Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Module 2 > Module 2 > Flashcards

Module 2 Flashcards

1
Q

What is the function of basophils?

A

Inflammatory/ allergic reactions, supplement mast cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the functions of eosinophils?

A

Inflammatory and allergic reactions, phagocytosis of antibody/ antigen complexes and fight parasites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are the function of monocytes?

A

Develop to macrophages when recruits to tissue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

2 types of lymphocytes?

A

T and B cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Name 3 peripheral RBC proteins?

A

Spectrin
Ankyrin
Actin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Name 2 integral RBC proteins and their functions?

A

Glycoproteins A- prevents sticking

Glut 1- Glucose transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the universal blood group for dogs?

A

DEA 4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What process determines blood group?

A

Glycosylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Are RBC processes aerobic or anaerobic?

A

Anaerobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the final product of glycolysis?

A

Pyruvate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How many ATP molecules does glycolysis produce?

A

NET 2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the negative allosteric inhibitor of Hb oxygen affinity?

A

2,3 BiPGlycerate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is the main step in the pentode phosphate pathway?

A

Oxidation of Glu-6-P by NADP+ to form pentose phosphates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the functions of pentose phosphates?

A

Nucleotides or converted to glycolysis intermediates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What problems does methemoglobin (HbFe3+) cause?

A

No oxygen transport
Precipitates in RBC–> Heinz bodies
ROS per oxidation of lipid membranes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is the function of a neutrophil?

A

Defence, phagocytosis, increase permeability of vessel walls

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Metabolic causes of methemogloinemia

A

High oxygen and metal ions in RBC

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Risk factors for methemogloinemia

A

Paracetamol (cats)
Onion, garlic (dogs)
Rye grass, nitrate fertilisers (cattle)
Maple leaf (horses)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What are the clinical signs of methemogloinemia?

A 
Cyanosis (purple)
Exercise intolerance
Vomiting 
Chocolate brown blood
Anameia
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What can reduce metHb back to Hb?

A

GSH (reduced glutathione)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What molecules make up heme group?

A

C,H,O,N and Fe atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Hb structure?

A

Protein and heme group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

How many binding sites does the Fe atom have and to what does it bind?

A

4 N rings and 2 oxygen molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Where is myoglobin stored?

A

Skeletal muscles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

How many oxygen molecules can Hb Bind to?

A

4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

How many molecule of oxygen can myoglobin bind?

A

1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What is an allosteric protein?

A

One that changes shape/ ligand affinity when bound by small molecules and oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Name an allosteric protein?

A

Haemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Does deoxy Hb or oxy Hb have higher affinity for oxygen?

A

Oxy Hb

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What has higher affinity for oxygen: myoglobin or Haemoglobin?

A

Myoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What is the effect of CO2 as an allosteric effector of oxygen binding to Hb?

A

Decrease Hb affinity for oxygen leading to release of oxygen and dissociation curve to right

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

A defect in which gene causes sickle cell anaemia?

A

Beta globin gene

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

In which condition does HbS precipitate inside RBCs and become stuck leading to the lysis of vessels?

A

Sickle cell anaemia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

How many base substitutions cause HbS?

A

1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

What is one advantage of HbS?

A

Resistance to malaria

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

What is the principal metabolic cause of jaundice?

A

High levels of free bilirubin in plasma

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

When is bilirubin produced?

A

During heme degradation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

How is bilirubin usually removed?

A

Binds to album and transported to liver then converted to bilirubin diglucoronide and excreted as bile

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

What does jaundice suggest?

A

Excessive RBC breakdown
Decreased albumin
Impaired liver fxn
Obstruction of bile duct

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Name main types of blood cells

A

Erythrocytes, Lymphocytes and Platelets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Function of erythrocytes?

A

Transport oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

Function of lymphocytes?

A

Protect against infection

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

Function of platelets?

A

Clotting

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

What proteins does plasma contain?

A

Albumin,
Immunoglobulins,
Metal ion binding proteins
Hormone binding proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

What are the three metal ion binding proteins?

A

Albumin, Transferrin and Ceruloplasmin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

What does ceruloplasmin transport?

A

Copper

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

What does albumin transport and what nature are these molecules?

A

fatty acids and sterols (hydrophobic), drugs (hydrophobic), bilirubin (hydrophobic & toxic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Which substance is an osmotic regulator, can be broken down to AA’s during malnutrition and decreases during kidney disease and parasitic infections?

A

Albumin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

What bond is present between the carboxylic group and amino group of an amino acid?

A

peptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Name the 6 hydrophobic AA’S?

A 
Glycine (G) (most simple)
Alanine (A)
Valine (V)
Leucine (L)
Phenylalanine (F) -aromatic
Tryptophan (W)- aromatic
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Hydrophilic, charged and polar AAs?

A 
Asparatate (D)
Glutamate (E)
Lysine (K)
Arginine (R)
Histidine (H)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

Hydrophilic, uncharged and polar AAs?

A 
Asparagine (N)
Glutamine (Q)
Serine (S)
Threonine (T)
Cysteine (C)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Bonding in primary protein structure?

A

peptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Bonding in secondary protein structure?

A

hydrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

Features of alpha helixes?

A

H bonding between CO and NH 4 residues away

3.6 amino acids per turn of helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

Features of beta sheets?

A

H bonding between CO and NH on different polypeptide strands

Strands can run in the same direction (parallel sheets) or different directions (anti-parallel sheets)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

Tertiary protein structure?

A

Weak, non covalent interactions
Responsible for folding
Disulphide binding between cysteine residues- stong

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

What are terameric proteins?

A

2 or more separate polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

Define a conservative substitution?

A

Codon still codes for same AA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

Define a radical substition and give an example?

A

Codon codes for different AA

E.g Sickle cell anameia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

Describe the structure of collagen?

A

Collagen is made of a collagen triple helix
3 collagen fibres intertwined, 3 AA per turn
Every third amino acid is Gly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

What bonds stabilise the structure of collagen?

A

Hydrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

Describe scurvy.

A

Vitamin C deficiency–> less hydroxylation of proline –> fewere H bonds –>collagen unstable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

Describe the features of globular proteins?

A

a lot of alpha helices
a lot of 3Y structure with lots of R group interactions,
non-structural proteins
ligand binding sites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

Describe the features of fibrous proteins?

A

2Y structures
H bonding,
structural proteins

66
Q

Describe the basis of prion diseases?

A

globular to fibrous and less folding
create lesions in the brain
Increase hydrogen bonding and beta sheet content

67
Q

Give an example of a prion disease?

A

Scrapie in sheep

68
Q

What do positive allosteric regulators do?

A

Increase ligand affinity

69
Q

What does qualitative mean?

A

Difference in AA sequence

70
Q

What do enzymes do?

A

Lower activation energy

71
Q

What is Km?

A

concentration of substrate at which ½ of enzyme’s active sites are saturated

72
Q

What is an allosteric enzyme?

A

Binds at different location, does not obey Michaelis mentin kinetics

73
Q

Where are RBCS produced in the foetus?

A

Bone marrow, liver, spleen

74
Q

What components does Erythropoiesis require?

A

AAs
Lipids
Carbs
Iron

75
Q

When does erythropoitein production increase and where does this take place?

A

0xygen deprivation

The kidneys

76
Q

How are erythrocytes removed from the blood stream?

A

Intravascular and extravascular lysis

77
Q

What is intravascular lysis?

A

Aged cells lyse within blood vessels, Hb binds to plasma protein haptoglobulin, complex is engulfed by cells of mononuclear phagocytic or macrophage system (MPS) and eventually recycled into new erythrocytes

78
Q

What is extravascular lysis?

A

Cellular fragments and ageing erythrocytes directly engulfed by cells of MPS

79
Q

What are the 3 responses involved in haemostasis?

A

Vascular constriction of smooth muscle, platelet plug formation and coagulation

80
Q

What 2 processes activate platelets?

A

Interaction with collagen and coversion or arachadonic acid to thromboxine A

81
Q

What factor is involved in platelet plug formation?

A

Von wilderband

82
Q

How is the final clot formed?

A

Thrombin converts fibrinogen to loose fibrin

83
Q

What breaks down fibrin?

A

Plasmin

84
Q

What are the accute clinical features of anaemia?

A

Accute:

Pallor, tachycardia, muscular weakness, subnormal temperature, coma, death

85
Q

What are the chronic clinical features of anaemia?

A

Fatigue/lethargy, exercise intolerance, tachycardia, fainting, pallor, cardiac murmur

86
Q

The presence of which cell in a blood sample is the main indicator of anaemia?

A

Reticulocytes

87
Q

What does haemolytic mean?

A

destruction of rbcs

88
Q

What is haemorrhagic anaemia?

A

excessive blood loss

89
Q

Describe the red cell morphology of haemorrhagic anaemia?

A

Normal in first few days/pre-regenerative
Anisocytosis: red blood cells are different sizes
Howell-Jolly bodies
nucleus extruded from cell and remnant of it can be found on exterior on cell
Macrocytic hypochromic RBCs (larger RBCs but less iron indicating less RBCs or [Hb])

90
Q

Describe the pathophysiology of hameorrhagic anaemia?

A

Polychromasia: abnormally high number of RBCs in blood stream due to prematurely released RBCs from bone marrow
Thromocytosis: high platelet counts
Neutrophilia: high number of neutrophils

91
Q

Which type of anemia: haemolytic or hameorrhagic, is most regenerative and why?

A

Hamemolytic: no lack of components

92
Q

Pathophysiology in haemolytic anaemia caused by intravascular lysis?

A

Hemoglobinemia – Free Hb in serum
Toxic nephrosis caused by saturation of haptoglobins Hb bound haptoglobins travel to kidneys, this results in haemoglobinuria (Hb in urine)

93
Q

Pathophysiology in haemolytic anaemia caused by extravascular lysis?

A

Phagocytosis of red cells and breakdown of heme into biliverdin→bilirubin→bilirubin+albumin→bilirubin+glucuronide→bile
Iron from destroyed erythrocytes recycled
Reduced red blood cell survival time

94
Q

Infectious causes of haemolytic anaemia

A

Mycoplasma (cell membrane)

Babesiosis (inside cell)

95
Q

RBC morphology (haemolytic anaemia)?

A

Heinz bodies

96
Q

Pathophysiology of haemolytic anaemia?

A

Reduced glutahione caused by chemicals—> hb converted to metHb and side product ROS—> ROS damaged RBC’s engulfed by macrophages and filtered by spleen = anaemia

97
Q

Common causes of haemolytic anaemia?

A

copper poisoning, paracetamol, garlic/onions, zinc, rape and kale, red maple, snake venoms

98
Q

What is the cause and main sign of fragmentation haemolytic anaemia?

A

Trauma to RBCs

Presence of schistocytes (fragments) and ancathocytes (spiked membrane RBCs) in blood

99
Q

How are schistocytes formed (small vessel disorder)?

A

Cut by fibrin mesh formed by increased coagulation

100
Q

What are the causes of immune mediated HAEMOLYTIC anaemia?

A

Blood transfusions
Neonatal isoerythrolysis
Autoimmune (Primary)
Secondary - tigger eg. drug, vaccin etc

101
Q

How does neonatal isoerythrolyis occur?

A

Maternal antibodies absorbed from colostrum and destroy neonates RBCs through phagocytosis
Mother must have different blood type but be previously sensitized to neonates blood group

102
Q

Describe canine autoimmune haemolytic anaemia.

A

Antibodies IgM or IgG produced against own RBCs

103
Q

Describe the role of IgG in canine autoimmune haemolytic anaemia and its test?

A

IgG coats RBC’S and then phagocytose in spleen
This leads to splenmegaly (enlarged spleen)
Coombs test

104
Q

Describe the role of IgG in canine autoimmune haemolytic anaemia and its test?

A

IgG causes auto agglutination (RBCS gather around IgM)

Slide agglutination test

105
Q

Define non regenerative anaemia?

A

Failure to produce RBCs in BM

106
Q

Causes of non regen anaemia?

A

Iron deficiency
Renal disease -erythropoietin
Inflammation- iron deficiency
Hypoplastic/ Aplastic anaemia- Bone marrow defunction

107
Q

What is aplastic anaemia?

A

Cellularity of bone marrow is reduced involving multiple cell lines

108
Q

What is pure red cell aplasia?

A

Cellularity of bone marrow is reduced, only RBCs affected

109
Q

Histological progression of aplastic anaemia?

A

Neutropenia
Thrombocytopenia
Anaemia

110
Q

Name 3 causes of red cell aplasia?

A

Vaccine
Pre- leukaemia
Infectious

111
Q

What is Polycythaemia (erythrocytosis)?

A

Abnormally increased red cell mass therefore higher [RBC], HCT/PCV and Hb content

112
Q

Causes of relative polycythaemia?

A

Decreased plasma

Contraction of spleen when excited

113
Q

Causes of secondary absolute polycythaemia?

A

Increased EPO
Appropriate- inceased hypoxia
Inappropriate- renal problems

114
Q

Clinical signs of polycythaemia?

A

Relative- Dehydration

Absolute- neurological, weakness, cyanosis

115
Q

Five freedoms?

A
  1. Freedom from Hunger and Thirst
  2. Freedom from Discomfort
  3. Freedom from Pain, Injury or Disease
  4. Freedom to Express Normal Behaviour
  5. Freedom from Fear and Distress
116
Q

What is “bulk flow”?

A

Movement of water and solutes together due to pressure gradient

117
Q

Describe the donnan effect and recognise its importance

A

presence of non-permeable solute affects the distribution of permeable solutes

118
Q

Define osmolarity

A

Number of solute particles per litre of solution

119
Q

Percentage body water (adult)

A

55- 60 percent

120
Q

Proportions of body water in ICF and ECF

A 
ICF= 2/3
ECF= 1/3
121
Q

What are the 4 “Starling’s forces”?

A

capillary hydrostatic pressure,
interstitial hydrostatic pressure,
osmotic pressure due to interstitial fluid proteins
oncotic pressure due to proteins

122
Q

Function of capillary hydrostatic pressure?

A

Moves water from capillary to interstitial fluid

123
Q

Function of interstitial hydrostatic pressure?

A

moves water from interstitial fluid to capillaries

124
Q

Function of osmotic pressure?

A

Moves water from capillaries to interstitial fluid

125
Q

Function of oncotic pressure?

A

Moves water from interstitial fluid to capillaries

126
Q

Where does net filtration occur?

A

Arterial end of capillary

127
Q

Where does net absorption occur?

A

Venous end of capillary

128
Q

An example of pure water loss?

A

Dehydration (lost from both ECF and ICF)

129
Q

An example of isotonic water loss?

A

Reduced plasma- only lost from ECF

130
Q

Describe crystalloid fluid replacement?

A

Water with sodium/ glucose base
Replaces electrolytes, alters pH of ECF, substitutes drinking
Diffuses rapidly

131
Q

3 examples of crytalloid solns?

A

Replacement fluids
Maintenance fluids
Hypertonic saline

132
Q

Describe colloid fluid replacement?

A

Contains macromolecules
Stays in vascular compartment longer
Used to replace proteins/ blood

133
Q

3 examples of colloid solutions?

A

Gelatin
Hydroxyethyl-starch fluids
Dextrans

134
Q

When is oxyglobin used for fluid replacement?

A

Shock cases

Auto immune haemolytic anaemia

135
Q

What are protozoa?

A

Single celled organisms
Multiply in host
Short generation times
Usually accute infections

136
Q

What are metazoa?

A

Multi cellular organisms
Do not multiply in host -dose dependant
Long generation time
Chronic infection common

137
Q

3 examples of protozoa

A

Babesia
Leishmania
Trypanosoma

138
Q

3 examples of metazoa

A

Round worms
Flat worms
Ectoparasites (fleas/ticks)

139
Q

Main features of babesia?

A

Tick vector

Replicate in RBC of host

140
Q

Main features of leishmania?

A

Sandfly vector

Replicate in macrophages

141
Q

Main features of nematodes (heart worm)?

A

Mosquito vector
Adults develop is pulmonary artery of heart
Larvae in blood

142
Q

How does stress occur and what are the features?

A

Induced by corticosteroids

Mature neutrophilia

143
Q

Features of inflammation? (histology)

A

neutrophilia
lymphopenia
monocytosis

144
Q

Causes of inflammation?

A

Tissue necrosis
Immune mediated disease
Infectious causes
Neoplasia

145
Q

What is leukaemia?

A

Overproduction of WBC

146
Q

When does chronic leukaemia occur?

A

Older animals

147
Q

What is transudate inflammation?

A

Leakage of fluid with water and electrolytes but low [protein] and [cell] – similar to edema (water in tissue)

148
Q

What is exudate inflammation?

A

Leakage of fluid containing water, electrolytes, high [protein] and high [inflammatory cells]

149
Q

What are the three Rs?

A

Replacement, reduction and refinement

150
Q

Describe the alpha helix in biological proteins?

A

H bonds parallel to the helix axis

151
Q

Are antigens on RBC surface equally antigenic?

A

No

152
Q

Why does CO have higher affinity for ISOLATED heme?

A

Distal histidine residue on globin chan reduces CO binding

153
Q

What blood tube for biochem

A

Heparin

154
Q

Order of blood tube fill?

A 
Plain
Sodium citrate
Serum
Heparin
EDTA
Sodium flouride
155
Q

Substitution cause of sickle cell anaemia ?

A

Substitution of polar AA with hydrophobic (non polar) AA in beta chain of Hb

156
Q

3 functions of lymphatic system?

A

Immune defence
Fluid balance
Lipid absorption

157
Q

Deficiency of C3 lead to:

A

Recurrent bacterial infection

158
Q

What is IgA?

A

Antibody found in mucosal secretions

159
Q

Describe affinity and avidity of IgM?

A

Pentameric
High avidity
Low affinity

160
Q

Which cells does MHC class 2 processing occur?

A

Dendritic
Macrophages
B cells

161
Q

Which immunoglobulin bonds to mast cells and induces granulation?

A

IgE

162
Q

What does ELISA test for?

A

Viral antigen

Module 2 (3 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions