[LEC/LAB] Complement System Flashcards
1
Q
3 PATHWAYS OF THE COMPLEMENT SYSTEM
A
CLASSICAL
ALTERNATIVE
MANNAN BINDING LECTIN
2
Q
ORIGINAL NAME OF THE ALTERNATIVE PATHWAY
A
PROPERDIN SYSYTEM
3
Q
WHAT USED TO BE DEEMED AS THE MAIN INITIATOR OF THE ALTERNATIVE PATHWAY
A
PROPERDIN
4
Q
WHERE ARE MOST PLASMA COMPLEMENT PROTEINS SYNTHESIZED
A
LIVER
5
Q
WHAT COMPLEMENT COMPONENT IS NOT SYNTHESIZED BY THE LIVER
A
C1
6
Q
WHERE IS C1 SYNTHESIZED
A
INTESTINAL EPITHELIAL CELLS
7
Q
SERUM PROTEIN THAT IS SYNTHESIZED IN THE ADIPOSE TISSUE
A
FACTOR D
8
Q
ADDITIONAL SOURCE OF EARLY COMPLEMENT COMPONENTS
A
MONOCYTES
MACROPHAGES
9
Q
[TRUE OR FALSE]
MOST OF THE PROTEINS INVOLVED IN THE COMPLEMENT SYSTEM ARE ACTIVE PRECURSORS
A
FALSE
INACTIVE PRECURSORS OR ZYMOGENS
10
Q
[FUNCTION OF THE SERUM PROTEIN]
C1q
A
BINDS TO FC REGION OF IGM AND IGG
11
Q
[FUNCTION OF THE SERUM PROTEIN]
C1r
A
ACTIVATES C1s
12
Q
[FUNCTION OF THE SERUM PROTEIN]
C1s
A
CLEAVES C4 AND C2
13
Q
[FUNCTION OF THE SERUM PROTEIN]
C4
A
PART OF THE C3 CONVERTASE
14
Q
[PROTEIN COMPONENTS]
C3 CONVERTASE
A
C4b2a
15
Q
[FUNCTION OF THE SERUM PROTEIN]
C2
A
BINDS TO C4B
FORMS C3 CONVERTASE
16
Q
[FUNCTION OF THE SERUM PROTEIN]
C3
A
KEY INTERMEDIATE IN ALL PATHWAYS
17
Q
[FUNCTION OF THE SERUM PROTEIN]
C5
A
INITIATES MAC
18
Q
[FUNCTION OF THE SERUM PROTEIN]
C6
A
BINDS TO C5b IN MAC
19
Q
[FUNCTION OF THE SERUM PROTEIN]
C7
A
BINDS TO C5bC6 IN MAC
20
Q
[FUNCTION OF THE SERUM PROTEIN]
C8
A
STARTS PORE FORMATION ON MEMBRANE
21
Q
[FUNCTION OF THE SERUM PROTEIN]
C9
A
POLYMERIZES TO CAUSE CELL LYSIS
22
Q
[PROTEIN COMPONENT]
C5 CONVERTASE
A
C4b2a3b
23
Q
[PROTEIN COMPONENT]
MAC
A
C5b6789
24
Q
[FUNCTION OF THE SERUM PROTEIN]
FACTOR B
A
BINDS TO C3B TO FORM C3 CONVERTASE
25
[FUNCTION OF THE SERUM PROTEIN]
FACTOR D
CLEAVES FACTOR B
26
[FUNCTION OF THE SERUM PROTEIN]
PROPERDIN
STABILIZES C3 CONVERTASE
ALTERNATIVE PATHWAY — C3bBb
27
[FUNCTION OF THE SERUM PROTEIN]
MBL
BINDS TO MANNOSE
28
[FUNCTION OF THE SERUM PROTEIN]
MASP-1
UNKNOWN
29
[FUNCTION OF THE SERUM PROTEIN]
MASP-2
CLEAVES C4 AND C2
30
MAIN ANTIBODY DIRECTED MECHANISM
CLASSICAL
31
ARE ALL IMMUNOGLOBULINS ABLE TO ACTIVATE THE CLASSICAL PATHWAY
NO
32
IG CLASSES THAT CAN ACTIVATE THE CLASSICAL PTW
IGM
IGG1
IGG2
IGG3
33
IG CLASSES THAT CANNOT ACTIVATE THE CLASSICAL PATHWAY
IGG4
IGA
IGE
34
IG CLASS THAT IS MOST EFFICIENT IN ACTIVATING THE COMPLEMENT AND WHY
IGM
MULTIPLE BINDING SITES
35
WHO WON A NOBEL PRIZE FOR DESCRIBING THE COMPLEMENT SYSTEM
JULES BORDET
36
IS THE COMPLEMENT CONSIDERED AS AN ACUTE PHASE REACTANT
WHY OR WHY NOT
YES
LEVELS RISE DURING AN INFECTION
37
IS THE COMPLEMENT SYSTEM HEAT LABILE
YES
SERUM IS HEATED TO 56C FOR 30 MINS
38
WILL THE COMPLEMENT SYSTEM BE ACTIVATED EVEN IF EPITOPES ARE FAR FROM EACH OTHER
NO
39
MOST EFFECTIVE IGG SUBUNIT FOR COMPLEMENT ACTIVATION
IGG3
IGG3>IGG1>IGG2
40
3 MAIN STAGES OF COMPLEMENT ACTIVATION
RECOGNITION — C1
ACTIVATION — C4, C2, C3
MAC — C56789
41
UNIT THAT COMPLETES THE LYSIS OF FOREGN PARTICLES
MAC
C56789
42
WHAT IS MAINTAINS THE STRUCTURE OF THE RECOGNITION UNIT
CALCIUM
43
C1 UNIT THAT BINDS TO AB MOLECULES
C1Q
44
C1 SUBUNITS THAT GENERATE ENZYME ACTIVITY TO BEGIN THE CASCADE
C1R
C1S
45
WHAT HAPPENS WHEN CALCIUM IS NOT PRESENT IN SERUM
C1R AND C1S DISSOCIATE FROM C1Q
46
WHAT REGION OF THE AB DOES C1Q RECOGNIZE
FC REGION
47
SERINE PROTEASE PROENZYMES
C1R
C1S
48
STRUCTURAL REQUIREMENT FOR C1 TO BE BOUND TO THE FC REGION
AT LEAST TWO OF THE GLOBULAR HEADS OF C1Q
49
AS BINDING OCCURS, WHAT ARE C1R AND C1S CONVERTED TO
ACTIVE ENZYMES
THEY ARE ORIGINALLY ZYMOGENS
50
WHAT IS A ZYMOGEN
INACTIVE ENZYME
51
WHY IS ACTIVATED C1R EXTREMELY SPECIFIC
ITS ONLY KNOWN SUBSTRATE IS C1S
52
DOES C1S HAVE LIMITED SPECIFICITY
WHY OR WHY NOT
YES
ITS ONLY SUBSTRATES ARE C4 AND C2
53
WHEN DOES THE RECOGNITION STAGE END
ONCE C1S IS ACTIVATED
54
WHEN DOES THE ACTIVATION STAGE START
WHEN C1S CLEAVES C4
55
WHEN DOES THE ACTIVATION STAGE END
WHEN C5 CONVERTASE IS PRODUCED
56
SECOND MOST ABUNDANT COMPLEMENT PROTEIN
C4
57
WHAT HAPPENS TO C4B WHEN IT FAILS TO BIND WITH A PROTEIN WITHIN A FEW SECONDS
IT REACTS WITH WATER
iC4B IS FORMED
iC4B IS RAPIDLY DEGRADED
COMPLEMENT CANNOT PROCEED
58
RATIO OF C1 TO C4 MOLECULES
1 C1 MOLECULE : 30 C4 MOLECULES (TO BE SPLIT)
59
BASIS OF NAMING COMPLEMENT PROTEINS
ORDER OF DISCOVERY
60
THE C2 GENE IS CLOSELY ASSOCIATED WITH THE GENE THAT CODES FOR THIS SERUM PROTEIN
FACTOR B
61
THE ONLY SERUM PROTEIN THAT BINDS “A”
C2a
62
C3B CAN ALSO SERVE AS WHAT KIND OF PROTEIN
OPSONIN
63
WHY ARE A LARGE NUMBER OF C3 MOLECULES NEEDED IN THE AMPLIFICATION STAGE
TO INCREASE THE CHANCES OF C3 BINDING
C3 HAS A SHORT HALF LIFE
C3 NEEDS TO BE BOUND IMMEDIATELY
IF NOT THEN IT BECOMES HYDROLYZED
64
POLYPEPTIDE CHAINS IN C5
ALPHA
BETA
65
WHERE DOES C5b ATTACH
TO THE CELL MEMBRANE
66
FUNCTION OF C8’S HYDROPHOBIC PART
ANCHOR THE MAC WITHIN THE TARGET MEMBRANE
67
PATHWAY ACTIVATED BY THE RECOGNITION OF SURFACE MOIETIES FOUND ON PATHOGENS
LECTIN
68
PATHWAY THAT PROVIDES AN ADDITIONAL LINK BETWEEN THE INNATE AND ACQUIRED IMMUNE RESPONSE
LECTIN PATHWAY
69
WHY IS THE LECTIN PATHWAY A LINK BETWEEN THE INNATE AND ACQUIRED IMMUNE RESPONSE
IT INVOLVES THE NONSPECIFIC RECOGNITION OF CARBOHYDRATES THAT ARE COMMON CONSTITUENTS OF MICROBIAL CELL WALLS
70
ARE THE LECTIN PATHWAY MOLECULES STRUCTURALLY SIMILAR TO THOSE OF THE CLASSICAL
YES
71
COMPLEMENT PROTEINS SHARED BY THE LECTIN AND CLASSICAL PATHWAYS
C4
C2
72
THREE CLASSES OF MOLECULES FOUND IN THE LECTIN PATHWAY
LECTINS
FOLINS
CL-K1
73
PROTEIN CLASS OF LECTINS, FOLINS, CL-K1, AND C1Q
COLLECTINS
74
IS MBL BINDING CALCIUM DEPENDENT
YES
75
WHERE IS MANNOSE FOUND
GLYCOPROTEINS OR CARBOHYDRATES OF MICROORGANISMS
76
WHY IS MBL CONSIDERED AS AN ACUTE PHASE PROTEIN
PRODUCED IN THE LIVER
NORMALLY PRESENT IN THE SERUN
INCREASES DURING AN INITIAL INFLAMMATORY RESPONSE
77
PATHWAY THAT PLAYS A ROLE IN INFANT’S DEFENSE MECHANISM
LECTIN PATHWAY
78
PATHWAY THAT FUNCTIONS AS AN AMPLIFICATION LOOP
ALTERNATIVE PATHWAY
79
TRIGGERING SUBSTANCES FOR THE ALTERNATIVE PATHWAY
BACTERIAL CELL WALLS
80
ROLE OF FACTOR B IS ANALOGOUS TO WHAT COMPLEMENT COMPONENT
C2
81
MAJOR FUNCTIONS OF THE COMPLEMENT SYSTEM
OPSONIZATION
INFLAMMATION
CYTOTOXICITY
82
[COMPLEMENT NOMENCLATURE]
i
INDICATED INACTIVATION
83
[COMPLEMENT NOMENCLATURE]
HORIZONTAL BAR
COMPLEMENT PROTEIN IS AN ACTIVE ENZYME
84
HEATING CONDITION AFTER 4 HOURS DELAY IN COMPLEMENT TESTING
RE-INACTIVATE SERUM AT 56C FOR 10 MINS
85
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
IMMUNE COMPLEXES
CLASSICAL
86
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
APOPTOTIC CELLS
COMPLEMENT
87
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
GRAM NEGATIVE BACTERIA
CLASSICAL
88
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
CRP
CLASSICAL
89
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
BACTERIA, FUNGI, VIRUSES
ALTERNATE
90
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
TUMOR CELLS
ALTERNATE
91
[PATHWAY ACTIVATED BY GIVEN INITIATOR]
MICROBES WITH TERMINAL MANNOSE GROUPS
MBL
92
[SIMILAR FUNCTION]
[MBL AND CLASSICAL]
MBL
C1Q
93
[SIMILAR FUNCTION]
[MBL AND CLASSICAL]
MASP-1
C1R
94
[SIMILAR FUNCTION]
[MBL AND CLASSICAL]
MASP-2
C1S
95
[FUNCTION OF THE SERUM PROTEIN]
C1-INH
DISSOCIATES C1R AND C1S FROM C1Q
96
[FUNCTION OF THE SERUM PROTEIN]
FACTOR I
CLEAVES C3B AND C4B
97
[FUNCTION OF THE SERUM PROTEIN] FACTOR H
COFACTOR WITH I TO INACTIVATE C3B
PREVENTS BINDING OF B TO C3B
98
[FUNCTION OF THE SERUM PROTEIN] C4BP
ACTS AS A COFACTOR WITH I TO INACTIVATE C4B
99
[FUNCTION OF THE SERUM PROTEIN] S PROTEIN
VITRONECTIN
PREVENTS ATTACHMENT OF C5B67 COMPLEX TO CELL MEMBRANES
100
CR1 IS ALSO KNOWN AS
CD35
101
[FUNCTION OF THE SERUM PROTEIN]
DAF
DISSOCIATES C3 CONVERTASE
102
[FUNCTION OF THE SERUM PROTEIN]
HRF
INHIBITS MAC
103
[FUNCTION OF THE SERUM PROTEIN]
MIRL OR CD59
INHIBITS MAC
104
SUBSTANCE THAT PROMOTES THE PRODUCTION OF HISTAMINE
ANAPHYLOTOXINS
105
PROTEINS THAT CAN PROMOTE VASODILATION
KININS
106
SHOULD IMMUNE COMPLEXES REMAIN IN THE BODY
NO
107
[COMPLEMENT COMPONENT/SERUM PROTEIN]
PROKININ
C2B
108
[COMPLEMENT COMPONENT/SERUM PROTEIN]
ANAPHYLOTOXIN
C3A
C4A
C5A
109
[COMPLEMENT COMPONENT/SERUM PROTEIN]
OPSONIN
C3B
C4B
110
[COMPLEMENT COMPONENT/SERUM PROTEIN]
CHEMOTACTIC FACTOR
C5A
111
[COMPLEMENT COMPONENT/SERUM PROTEIN]
CHEMOTOXIN
C5B67
112
ABILITY OF CELLS TO BIND COMPLEMENT COATED PARTICLES
IMMUNE ADHERENCE
113
MOST EFFICICENT COFACTOR FOR FACTOR I-MEDIATED CLEAVAGE OF C3B
MCP
CD46
114
PROTECTS THE HOST CELLS FROM BYSTANDER LYSIS
DAF
115
[COMPLEMENT COMPONENT/SERUM PROTEIN]
IMMUNE ADHERENCE
C3B
116
[ASSOCIATED DISEASE]
C1QRS
LUPUS ERYTHRMATOUS-LIKE SYNDROME
RECURRENT INFECTIONS
117
[ASSOCIATED DISEASE]
C2
LUPUS ERYTHEMATOUS-LIKE SYNDROME
RECURRENT INFECTIONS
ATHEROSCLEROSIS
118
[ASSOCIATED DISEASE]
C3
SEVERE RECURRENT INFECTIONS
119
[ASSOCIATED DISEASE]
C4
LUPUS LIKE SYNDROME
120
[ASSOCIATED DISEASE]
C5678
NEISSERIA INFECTION
121
[ASSOCIATED DISEASE]
C9
NONE
122
[ASSOCIATED DISEASE]
C1-INH
HEREDITARY ANGIOEDEMA
123
[ASSOCIATED DISEASE]
DAF
PAROXYSMAL NOCTURNAL HEMOGLOBINURIA
124
[ASSOCIATED DISEASE]
HRF
PAROXYSMAL NOCTURNAL HEMOGLOBINURIA
125
[ASSOCIATED DISEASE]
FACTOR H OR I
RECURRENT BACTERIAL INFECTIONS
126
[ASSOCIATED DISEASE]
MBL
PNEUMOCOCCAL DISEASE
SEPSIS
NEISSERIA INFECTIONS
127
WHAT DECREASES THE DIAMETER OF BLOOD VESSELS VIA IMMUNE COMPLEXES
MICROCLOTS
128
INHIBITOR THAT LEADS TO FRAGMENTOCYTES
ANTIFACTOR H
129
DIFFERENCE OF CH50 VS AH50
CH50
Sheep RBC
AH50
Rabbit RBC
130
[COMPLEMENT ASSAY INTERPRETATION]
CH50 LOW
AH50 NORMAL
MISSING C1QRS
MISSING C4
131
[COMPLEMENT ASSAY INTERPRETATION]
CH50 NORMAL
AH50 LOW
MISSING PROPERDIN
MISSING FACTOR B OR D
132
[COMPLEMENT ASSAY INTERPRETATION]
CH50 LOW
AH50 LOW
MISSING C3
MISSING C56789
133
[COMPLEMENT ASSAY INTERPRETATION]
LATE COMPONENTS LOW
MISSING FACTOR H OR I
134
WHAT HOLDS C1QRS TOGETHER
CALCIUM
135
BETA GLOBULIN THAT ORIGINATES FROM PROC4
C4
136
WILL A PRIMITIVE MECHANISM REQUIRE C1, C2, AND C4
NO
137
C3Bb IS DEPENDENT ON WHAT ION
MAGNESIUM
