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immunio globulins Flashcards

1
Q

what are the two responses of immune system

A

*Specific & Non Specific response

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2
Q

what are the exterior barriers of “Non Specific response”

A

Skin, Mucous membrane, Secretions

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3
Q

what does “non Specific response” involves and includes?

A

Involves myeloid leukocytes (including all phagocytic cells) such as macrophages

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4
Q

What will Participate in the inflammatory response to injury or disease.

A

Macrophages and Mast cell

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5
Q

what are cytokines

A

Proteins signal between cells,

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6
Q

what are the specs of Specific response

A

*Antigen-antibody relationship (acquired immunity).
*Vaccinations depend on this
*Involves lymphocytes (B, T and plasma cells)

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7
Q

what are the components of immune system?

A

A) Cellular
B) molecular

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8
Q

what is the role of B-lymphocytes in cellular immune system

A

it is responsible for humoral response (plasma immunoglobulins; humoral antibodies).

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9
Q

what is the role of T-lymphocytes in cellular immune system

A

it is responsible for cellular response (Cytotoxic killer T cells & Helper cells).
Macrophages.

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10
Q

Mature B cells are produce by ?

A

Molecular immunoglobulins

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11
Q

what are immunoglobulin and made for ??

A

Immunoglobulin is a glycoprotein that is made in response to an antigen

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12
Q

what globulin is immunoglobulins are

A

immunoglobulin are GAMMA globulin

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13
Q

immunoglobulin are synthesized by ?

A

plasma cell

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14
Q

what is the Constitute of total serum proteins in immunoglobulin

A

25-30%

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15
Q

where does antibodies of immunoglobulin present in ??

A

serum, tissue fluids & mucosal surfaces.

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16
Q

what is the different between antibodies and immunoglobulin

A

All antibodies are immunoglobulins, but all immunoglobulins may not be antibodies.

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17
Q

basic structure of immunoglobulin

A

Composed of 4 polypeptide chains.

2 identical light & 2 identical heavy chains.

Linked by disulphide bonds.

Light chains similar in all immunoglobulins.

Light chains occur in 2 varieties kappa & lambda

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18
Q

light and heavy chains of immunoglobulin subdivides into ?

A

variable & constant region.

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19
Q

what does Each heavy & light chain contains ?

A

amino terminal & carboxy terminal

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20
Q

what are heavy chain?

A

Heavy chains are structurally & antigenically distinct for each class.

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21
Q

how does loops form

A

Each immunoglobulin peptide chain has intra chain disulphide bonds

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22
Q

what is domain

A

Each loop is compactly folded to form a globular structure

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23
Q

what is light chain immunoglobulin contain

A

Light chain contains a single variable domain (VL) & a single constant domain (CL).

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24
Q

what does heavy chain immunoglobulin contain

A

Heavy chain contains one variable domain (VH) & 3 constant domains (CH1, CH2, CH3).

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25
Q

what is hinge region

A

the segment in heavy chain –between CH1, CH2.

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26
Q

what is papain enzyme?

A

Peptide bonds in the hinge region are broken.
Produces 3 fragments.
2 identical fragments called Fab (functional antigen binding) fragments; antigen binding activity.
The other fragment called Fc fragment (Fraction crystallizable).

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27
Q

what is pepsin digestion produce

A

Produce a single fragment composed of 2 Fab like subunits F(ab); 2 binds antigen.

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28
Q

Is “Fc fragment” is recovered in proteolytic enzyme

A

Fc fragment is not recovered; digested to small numerous peptides

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29
Q

what is Fc region composed of?

A

is composed of two heavy chains that contribute two or three constant domains depending on the class of the antibody

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30
Q

classification of immunoglobulin

A

classified as 5 types
Ig G - (gamma)
Ig A - (alpha)
Ig M - (mu)
Ig D - (delta)
Ig E - (epsilon)

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31
Q

what is the most abundant immunoglobulin in serum ?

A

Immunoglobulin G (igG)

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32
Q

what is the constitution of igG and where it is present?

A

75-80% total Ig and present in blood, plasma & tissue fluids.

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33
Q

life time of IgG

A

It has a half life of 23 days: the longest of all of the Ig isotypes

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34
Q

what does IgG do at the period of birth and to the fetus ?

A

Crosses placenta & provide natural immunity to fetus & neonate at birth

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35
Q

what does IgG do to toxin?

A

it neutralize the toxin

36
Q

what does it will do to the virus?

A

It opsonizing; increase the susceptibility of (bacteria) to ingestion by phagocytes.

37
Q

What are the sub classes of IgG?

A

Ig G1, Ig G2, Ig G3, Ig G4.

38
Q

Biological Functions of IgG Subclasses

A

IgG1, IgG3, IgG4 – cross placenta & protect fetus

IgG1 & IgG3 binds to Fc receptor on phagocytic cells, monocytes & macrophages and mediate opsonizations (susceptibility of (bacteria) to ingestion by phagocytes)

39
Q

how many percentage does IgA constitute and where does it present?

A

Constitutes 10-15 % of total Ig.

Present in milk, saliva, tears, mucous of respiratory, digestive & genitourinary tracts.

40
Q

in serum IgA exist as?

A

monomers

41
Q

in external secretion IgA exist as? and what is has? life time ?

A

In external secretions, exist as dimer called secretory Ig.
Has ‘J’ chain & secretory piece.
Half life: 6-8 days

42
Q

Formation of Secretory Ig A

A

Dimeric Ig A binds to the receptor on the surface of the epithelial cells – endocytosed & transported across the cell to the luminal surface

43
Q

what happened to
IgA after reaching to surface

A

the poly-Ig receptor is cleaved.

44
Q

what will happen to the remaining portion of the receptors in IgA

A

It will remains attached to the Ig A dimer as a secretory component.

45
Q

what will the secretory do in IgA ?

A

It will protects Ig A from digestive enzymes & denaturation by bacterial proteases

46
Q

Functions of Ig A

A

Provides local immunity.

Secretory IgA binds to surface antigens of microorganism & prevent its attachment

invasion of the mucosal surfaces of respiratory & digestive tract and immune elimination.

invasion of the mucosal surfaces of respiratory & digestive tract and immune elimination.

47
Q

what does secretory IgA provides?

A

It provides important line of defense against salmonella, Vibrio cholerae, N. gonorrhoeae, influenza virus and poliovirus.

48
Q

Functions of Ig A

A

Secretory IgA present in breast milk protects newborn during first months of life.

Promotes phagocytosis & intracellular killing of microorganisms.

49
Q

what is the amount of protein in IgM

A

for 5-10% of total immunoglobulin proteins.

50
Q

how many monomeric units are there in IgM

A

Polymer of five monomeric units (pentamer).

51
Q

with what is IgM is held ?

A

Held together by disulfide bonds & ‘J’ chain.

52
Q

what is the molecular weight and life time of IgM

A

Mol. Wt. of 900,000- 1,000,000 (millionaire molecule).
Half life: 5 days.

53
Q

Functions Of Ig M

A

It agglutinates bacteria.

Causes opsonization & immune hemolysis.

Believed to be responsible for protection against blood invasion by microorganisms.

54
Q

what is the First Ig to be produced in primary response to antigen.

A

immunoglobulin M (IgM)

55
Q

what is the life time of IgM

A

Relatively short-lived hence its demonstration in the serum indicates recent infection.

56
Q

where does Monomeric IgM appears?
and how it act?

A

Monomeric IgM appears on the surface of unstimulated B lymphocytes & act as receptors for antigens.

57
Q

how many percentage IgM contain and where it present?

A

Most of IgM (80%) present intravascularly.
And in low concentration in intercellular tissue fluids

58
Q

what infection does IgM antibodies indicates

A

Presence of IgM antibody in serum of newborn indicate congenital infection

59
Q

does IgM can cross placenta

A

No it Cannot cross placenta.

60
Q

Earliest immunoglobulin to be synthesized by fetus at?

A

20 weeks

61
Q

structure and region of domains of IgE

A

Structure is similar to IgG.
Has 4 constant region domains

62
Q

what is the molecular weight and life time of IgE

A

Mol. Wt. 1,90,000.
Half life: 2 days.

63
Q

what is Normal serum concentration

A

0.3 ug/ml

64
Q

where does IgE present

A

Mostly present extra cellularly.

65
Q

what is the Heat labile
of IgE and does it cross placenta ?

A

Heat labile (inactivated at 560C in 1 hour).
Does not cross placenta.

66
Q

where does IgE produced and binds

A

Produced in the lining of respiratory & intestinal tract.

Binds to the Fragment, crystallizable (Fc)receptors on the membranes of blood basophils & tissue mast cells.

67
Q

Functions of Immunoglobulin E (Ig E)

A

Mediates immediate hypersensitivity reaction.

Responsible for symptoms of anaphylactic shock, hay fever & asthma.

Play a role in immunity against helminthic parasites.

68
Q

where does IgE binds

A

IgE binds to Fc receptors on the membrane of blood basophils & tissue mast cells.

69
Q

what will happen to IgE while binding with same antigen?

A

cells degranulates; release histamine & pharmacological mediators of anaphylaxis from cell.

70
Q

Physical role of IgE

A

The physiological role of IgE appears to be protection against pathogens by mast cell degranulation & release of inflammatory mediators.

71
Q

structure and concentration of IgD

A

Structure is similar to IgG.
Serum concentration 30 ug/ ml.

72
Q

total percentage of constitute ig and life time

A

Constitutes 0.2% of total Ig.
Half life: 3 days

73
Q

what will happened IgD together with IgM

A

IgD together with IgM is major membrane bound Ig on unstimulated B lymphocytes and it acts as recognition receptors for antigens.

74
Q

Role of different immunoglobulin classes

A

Ig G: Protects the body fluids

Ig A: Protects the body surfaces

Ig M: Protects the blood stream

Ig E: Mediates type I hypersensitivity

Ig D: Role not known

75
Q

what is multiple myeloma (MM)

A

MM is a group of diseases characterized by proliferation of single plasma cell clone (myeloma cell)

76
Q

what will multiple myeloma (MM) cause

A

it cause overproduction of monoclonal immunoglobulin molecules known as paraprotein (myeloma M-protein).

77
Q

What is the origin of M-protein? in patients(percentage)

A

55% - IgG
23% - IgA
20% - Ig light chains
2 % - IgD, IgM

78
Q

Where are myeloma cells & paraproteins localized?

A

Myeloma cells
Bone marrow
Blood

Paraprotein
Blood
Urine (light chain -Bence- Jones protein)

79
Q

What is Biochemical Profile of Multiple Myeloma?

A

Plasma cell > 10%

Serum electrophoresis: M- band (sharp peak in the gamma-globin fraction).

Hypercalciemia

Normal ALP.

20% of patients with light chain paraprotein do not detect it in serum but show presence of Bence-Jones protein in the urine.

80
Q

What are Bence-Jones proteins?

A

Bence-Jones protein is Ig light chain.

The presence of specific protein in the urine of patient with Multiple Myeloma (MM)

81
Q

How are they detected by heating test?

A

ppt at 40-500C but dissolve on further urine heating to boiling point.

82
Q

what is Bone disease – lytic lesions of
bone ?

A

Activation of osteoclasts (increase resorption).

Inhibition of osteoblasts (decrease formation).

Pain, deformation.

83
Q

what is impaired renal function?

A

Overflow proteinuria.

84
Q

what causes renal tubular amyloidosis ?

A

Multiple myeloma may cause renal tubular amyloidosis

85
Q

what is amyloidosis and where it present

A

Amyloidosis,a buildup of abnormal protein, called amyloid, in the tissues and organs

86
Q

Obstruction of lumen of nephrons by

A

paraproteins.

87
Q

what is anemia

A

Bone marrow erythropoietic cell are replaced by the plasma cells, resulting in anemia.

amino acid (1 decks)

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