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Histology > Intro to Cytology HANDOUT > Flashcards

Intro to Cytology HANDOUT Flashcards

1
Q

Describe eukaryotic cells organelles and particles

A

contain a number of membranes that form barriers between the cell and external enironment (pm) and also subdivide the cell into compartments

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2
Q

what are organelles

A

membrane bound compartments within the cell

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3
Q

what do membranes allow

A

each type of organelle to maintain novel ionic and enzymatic interior environments, which are different from the surrounding cytoplasm.

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4
Q

what are membranes composed of

A

lipids, proteins, carbs

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5
Q

membranes and visualization

A

cannot be visualised in a light microscope bc they are too thing (7nm) and do not stain with standard histological dyes (H&E), but can be seen in an electron microscope when stained with osmium tetroxide

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6
Q

Membrane lipid types

A

phospholipids, cholesterol, glycolipids

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7
Q

polarity of membrane lipids

A

ampipathic - they have uncharged hydrophobic (dont like water) tails and polar hydrophilic heads .

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8
Q

what does the ampipathic nature of membrane lipids cause

A

them to spontaeously form a lipid bilayer with the hydrophobic tails facing each other and the hydrophilic heads facing towards the aqueous environment

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9
Q

what is the key to the organization of the membrane

A

the presence of the hydrophobic center, which acts as an anchor to membrane proteins that can move within the lipid bilayer - FLUID MOSAIC MODEL

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10
Q

Permeability of the membrane

A

highly permeable for small, uncharged molecules that cross the membrane by simple diffusion. All other molecules such as ions and large molecules require membrane transport proteins to provide them with passage across the membrane.

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11
Q

how can membrane proteins be classified

A

based on their structure and based on their function

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12
Q

how do you divide structurally membrane proteins

A

integral and peripheral

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13
Q

describe integral membrane proteins

A

they have a hydrophobic region which is embedded into the hydrophobic core of the membrane.

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14
Q

what are transmembrane proteins

A

integral membrane proteins that extend all the way through the membrane

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15
Q

describe peripheral membrane proteins

A

they are not embedded within the lipid bilayer and attach either to integral proteins or to the hydrophilic heads of the membrane lipids.

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16
Q

How can membrane proteins be divided functionally

A

into transport proteins, receptors, and structural proteins

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17
Q

transport proteins description

A

the lipid bilayer forms a barrier which is impassible for charged and polar molecules. Transport proteins selectively allow such molecules to cross the membranes. There are several classes of transport proteins: Channel, carrier, pumps

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18
Q

channel proteins

A

form “pores”, which allow passage of small molecules across the membrane via passive diffusion. Channels are ion-selective.

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19
Q

Carrier proteins

A

drag other molecules through the membrane by hiding them in a cleft in the protein

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20
Q

Pumps

A

use ATP energy to pump ions actively though the membrane

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21
Q

Receptors

A

Some transmembrane proteins bind to specific molecules in the extracellular matrix. This specific binding can result in a conformational change in the transmembrane protein that can serve as a signal that allows the cell to adapt to its evironment

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22
Q

Structural or anchoring proteins serve to

A

attach cell to its surroundings. They use their cytoplasmic domains to link to the elements of the cytoskeleton, and their extracellular domains to link to the extracellular proteins

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23
Q

Carbohydrates description

A

mostly oligosaccharides, are often attached to the extracellular domains of membrane proteins and lipids to form glycoproteins and glycolipids.

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24
Q

What is the glycocalyx

A

a fuzzy coating on the external surface of a cell due to the large amount of carbohydrates attached to proteins and lipids. This can be seen on an electron microscope

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25
Q

What are particles and inclusions for

A

synthesis and storage.

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26
Q

2 main types of particles and inclusions

A

ribosomes and glycogen particles

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27
Q

What are ribosomes

A

RNA/protein particles that catalyze protein synthesis. They bring together mRNA and tRNA to synthesis a polypeptide

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28
Q

Structure of ribosomes

A

15-25nm in size and consist of a small subunit and a large subunit. Each subunit consists of one or more ribosomal RNA (rRNA) and many specialized proteins

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29
Q

How do ribosomes in eukaryotic cells exist

A

either as free ribosomes, mitochondrial ribosomes, or ribosomes bound to rough ER

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30
Q

Where are the majority of cellular proteins synthesized

A

on free ribosomes, except those in the Golgi apparatus, lysozomes, secretory granules, and plasma membrane, which are synthesized on RER ribosomes

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31
Q

how much of mitochondrial proteins are synthesized on mitochondrial ribosomes

A

20%. The rest are on free ribosomes int he cytoplasm

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32
Q

Describe Polysomes

A

During protein synthesis, many ribosomes attach to a single mRNA molecule. This string of ribosomes connected to mRNA is known as a polysome.

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33
Q

Glycogen particles

A

a storage form of polysaccharides

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34
Q

Endoplasmic Reticulum consists of

A

series of membrane-formed anastomosing tubules and cisternae

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35
Q

what is cisternae

A

flattened, pancake like vesicles

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36
Q

what is the ER subdivided into

A

smooth and rough ER

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37
Q

what part of the ER has a large amount of ribosomes bound to it

A

the cytoplasmic side of the rough ER

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38
Q

Smooth ER description

A

does not have ribosomes bound to its surface and it also has a more tubular appearance than the rough ER.

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39
Q

functions of the SER

A
  1. Lipid and steroid metabolism. - Phospholipids for all cells membranes are produced here so the SER is involved in membrane synthesis and recycling.
  2. Detoxifcation of noxious substances
  3. Glycogen metabolism
  4. Storage and transport of Ca2+ (in muscle tissue SER)
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40
Q

where does SER become prominent

A

in steroid secreting cells

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41
Q

where is SER very well developed

A

in liver cells and contains enzymes that can modify and detoxify such toxins like carcinogens, pesticides, etc.

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42
Q

SER in muscle tissue is called

A

sarcoplasmic reticulum - here is is involved in storage and transport of Ca2+, which regulates the contractions of muscle cell.

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43
Q

Rough ER description

A

has ribosomes bound to its surface, which creates its rough look.

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44
Q

What is RER mainly formed of

A

cisternae

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45
Q

Where is RER prominent

A

in cells specialized for protein secretion, so it is the principle site of synthesis of proteins destined for export out of the cell. Proteins found in the GA, lysosomes, and the PM are also synthesized in the RER

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46
Q

Golgi Apparatus consists of

A

series of stacked, flattened, membrane limited cisternae and tubular extensions.

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47
Q

What does GA receive

A

proteins synthesized in the RER

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48
Q

describe the stack of GA cisternae

A

polarized.

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49
Q

sides of the GA

A

the side receiving vesicles from the RER is cis Golgi. The middle cisternae form the medial Golgi and the cisternae from which the mature proteins are transported form the trans Golgi

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50
Q

how does the GA function

A

in the post translational modification, sorting, ang packaging of proteins

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51
Q

Describe the modification of protein process in the GA

A

(such as adding or removing sugar residues, sulfate or phosphate groups). The early stages of this process occur in the cis Golgi, intermediate steps occur in the medial Golgi, and the final modifications are made in the trans Golgi

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52
Q

Sorting and packaging of proteins into transport vesicles in the Golgi location

A

mainly in the trans Golgi network. From here, there are 3 main destinations for the proteins

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53
Q

what happens after proteins leave the Golgi

A

most leave with specific signal sequences, which direct them to their destination

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54
Q

Secretory vesicles description

A

where many cells (pancreatic acinar cells) store proteins and other products.

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55
Q

maturation process of secretory vesicles

A

the secretory proteins are retained within the vesicle. Mature secretory vesicles eventually fuse with the plasma membrane to release the secretory product into the extracellular space in response to a certain signal.

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56
Q

Lysosomes description

A

spherical organelles of variable size produced by the Golgi. They are often involved in digesting the material taken up from outside the cell and in degradation of senescent organelles.

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57
Q

How are lysosomes characterized

A

by low pH and presence of hydrolytic enzymes.

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58
Q

Principle sorting signal which directs proteins from the trans Golgi network to the lysosome

A

mannose-6-phosphate

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59
Q

what happens if one of the enzymes that creates mannose 6 phosphate is mutated

A

it causes the lysosomal protein to be secreted into the intercellular space -> resulting in I-cell disease (mucolipidosis), which is one of the lysosomal storage diseases.

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60
Q

How can lysosomes be classified

A
  1. Primary lysosomes
  2. Secondary lysosomes
  3. Lipofuscin granules
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61
Q

Primary lysosomes

A

lysosomes which have not yet received substrates for digestion

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62
Q

Secondary Lysosomes

A

results from the fusion of primary lysos with their target

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63
Q

Lipofuscin grranules

A

or residual bodies are senescent lysosomes with undigestible material

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64
Q

Constitutive pathway

A

Proteins in the trans Golgi, which are not destined for either lysosomes or secretory granules are sorted into small vesicles, which are transported directly to the pm, where the vesicle fuses with the pm. Integral membrane proteins and proteins that are secreted continuously into the extracellular space (collagen) reach the plasma membrane by this route.

65
Q

Peroxisomes description

A

small (0.5um) membrane bound organelles containing oxidative enzymes, particularly catalase.

66
Q

what are peroxisomes used for

A

to oxidize a wide range of organic substances including very long chain fatty acids and to converse ethanol to acetaldehyde

67
Q

what do oxidative enzymes produce and why

A

produce hydrogen peroxide, which is a toxic substance.

68
Q

what does abnormal functioning of peroxisomes cause

A

severe disorders

69
Q

Zellweger Syndrome

A

a congenital disease which is caused by mutations in the proteins that are responsible for the proper transport of peroxisomal enzymes from the cytoplasm, where they are synthesized on free ribosomes, to peroxisomes. This affects brain development through the improper formation of the myelin sheath. There is no cure or a standard course of treatment and patients usually die before 6 months of age.

70
Q

Adrenoleukodystrophy

A

Caused by oxidation of very long chain fatty acids. It is inherited X-linked disorder that results in progressive brain damage, failure of he adrenal glands, and eventually death. The symptoms are caused by the accumulation of lipids in the brain and adrenals.

71
Q

What are mitochondria involve din

A

the production of ATP through the oxidation of pyruvate and fatty acids.

72
Q

where are mitochondria present

A

virtually all cells (except RBC and terminal keratinocytes), but are most numerous in cells that use large amounts of energy.

73
Q

What can mitochondria do that is unique

A

they can change their location and shape and can be compared with mobile power generators as they migrate from one area of the cell to another to supply the energy where needed.

74
Q

Mitochondria evolution

A

believed to have evolved from aerobic bacteria (symbiotic prok) that were engulfed by eukaryotic cells and differ from the organelles discussed above in several ways.

  1. mitochondria contain their own separate genome
  2. possess 2 membranes
  3. increase their number by division
75
Q

Mitochondria sizes and shapes

A

vary (1-5um). Including spheres, rods, elongated filaments, and even spirals. But all have 2 membranes with an intermembrane space between them.

76
Q

What is the space enclosed within the inner membrane of the mitochondria

A

the mitochondrial matrix

77
Q

Outer mitochondrial membrane

A

contacts the cytoplasm on the outer side and the intermembrane space on the inner side. It contains numerous pores (anion channels) which allow passage of small molecules (up to 5000 daltons), ions, and metabolites

78
Q

Inner mitochondrial membrane

A

thinner than the outer membrane and highly folded into the cristae. The inner membrane contains many of the enzymes involved in energy production

79
Q

describe cristae in mitochondri

A

project into the matrix and greatly increase the inner membrane surface

80
Q

Cristae in steroid producing cells

A

may have tubulovesicular appearance.

81
Q

pH and ionic composition of the intermembrane space

A

similar to the cytoplasm

82
Q

protein composition of intermembrane space

A

is unique in containing enzymes that use ATP generated in the inner membrane.

83
Q

Cytochrome C

A

located in intermembrane space. Important factor in initiating apoptosis.

84
Q

what are mitochondria sensors of

A

cell health and if the cell is no viable mitochondria release Cytochrome C, which triggers the intrinsic pathway of programmed cell death.

85
Q

describe the matrix of the mitochondria

A

enclosed within the inner mitochondrial membrane and contains soluble enzymes including those for the Krebs Cycle, DNA transcription, etc.

86
Q

What does the mitochondrial matrix contain

A

mitochondrial DNA, mito ribosomes, rRNA, mRNA, tRNA, and electron dense granules

87
Q

electron dense granules do what

A

store Ca2+ so mitochondria can also regulate concentration of certain ions in the cytoplasm

88
Q

SER and mitochondrial shared role is

A

regulation of certain ions in the cytoplasm

89
Q

how much of the proteins involved in oxidative phosphorylation are encoded by mitochondrial DNA

A

1/5

90
Q

What are mutations in both nuclear and mitochondrial genes caused by

A

the so called mitochondrial myopathis

91
Q

mitochondrial myopathies are

A

Diseases that involve the mitochondrial DNA. They show maternal inheritance since only the oocyte contributes mitochondria to the embryo.

92
Q

Presentation of mitochondrial disesases

A

present in young adulthood and manifest with proximal muscle weakness, sometimes affecting the extraocular muscles involved in eye movements. The weakness may be accompanied by other neurological symptoms, lactic acidosis, and cardiomyopathy.

93
Q

Nucleus description

A

a large (5-10um) membrane limited organelle that contains the genome in euk cells in the form of DNA bound to proteins, which is known as chromatin. The nucleus also contains machinery for DNA replication and RNA transcription and processing and one or more nucleoli.

94
Q

what is the nucleus surrounded by

A

double membrane called the nuclear envelope

95
Q

nuclear envelope

A

consists of 2 membranes (inner and outer), perinuclear space between them, nuclear lamina, and nuclear pores

96
Q

outer nuclear membrane

A

closely resembles the membrane of the RER and is continuous with the latter. Ribosomes are commonly attached to the cytoplasmic surface of the outer nuclear membrane in a manner identical to the rest of the RER

97
Q

Perinuclear space

A

continuous with the lumen of the RER

98
Q

Inner nuclear membran

A

distinct from the endoplasmic reticulum in its ability to bind chromatins and lamins. It is supported by a rigid network of intermediate filaments.

99
Q

Nuclear lamina

A

thin, protein dense layer attached to the inner nuclear membrane, which represents the skeleton of the nucleus formed by specialized intermediate filament proteins called lamins

100
Q

how are lamins distinct from other intermediate filaments

A

they disassemble during mitosis and reassemble when mitosis ends. Lamin filaments are cross linked into orthogonal lattice, which is attached to the inner nuclear membrane.

101
Q

Nuclear pores

A

70-80nm openings through the envelope, which allow communication between the cytopolasm and the nucleus. The pores have a rather complex structure with protein spokes projecting into the lumen of the pore to the central plug. The pores allow free passage for small (9nm or less) particles.

102
Q

How do larger particles (proteins, RNA protein complexes) get out of the nucleus

A

must be actively transported out

103
Q

Chromatin contains

A

DNA associated with roughly an equal mass of various nuclear proteins such as histones.

104
Q

chromatin in the nucleus of a non-dividing cell

A

2 types. More densely packed heterochromatin and less densely packed euchromatin

105
Q

Euchromatin

A

contains transcriptionally active DNA, which is more loosely packed as a result appears to be lightly stained in both light and electron microscope.

106
Q

what does euchromatin indicate

A

active chromatin, or the chromatin that is stretched out so that the DNA can be read and transcribed

107
Q

where is euchromatin prominent

A

in metabolically active cells such as neurons

108
Q

Heterochromatin predominates in

A

metabolically inactive cells

109
Q

heterochromatin contains

A

transcriptionally inactive DNA, which is densely packed. As a result, heterochromatin stains more intensely than euchromatin.

110
Q

Nucleolus

A

small area within the nucleus in which ribosomal RNA is processed and assembled into ribosomal subunits.

111
Q

what does the nucleolus contain

A

3 morphologically distinct regions when vied with TEM: Fibrillar centers, dense fibrillar component, and granular component

112
Q

Fibrillar centers

A

contain DNA loops with rRNA genes and transcription factors

113
Q

Dense fibrillar component

A

(pars fibrosa) contains ribosomal genes that are being translated and large amounts of RNA

114
Q

granular component

A

(pars granulosa) is the site for ribosome assembly and is made of densely packed clusters of pre-ribosomal particles

115
Q

Cytoskeleton determines

A

the shape of cells, provides structural support for its organelles and plays a major role in cell motility (included mitosis and cytokinesis).

116
Q

Cytoskeleton composition

A

consists of 2 major types of filaments: actin filaments, microtubules, and intermediate filaments

117
Q

Actin cytoskeleton role

A

cell movement, cell shape, and organelle transport

118
Q

forms of actin

A

G-actin and F-acting

119
Q

G-actin

A

soluble monomeric globular protein. It can polymerize into a double stranded helical filament which is called F-actin.

120
Q

polymerization of G-action

A

to make F-action. Occurs from head to tail so the actin filaments have polarity.

121
Q

other name for F-actin filaments

A

thin filaments

122
Q

functions of thin filaments

A
  1. Actin thin filaments form a thin sheath beneath the cytoplasm called the cortex. Cross lined actin filaments resist cell deformation, transmit forces, and restrict the movement of organelles
  2. Interacts with myosin to generate force and movement
123
Q

cortex

A

Cross lined actin filaments resist cell deformation, transmit forces, and restrict the movement of organelles. The cortex also reinforces the plasma membrane and restricts lateral motion of some integral membrane proteins

124
Q

myosin is the

A

motor associated with thin filaments.

125
Q

Microtubules

A

cytoskeletal elements present in all cells except erythrocytes

126
Q

Functions of microtubules

A
  1. organelle and vesicle movement (sometimes over rather long distances like across the axon of a neuron)
  2. Formation of the mitotic spindle and chromosome movement during mitosis and meiosis
  3. beating of cilia and flagella
127
Q

Structure of microtubules

A

They are stiff, non branching, cylindrical polymers made of 1 polymerized globular proteins (alpha and beta tubulin)

128
Q

how are tubulin molecules polymerized

A

side to side and head to tail so microtubules have a plus and minus end.

129
Q

Plus and v minus end of microtubule

A

Plus grows faster. Plus is cell periphery and minus associated with the microtubule-organizing center/centriole.

130
Q

motor proteins associated with microtubules

A

2 types - Dyneins and Kinesins

131
Q

energy used in Dynein and Kinesin

A

ATP energy to generate force that moves the motor and materials attached to it along the microtubule.

132
Q

Dyneins description

A

group of motor proteins that move towards the minus end of a microtubules. They are involved in the beating of cilia and flagella.

133
Q

Kinesins description

A

group of motor proteins that move towards the plus end of a microtubule

134
Q

Higher order structures

A

Microtubules in euk cells are organized into several higher order structures, including cilia, flagella, centrioles, and microtubules-organizing centers

135
Q

Axoneme

A

forms the core of cilia and flagella. Composed if 9 doublets and a central pair of microtubules. Dynein arms attached to the A-tubules of each of the doublets interacts with the neighboring B-tubules of the next doublet and by walking along it cases the bending of the axoneme. The axoneme generates force for the movement of cilia and flagella

136
Q

what is at the base of each cilium or flagellum

A

centriole, or a basal body, also composed of microtubules arranged into 9 triplets without the central pair

137
Q

most human cells except neurons and RBCs contain

A

a microtubule-organizing center (MTOC)

138
Q

MTOC consists of

A

2 centrioles. Virtually all cellular microtubules arise from the MTOC

139
Q

Intermediate filaments description

A

they are intermediate in thickness between actin filaments and microtubules. They are strong, but flexible polymers that provide mechanical support for cells. Intermediate filaments do NOT have polarity and there are no motor proteins associated with them

140
Q

classes of intermediate filaments

A

several major classes that have certain distribution in different types of tissues.

  1. Lamins
  2. Keratins
  3. Vimentin
  4. Desmin
  5. Glial fibrillary acidic protein
  6. Neurofilaments
141
Q

Lamins location and function

A

form a meshwork of filaments on the inner side of the nuclear envelope, where they form the nuclear lamina and provide structural support for the nucleus

142
Q

Keratins location

A

principally in epithelial cells

143
Q

Vimentin primary location

A

fibroblasts of the connective tissue

144
Q

Desmin location

A

muscle cells

145
Q

GFAP location

A

in the support cells of the nervous system, called glial cells

146
Q

neurofilaments location

A

neurons

147
Q

what do cytoplasmic intermediate filaments form

A

bundles between the pm and the nucleus. They spread tensile forces, maintain cell architecture and act as a cocoon when the cell is damaged. Intermediate filaments anchor ion channel proteins.

148
Q

Colors of most tissues

A

colorless - this is why we need dye

149
Q

components of most dyes used

A

basophilic and acidophilic components

150
Q

most commonly used combo of dyes

A

Hematoxylin and eosin (H&E).

151
Q

Hematoxylin

A

a basic dye as it stains structures, which have acids in their composition, such as nucleic acids or glucosaminoglycans blue.

152
Q

Eosin

A

acid dye - it stains basic cell components.

153
Q

Nucleus staining with H&E dye

A

Dark blue/purple

154
Q

Cytoplasm staining with H&E dye

A

Pink

155
Q

Mitochondria staining with H&E dye

A

Pink

156
Q

RER/Ribosomes staining with H&E dye

A

Blue

157
Q

Membranes, GA, SER staining with H&E dye

A

Do not stain

158
Q

Collagen staining with H&E dye

A

Pink

159
Q

Glucosaminoglycans staining with H&E dye

A

Blue

Histology (3 decks)

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