
Q

Cell Adhesion Molecule plentiful on WBC that participate in phagocytosis. Used by both macrophages and monocytes.

A

Selectins

76
Q

Act as ligands, bind to ligands can participate in paracrine autocrine or juxtacrin functions

A

Cell Adhesion Molecules CAM

77
Q

Cell Adhesion Molecules

A

Selectins
Integrins
Cadherins
Immunoglobulin Super Family

78
Q

Organelles

A

Subcellular component with a membrane that resembles the cell membrane in structure and function

79
Q

Vacuoles

A

Structures with membranes that are not lipid bilayer

80
Q

Cytoplasm

A

Electrolytes and solutes that form a colloidal substance, can also be called cell matrix, cytosol or cell ground substance

81
Q

Nucleus

A

Protective container for the cells DNA. DNA never leaves the nucleus but messages (mRNA) can be sent to other parts of the cell.

82
Q

Ribosomes

A

Smallest organelles found in all cells. Build proteins by putting together long chains of amino acids according to mRNA, thousands in each cell.

83
Q

Mitochondria

A

Powerhouse of the cell. Converts glucose to ATP.

84
Q

Cell Membrane

A

Controls what molecules are allowed in and out of the cell. Also known as plasma membrane. Made up of phospholipids that form the outer barrier of the cell.

85
Q

Cytoplasm

A

Cytosol, the liquid that fills cells and contains proteins and dissolved ions that are involved in many cell reactions.

86
Q

Vacuole

A

Membrane enclosed sac that can be filled with anything the cell needs to be kept separate, can store food, water etc.

87
Q

Golgi body

A

Receives products from the endoplasmic reticulum and adds their final modifications. Sorts these products and sends them to their final destinations.

88
Q

Lysosome

A

A membrane enclosed bag of digestive juices. Breaks down large molecules and old cell parts into their components to be recycled to build new cell parts.
Primary lysosome has not used it’s enzymes. A secondary lysosome has used it’s juices and is activated when fusing with a phagosome.

89
Q

Rough Endoplasmic Reticulum

A

Large folded membrane system studded with ribosomes. Ribosomes build proteins and the endoplasmic reticulum helps to fold or modify them. Products are then shipped to the Golgi.

90
Q

Smooth Endoplasmic Reticulum

A

Large folded membrane system that puts together lipids. Is also important for making new membranes.

91
Q

Microtubules

A

Long tubes or cord like structures that provide cells internal structure and allow movement. Other organelles are anchored to the network called the cytoskeleton. Microtubules work together in muscle contraction and the movement of cilia and flagella.
Have a positive end and a negative end.
Negative is toward the center of the cell, positive is toward the cell membrane.
Dynein moves materials outside in and kinesin moves molecules inside out.

92
Q

Endoplasmic Reticulum

A

Reticulated organelle with a large lumen for protein processing (modification and synthesis).

93
Q

Major events in the in the lumen of the ER

A

Protein sorting
Protein trafficking
Protein modification

94
Q

Major events outside of the lumen of the ER

A

Translation

Transcription

95
Q

Steps of protein synthesis in the RER

A

External stimuli acts on a ligand (receptor) and forms the ligand receptor complex. The ligand receptor complex is internalized and will associate with the CREB.

96
Q

CREB Interaction

A

Cyclic AMP will act as a second messenger and activate a dormant kinase along with ATP. CAMP and ADP-P will phosphorylate protein kinase A.
CAMP and phosphorylated protein kinase A will form the Cyclic AMP Response Element Binding (CREB)
CREB will enter the nucleus.

97
Q

Events between CREB entering the nucleus and mRNA leaving the nucleus for the Rough Endoplasmic Reticulum

A

The CREB will locate the structural gene and bind to the response element on said gene. The ligand will leave the CREB unit to be recycled in the cell.
The response element will bind with the CREB to produce transcription factors and RNA polymerase.
RNA polymerase will copy the information in the structural gene and produce mRNA.
mRNA will enter the ribosomes.
Amino Acids are also located in ribosomes.

98
Q

Synthesis of codons (mRNA) and anticodons (tRNA)

A

mRNA and tRNA will combine to pick appropriate amino acids- translation.
Amino acids will be added to the incomplete polypeptide.
The synthesized protein will be inserted into the membrane of the ER for modification in the lumen by a signal recognition receptor on the RER.

99
Q

These unfold the protein in the RER lumen

A

Cytoplasmic chaperones

100
Q

This does not require a signal recognition molecule

A

A free ribosome

101
Q

Signal peptidase

A

Catalyzes the cleaving of the signal recognition particle and dissolves the ribosome

102
Q

Post translational translocation

A

Occurs in free ribosomes

Translation ends before translocation occurs

103
Q

Cotranslational translocation

A

Occurs as the protein is being carried into the lumen of the RER on the attached ribosomes.

104
Q

Protein trafficking

A

Follows the cleaving of the signal recognition particle and is the formation of a transport protein channel

105
Q

Process by which young proteins are stabilized

A

Modification

106
Q

How is modification done?

A

Formation of disulfide bridges and glycosylation

107
Q

Disulfide bridges

A

A linear protein with cysteine is acted on by disulfide isomerase to form a disulfide bonds. This brings molecules closer together and changes the structure of the protein.

108
Q

Oxidation of reduced cystein in the lumen of the RER

A

Oxidation reaction with disulfide isomerase and cystein that lead to the formation of disulfide bridges and change the shape of the protein,

109
Q

Glycosylation

A

Addition of a glycan (sugar) to a newly synthesized protein with enzyme oligosaccharide transferase.

110
Q

N-linked glycosylation

A

The nitrogen in asparagine is added by oligosaccharide transferase in the RER.

111
Q

O-linked glycosylation

A

This is not exclusive to the RER
The hydroxyl group (OH) of serine and threonine are acted on by oligosaccharide transferase in the RER, Golgi, cytosol and nucleus.

112
Q

Glypation

A

The glycan (sugar) is added by oligosaccharide transferase to a phospholipid and a protein.

113
Q

C- linked glycosylation

A

Oligosaccharide transferase binds mannose to the indole ring of tryptophan.
Mannose is a pathogen recognition receptor on a macrophage.

114
Q

Phosphoglycosylation

A

Glycan is added to serine through a phosphodiester bond by oligosaccharide transferase.

115
Q

Events that stabilize a protein in order to send it to the Golgi Apparatus

A

Protein is stabilized in the RER disulfide isomerase forming disulfide bridges with cystein and oligosaccharide transferase adding sugars through glycosylation.

116
Q

Golgi apparatus

A

Structure within the cell that finishes protein processing and releases the finished product.

117
Q

Antegrade transport

A

Perfect protein is escorted to the entry face of the Gogli apparatus for further processing by COP II (coatomer protein)

118
Q

Retrograde transport

A

A protein with a defect is escorted from the entry face of the Gogli apparatus back to the RER with chaperone protein COP I (Coatomer protein I)

119
Q

Structure of the Gogli Apparatus

A

Entry face
Middle: transgolgi stalk and medial stalk
Exit face which releases secretory vesicles

120
Q

Exocytosis

A

How secretory vesicles with differing protein concentrations will leave the Golgi apparatus.

121
Q

Constitutive exocytosis

A

Exocytosis at the Golgi apparatus where secretory vesicles of differing proteins are release without a stimulus.

122
Q

Regulatory exocytosis

A

Exocytosis at the Golgi apparatus that requires a stimulus for the release of secretory vesicles of differing protein concentrations.

123
Q

Membrane redistribution

A

Occurs when proteins are released from the Golgi apparatus via constitutive or regulatory exocytosis to be incorporated back into the cell.
These proteins can be incorporated back into the cell, cell membrane or various organelles.

Physiology Dr. Aka's class (2 decks)

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