[LEC/LAB] Complement System Flashcards

1
Q

3 PATHWAYS OF THE COMPLEMENT SYSTEM

A

CLASSICAL
ALTERNATIVE
MANNAN BINDING LECTIN

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2
Q

ORIGINAL NAME OF THE ALTERNATIVE PATHWAY

A

PROPERDIN SYSYTEM

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3
Q

WHAT USED TO BE DEEMED AS THE MAIN INITIATOR OF THE ALTERNATIVE PATHWAY

A

PROPERDIN

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4
Q

WHERE ARE MOST PLASMA COMPLEMENT PROTEINS SYNTHESIZED

A

LIVER

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5
Q

WHAT COMPLEMENT COMPONENT IS NOT SYNTHESIZED BY THE LIVER

A

C1

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6
Q

WHERE IS C1 SYNTHESIZED

A

INTESTINAL EPITHELIAL CELLS

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7
Q

SERUM PROTEIN THAT IS SYNTHESIZED IN THE ADIPOSE TISSUE

A

FACTOR D

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8
Q

ADDITIONAL SOURCE OF EARLY COMPLEMENT COMPONENTS

A

MONOCYTES
MACROPHAGES

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9
Q

[TRUE OR FALSE]
MOST OF THE PROTEINS INVOLVED IN THE COMPLEMENT SYSTEM ARE ACTIVE PRECURSORS

A

FALSE
INACTIVE PRECURSORS OR ZYMOGENS

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10
Q

[FUNCTION OF THE SERUM PROTEIN]
C1q

A

BINDS TO FC REGION OF IGM AND IGG

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11
Q

[FUNCTION OF THE SERUM PROTEIN]
C1r

A

ACTIVATES C1s

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12
Q

[FUNCTION OF THE SERUM PROTEIN]
C1s

A

CLEAVES C4 AND C2

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13
Q

[FUNCTION OF THE SERUM PROTEIN]
C4

A

PART OF THE C3 CONVERTASE

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14
Q

[PROTEIN COMPONENTS]
C3 CONVERTASE

A

C4b2a

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15
Q

[FUNCTION OF THE SERUM PROTEIN]
C2

A

BINDS TO C4B
FORMS C3 CONVERTASE

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16
Q

[FUNCTION OF THE SERUM PROTEIN]
C3

A

KEY INTERMEDIATE IN ALL PATHWAYS

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17
Q

[FUNCTION OF THE SERUM PROTEIN]
C5

A

INITIATES MAC

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18
Q

[FUNCTION OF THE SERUM PROTEIN]
C6

A

BINDS TO C5b IN MAC

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19
Q

[FUNCTION OF THE SERUM PROTEIN]
C7

A

BINDS TO C5bC6 IN MAC

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20
Q

[FUNCTION OF THE SERUM PROTEIN]
C8

A

STARTS PORE FORMATION ON MEMBRANE

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21
Q

[FUNCTION OF THE SERUM PROTEIN]
C9

A

POLYMERIZES TO CAUSE CELL LYSIS

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22
Q

[PROTEIN COMPONENT]
C5 CONVERTASE

A

C4b2a3b

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23
Q

[PROTEIN COMPONENT]
MAC

A

C5b6789

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24
Q

[FUNCTION OF THE SERUM PROTEIN]
FACTOR B

A

BINDS TO C3B TO FORM C3 CONVERTASE

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25
Q

[FUNCTION OF THE SERUM PROTEIN]
FACTOR D

A

CLEAVES FACTOR B

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26
Q

[FUNCTION OF THE SERUM PROTEIN]
PROPERDIN

A

STABILIZES C3 CONVERTASE
ALTERNATIVE PATHWAY — C3bBb

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27
Q

[FUNCTION OF THE SERUM PROTEIN]
MBL

A

BINDS TO MANNOSE

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28
Q

[FUNCTION OF THE SERUM PROTEIN]
MASP-1

A

UNKNOWN

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29
Q

[FUNCTION OF THE SERUM PROTEIN]
MASP-2

A

CLEAVES C4 AND C2

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30
Q

MAIN ANTIBODY DIRECTED MECHANISM

A

CLASSICAL

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31
Q

ARE ALL IMMUNOGLOBULINS ABLE TO ACTIVATE THE CLASSICAL PATHWAY

A

NO

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32
Q

IG CLASSES THAT CAN ACTIVATE THE CLASSICAL PTW

A

IGM
IGG1
IGG2
IGG3

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33
Q

IG CLASSES THAT CANNOT ACTIVATE THE CLASSICAL PATHWAY

A

IGG4
IGA
IGE

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34
Q

IG CLASS THAT IS MOST EFFICIENT IN ACTIVATING THE COMPLEMENT AND WHY

A

IGM
MULTIPLE BINDING SITES

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35
Q

WHO WON A NOBEL PRIZE FOR DESCRIBING THE COMPLEMENT SYSTEM

A

JULES BORDET

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36
Q

IS THE COMPLEMENT CONSIDERED AS AN ACUTE PHASE REACTANT
WHY OR WHY NOT

A

YES
LEVELS RISE DURING AN INFECTION

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37
Q

IS THE COMPLEMENT SYSTEM HEAT LABILE

A

YES
SERUM IS HEATED TO 56C FOR 30 MINS

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38
Q

WILL THE COMPLEMENT SYSTEM BE ACTIVATED EVEN IF EPITOPES ARE FAR FROM EACH OTHER

A

NO

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39
Q

MOST EFFECTIVE IGG SUBUNIT FOR COMPLEMENT ACTIVATION

A

IGG3
IGG3>IGG1>IGG2

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40
Q

3 MAIN STAGES OF COMPLEMENT ACTIVATION

A

RECOGNITION — C1
ACTIVATION — C4, C2, C3
MAC — C56789

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41
Q

UNIT THAT COMPLETES THE LYSIS OF FOREGN PARTICLES

A

MAC
C56789

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42
Q

WHAT IS MAINTAINS THE STRUCTURE OF THE RECOGNITION UNIT

A

CALCIUM

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43
Q

C1 UNIT THAT BINDS TO AB MOLECULES

A

C1Q

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44
Q

C1 SUBUNITS THAT GENERATE ENZYME ACTIVITY TO BEGIN THE CASCADE

A

C1R
C1S

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45
Q

WHAT HAPPENS WHEN CALCIUM IS NOT PRESENT IN SERUM

A

C1R AND C1S DISSOCIATE FROM C1Q

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46
Q

WHAT REGION OF THE AB DOES C1Q RECOGNIZE

A

FC REGION

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47
Q

SERINE PROTEASE PROENZYMES

A

C1R
C1S

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48
Q

STRUCTURAL REQUIREMENT FOR C1 TO BE BOUND TO THE FC REGION

A

AT LEAST TWO OF THE GLOBULAR HEADS OF C1Q

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49
Q

AS BINDING OCCURS, WHAT ARE C1R AND C1S CONVERTED TO

A

ACTIVE ENZYMES
THEY ARE ORIGINALLY ZYMOGENS

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50
Q

WHAT IS A ZYMOGEN

A

INACTIVE ENZYME

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51
Q

WHY IS ACTIVATED C1R EXTREMELY SPECIFIC

A

ITS ONLY KNOWN SUBSTRATE IS C1S

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52
Q

DOES C1S HAVE LIMITED SPECIFICITY
WHY OR WHY NOT

A

YES
ITS ONLY SUBSTRATES ARE C4 AND C2

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53
Q

WHEN DOES THE RECOGNITION STAGE END

A

ONCE C1S IS ACTIVATED

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54
Q

WHEN DOES THE ACTIVATION STAGE START

A

WHEN C1S CLEAVES C4

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55
Q

WHEN DOES THE ACTIVATION STAGE END

A

WHEN C5 CONVERTASE IS PRODUCED

56
Q

SECOND MOST ABUNDANT COMPLEMENT PROTEIN

A

C4

57
Q

WHAT HAPPENS TO C4B WHEN IT FAILS TO BIND WITH A PROTEIN WITHIN A FEW SECONDS

A

IT REACTS WITH WATER
iC4B IS FORMED
iC4B IS RAPIDLY DEGRADED
COMPLEMENT CANNOT PROCEED

58
Q

RATIO OF C1 TO C4 MOLECULES

A

1 C1 MOLECULE : 30 C4 MOLECULES (TO BE SPLIT)

59
Q

BASIS OF NAMING COMPLEMENT PROTEINS

A

ORDER OF DISCOVERY

60
Q

THE C2 GENE IS CLOSELY ASSOCIATED WITH THE GENE THAT CODES FOR THIS SERUM PROTEIN

A

FACTOR B

61
Q

THE ONLY SERUM PROTEIN THAT BINDS “A”

A

C2a

62
Q

C3B CAN ALSO SERVE AS WHAT KIND OF PROTEIN

A

OPSONIN

63
Q

WHY ARE A LARGE NUMBER OF C3 MOLECULES NEEDED IN THE AMPLIFICATION STAGE

A

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
Q

POLYPEPTIDE CHAINS IN C5

A

ALPHA
BETA

65
Q

WHERE DOES C5b ATTACH

A

TO THE CELL MEMBRANE

66
Q

FUNCTION OF C8’S HYDROPHOBIC PART

A

ANCHOR THE MAC WITHIN THE TARGET MEMBRANE

67
Q

PATHWAY ACTIVATED BY THE RECOGNITION OF SURFACE MOIETIES FOUND ON PATHOGENS

A

LECTIN

68
Q

PATHWAY THAT PROVIDES AN ADDITIONAL LINK BETWEEN THE INNATE AND ACQUIRED IMMUNE RESPONSE

A

LECTIN PATHWAY

69
Q

WHY IS THE LECTIN PATHWAY A LINK BETWEEN THE INNATE AND ACQUIRED IMMUNE RESPONSE

A

IT INVOLVES THE NONSPECIFIC RECOGNITION OF CARBOHYDRATES THAT ARE COMMON CONSTITUENTS OF MICROBIAL CELL WALLS

70
Q

ARE THE LECTIN PATHWAY MOLECULES STRUCTURALLY SIMILAR TO THOSE OF THE CLASSICAL

A

YES

71
Q

COMPLEMENT PROTEINS SHARED BY THE LECTIN AND CLASSICAL PATHWAYS

A

C4
C2

72
Q

THREE CLASSES OF MOLECULES FOUND IN THE LECTIN PATHWAY

A

LECTINS
FOLINS
CL-K1

73
Q

PROTEIN CLASS OF LECTINS, FOLINS, CL-K1, AND C1Q

A

COLLECTINS

74
Q

IS MBL BINDING CALCIUM DEPENDENT

A

YES

75
Q

WHERE IS MANNOSE FOUND

A

GLYCOPROTEINS OR CARBOHYDRATES OF MICROORGANISMS

76
Q

WHY IS MBL CONSIDERED AS AN ACUTE PHASE PROTEIN

A

PRODUCED IN THE LIVER
NORMALLY PRESENT IN THE SERUN
INCREASES DURING AN INITIAL INFLAMMATORY RESPONSE

77
Q

PATHWAY THAT PLAYS A ROLE IN INFANT’S DEFENSE MECHANISM

A

LECTIN PATHWAY

78
Q

PATHWAY THAT FUNCTIONS AS AN AMPLIFICATION LOOP

A

ALTERNATIVE PATHWAY

79
Q

TRIGGERING SUBSTANCES FOR THE ALTERNATIVE PATHWAY

A

BACTERIAL CELL WALLS

80
Q

ROLE OF FACTOR B IS ANALOGOUS TO WHAT COMPLEMENT COMPONENT

A

C2

81
Q

MAJOR FUNCTIONS OF THE COMPLEMENT SYSTEM

A

OPSONIZATION
INFLAMMATION
CYTOTOXICITY

82
Q

[COMPLEMENT NOMENCLATURE]
i

A

INDICATED INACTIVATION

83
Q

[COMPLEMENT NOMENCLATURE]
HORIZONTAL BAR

A

COMPLEMENT PROTEIN IS AN ACTIVE ENZYME

84
Q

HEATING CONDITION AFTER 4 HOURS DELAY IN COMPLEMENT TESTING

A

RE-INACTIVATE SERUM AT 56C FOR 10 MINS

85
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
IMMUNE COMPLEXES

A

CLASSICAL

86
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
APOPTOTIC CELLS

A

COMPLEMENT

87
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
GRAM NEGATIVE BACTERIA

A

CLASSICAL

88
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
CRP

A

CLASSICAL

89
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
BACTERIA, FUNGI, VIRUSES

A

ALTERNATE

90
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
TUMOR CELLS

A

ALTERNATE

91
Q

[PATHWAY ACTIVATED BY GIVEN INITIATOR]
MICROBES WITH TERMINAL MANNOSE GROUPS

A

MBL

92
Q

[SIMILAR FUNCTION]
[MBL AND CLASSICAL]
MBL

A

C1Q

93
Q

[SIMILAR FUNCTION]
[MBL AND CLASSICAL]
MASP-1

A

C1R

94
Q

[SIMILAR FUNCTION]
[MBL AND CLASSICAL]
MASP-2

A

C1S

95
Q

[FUNCTION OF THE SERUM PROTEIN]
C1-INH

A

DISSOCIATES C1R AND C1S FROM C1Q

96
Q

[FUNCTION OF THE SERUM PROTEIN]
FACTOR I

A

CLEAVES C3B AND C4B

97
Q

[FUNCTION OF THE SERUM PROTEIN] FACTOR H

A

COFACTOR WITH I TO INACTIVATE C3B
PREVENTS BINDING OF B TO C3B

98
Q

[FUNCTION OF THE SERUM PROTEIN] C4BP

A

ACTS AS A COFACTOR WITH I TO INACTIVATE C4B

99
Q

[FUNCTION OF THE SERUM PROTEIN] S PROTEIN
VITRONECTIN

A

PREVENTS ATTACHMENT OF C5B67 COMPLEX TO CELL MEMBRANES

100
Q

CR1 IS ALSO KNOWN AS

A

CD35

101
Q

[FUNCTION OF THE SERUM PROTEIN]
DAF

A

DISSOCIATES C3 CONVERTASE

102
Q

[FUNCTION OF THE SERUM PROTEIN]
HRF

A

INHIBITS MAC

103
Q

[FUNCTION OF THE SERUM PROTEIN]
MIRL OR CD59

A

INHIBITS MAC

104
Q

SUBSTANCE THAT PROMOTES THE PRODUCTION OF HISTAMINE

A

ANAPHYLOTOXINS

105
Q

PROTEINS THAT CAN PROMOTE VASODILATION

A

KININS

106
Q

SHOULD IMMUNE COMPLEXES REMAIN IN THE BODY

A

NO

107
Q

[COMPLEMENT COMPONENT/SERUM PROTEIN]
PROKININ

A

C2B

108
Q

[COMPLEMENT COMPONENT/SERUM PROTEIN]
ANAPHYLOTOXIN

A

C3A
C4A
C5A

109
Q

[COMPLEMENT COMPONENT/SERUM PROTEIN]
OPSONIN

A

C3B
C4B

110
Q

[COMPLEMENT COMPONENT/SERUM PROTEIN]
CHEMOTACTIC FACTOR

A

C5A

111
Q

[COMPLEMENT COMPONENT/SERUM PROTEIN]
CHEMOTOXIN

A

C5B67

112
Q

ABILITY OF CELLS TO BIND COMPLEMENT COATED PARTICLES

A

IMMUNE ADHERENCE

113
Q

MOST EFFICICENT COFACTOR FOR FACTOR I-MEDIATED CLEAVAGE OF C3B

A

MCP
CD46

114
Q

PROTECTS THE HOST CELLS FROM BYSTANDER LYSIS

A

DAF

115
Q

[COMPLEMENT COMPONENT/SERUM PROTEIN]
IMMUNE ADHERENCE

A

C3B

116
Q

[ASSOCIATED DISEASE]
C1QRS

A

LUPUS ERYTHRMATOUS-LIKE SYNDROME
RECURRENT INFECTIONS

117
Q

[ASSOCIATED DISEASE]
C2

A

LUPUS ERYTHEMATOUS-LIKE SYNDROME
RECURRENT INFECTIONS
ATHEROSCLEROSIS

118
Q

[ASSOCIATED DISEASE]
C3

A

SEVERE RECURRENT INFECTIONS

119
Q

[ASSOCIATED DISEASE]
C4

A

LUPUS LIKE SYNDROME

120
Q

[ASSOCIATED DISEASE]
C5678

A

NEISSERIA INFECTION

121
Q

[ASSOCIATED DISEASE]
C9

A

NONE

122
Q

[ASSOCIATED DISEASE]
C1-INH

A

HEREDITARY ANGIOEDEMA

123
Q

[ASSOCIATED DISEASE]
DAF

A

PAROXYSMAL NOCTURNAL HEMOGLOBINURIA

124
Q

[ASSOCIATED DISEASE]
HRF

A

PAROXYSMAL NOCTURNAL HEMOGLOBINURIA

125
Q

[ASSOCIATED DISEASE]
FACTOR H OR I

A

RECURRENT BACTERIAL INFECTIONS

126
Q

[ASSOCIATED DISEASE]
MBL

A

PNEUMOCOCCAL DISEASE
SEPSIS
NEISSERIA INFECTIONS

127
Q

WHAT DECREASES THE DIAMETER OF BLOOD VESSELS VIA IMMUNE COMPLEXES

A

MICROCLOTS

128
Q

INHIBITOR THAT LEADS TO FRAGMENTOCYTES

A

ANTIFACTOR H

129
Q

DIFFERENCE OF CH50 VS AH50

A

CH50
Sheep RBC

AH50
Rabbit RBC

130
Q

[COMPLEMENT ASSAY INTERPRETATION]
CH50 LOW
AH50 NORMAL

A

MISSING C1QRS
MISSING C4

131
Q

[COMPLEMENT ASSAY INTERPRETATION]
CH50 NORMAL
AH50 LOW

A

MISSING PROPERDIN
MISSING FACTOR B OR D

132
Q

[COMPLEMENT ASSAY INTERPRETATION]
CH50 LOW
AH50 LOW

A

MISSING C3
MISSING C56789

133
Q

[COMPLEMENT ASSAY INTERPRETATION]
LATE COMPONENTS LOW

A

MISSING FACTOR H OR I

134
Q

WHAT HOLDS C1QRS TOGETHER

A

CALCIUM

135
Q

BETA GLOBULIN THAT ORIGINATES FROM PROC4

A

C4

136
Q

WILL A PRIMITIVE MECHANISM REQUIRE C1, C2, AND C4

A

NO

137
Q

C3Bb IS DEPENDENT ON WHAT ION

A

MAGNESIUM