immunoglobulins

[Guest guest]

Molecular Biology of the Cell, 3rd edn. Part IV. Cells in Their Social

Context Chapter 23 . The Immune System

The Functional Properties of Antibodies 10

Introduction

Vertebrates rapidly die of infection if they are unable to make antibodies.

Antibodies defend us against infection by inactivating viruses and bacterial

toxins and by recruiting the complement system and various types of white

blood cells to kill extracellular microorganisms and larger parasites.

Synthesized exclusively by B cells, antibodies are produced in millions of

forms, each with a different amino acid sequence and a different binding

site for antigen. Collectively called immunoglobulins (abbreviated as Ig),

they are among the most abundant protein components in the blood,

constituting about 20% of the total plasma protein by weight. In this

section we describe the five classes of antibodies found in higher

vertebrates, each of which mediates a characteristic biological response

following antigen binding.

>>>>SNIP

Summary

A typical antibody molecule is a Y-shaped protein with two identical

antigen-binding sites at the tips of the Y (the Fab regions) and binding

sites for complement components and/or various cell-surface receptors on the

tail of the Y (the Fc region). Antibodies defend vertebrates against

infection by inactivating viruses and bacterial toxins and by recruiting the

complement system and various cells to kill and ingest invading

microorganisms.

Each B cell clone makes antibody molecules with a unique antigen-binding

site. Initially, the molecules are inserted into the plasma membrane, where

they serve as receptors for antigen. Antigen binding to these receptors

activates the B cells (usually with the aid of helper T cells) to multiply

and mature either into memory cells or into antibody-secreting cells, which

secrete antibodies with the same unique antigen-binding site as the

membrane-bound antibodies.

Each antibody molecule is composed of two identical heavy chains and two

identical light chains. Typically, parts of both the heavy and light chains

form the antigen-binding sites. There are five classes of antibodies (IgA,

IgD, IgE, IgG, and IgM), each with a distinctive heavy chain (a, d, l, g,

and m, respectively). The heavy chains also form the Fc region of the

antibody, which determines what other proteins will bind to the antibody and

therefore what biological properties the antibody class has. Either type of

light chain (k or l) can be associated with any class of heavy chain, but

the type of light chain does not seem to influence the properties of the

antibody.

The complement system cooperates with antibodies to defend vertebrates

against infection. The early components are proenzymes that circulate in the

blood and are sequentially activated in an amplifying series of limited

proteolytic reactions. The most important complement component is the C3

protein, which is activated by proteolytic cleavage and binds to the

membrane of a microbial cell, where it helps to initiate the local assembly

of the late complement components and to induce the phagocytosis of the

microbial cell. The late components form large membrane attack complexes in

the microbial cell membrane and thereby kill the invading microorganism.

>>>>>SNIP

There Are Five Classes of Heavy Chains, Each with Different Biological

Properties 10 , 14

In higher vertebrates there are five classes of antibodies, IgA, IgD, IgE,

IgG, and IgM, each with its own class of heavy chain - a, d, e, g, and m,

respectively. IgA molecules have a chains, IgG molecules have g chains, and

so on. In addition, there are a number of subclasses of IgG and IgA

immunoglobulins; for example, there are four human IgG subclasses (IgG1,

IgG2, IgG3, and IgG4) having g1 , g2 , g3 , and g4 heavy chains,

respectively. The various heavy chains impart a distinctive conformation to

the hinge and tail regions of antibodies and give each class (and subclass)

characteristic properties of its own.

IgM, which has a m heavy chain, is always the first class of antibody

produced by a developing B cell, although many B cells eventually switch to

making other classes of antibody (discussed below). The immediate precursor

of a B cell, called a pre-B cell, initially makes m chains, which associate

with non-light-chain polypeptides (often referred to as surrogate light

chains) and insert into the plasma membrane. As the synthesis of bona fide

light chains increases, these combine with the mu chains, displacing the

surrogate light chains, to form a four-chain IgM molecule (with two m chains

and two light chains), which inserts into the plasma membrane. The cell now

has cell-surface receptors with which it can bind antigen, and at this point

it is called a virgin B cell . Many virgin B cells soon start to produce

cell-surface IgD molecules as well, with the same antigen-binding site as

the IgM molecules.

IgM is not only the first class of antibody to appear on the surface of a

developing B cell, it is also the major class secreted into the blood in the

early stages of a primary antibody response. In its secreted form IgM is a

pentamer composed of five four-chain units and thus has a total of 10

antigen-binding sites. Each pentamer contains one copy of another

polypeptide chain, called a J (joining) chain. The J chain is produced by

IgM-secreting cells and is covalently inserted between two adjacent tail

(Fc) regions ( Figure 23-19 ).

The binding of antigen to the Fab regions of the secreted pentameric IgM

molecule induces the Fc regions to bind to and thereby activate the first

component of the complement system . As we discuss later, when the antigen

is on the surface of an invading microorganism, the resulting activation of

complement unleashes a biochemical attack that kills the microorganism.

Unlike IgM, IgD molecules are rarely secreted by an activated B cell, and

their functions (other than as receptors for antigen) are unknown.

The major class of immunoglobulin in the blood is IgG, which is produced in

large quantities during secondary immune responses. Besides activating the

complement system, the Fc region of an IgG molecule binds to specific

receptors on macrophages and neutrophils. Largely by means of such Fc

receptors, these phagocytic cells bind, ingest, and destroy infecting

microorganisms that have become coated with the IgG antibodies produced in

response to the infection ( Figure 23-20 ). Some white blood cells that

express Fc receptors can also kill IgG-coated foreign eucaryotic cells

without phagocytosing them.

IgG molecules are the only antibodies that can pass from mother to fetus via

the placenta. Cells of the placenta that are in contact with maternal blood

have Fc receptors that bind IgG molecules and mediate their passage to the

fetus. The antibodies are first taken up from the maternal blood by

receptor-mediated endocytosis and then transported across the cell in

vesicles and released by exocytosis into the fetal blood (a process called

transcytosis, discussed in Chapter 13 ). Because other classes of antibodies

do not bind to these receptors, they cannot pass across the placenta. IgG is

also secreted into the mother's milk and is taken up from the gut of the

neonate into the blood.

IgA is the principal class of antibody in secretions (saliva, tears, milk,

and respiratory and intestinal secretions) ( Figure 23-21 ). It is

transported through secretory epithelial cells from the extracellular fluid

into the secreted fluid by another type of Fc receptor that is unique to

secretory epithelia ( Figure 23-22 ).

The Fc region of IgE molecules binds with unusually high affinity ( Ka 1010

liters/mole) to yet another class of Fc receptors. These receptors are

located on the surface of mast cells in tissues and on basophils in the

blood, and the IgE molecules bound to them in turn serve as receptors for

antigen. Antigen binding triggers the cells to secrete a variety of

biologically active amines, especially histamine ( Figure 23-23 ). These

amines cause dilation and increased permeability of blood vessels and are

largely responsible for the clinical manifestations of such allergic

reactions as hay fever, asthma, and hives. In normal circumstances the blood

vessel changes are thought to help white blood cells, antibodies, and

complement components to enter sites of inflammation. Mast cells also

secrete factors that attract and activate a special class of white blood

cells called eosinophils, which can kill various types of parasites,

especially if the parasites are coated with IgE or IgA antibodies.

The properties of the various classes of antibodies in humans are summarized

in Table 23-1 .

Antibodies Can Have Either k or l Light Chains, but Not Both

In addition to the five classes of heavy chains, higher vertebrates have two

types of light chains, k and l, either of which may be associated with any

of the heavy chains. An individual antibody molecule always consists of

identical light chains and identical heavy chains; therefore, its two

antigen-binding sites are always identical. This symmetry is crucial for the

cross-linking function of secreted antibodies. An Ig molecule, consequently,

may have either k or l light chains, but not both. No difference in the

biological function of these two types of light chain has yet been

identified.

The Strength of an Antibody-Antigen Interaction Depends on Both the Number

of Antigen-binding Sites Occupied and the Affinity of Each Binding Site 10 ,

15

The binding of an antigen to antibody, like the binding of a substrate to an

enzyme, is reversible. It is mediated by the sum of many relatively weak

noncovalent forces, including hydrophobic and hydrogen bonds, van der Waals

forces, and ionic interactions. These weak forces are effective only when

the antigen molecule is close enough to allow some of its atoms to fit into

complementary recesses on the surface of the antibody. The complementary

regions of a four-chain antibody unit are its two identical antigen-binding

sites; the corresponding region on the antigen is an antigenic determinant (

Figure 23-24 ). Most antigenic macromolecules have many different antigenic

determinants; if two or more of them are identical (as in a polymer with a

repeating structure), the antigen is said to be multivalent ( Figure 23-25

).

The reversible binding reaction between an antigen with a single antigenic

determinant (denoted Ag) and a single antigen-binding site (denoted Ab) can

be expressed as

The equilibrium point depends both on the concentrations of Ab and Ag and on

the strength of their interaction. Clearly, a larger fraction of Ab will

become associated with Ag as the concentration of Ag is increased. The

strength of the interaction is generally expressed as the affinity constant

( Ka ) (see Figure 3-9 ), where

(the square brackets indicate the concentration of each component at

equilibrium).

The affinity constant, sometimes called the association constant, can be

determined by measuring the concentration of free Ag required to fill half

of the antigen-binding sites on the antibody. When half the sites are

filled, [AgAb] = [Ab] and Ka = 1/[Ag]. Thus the reciprocal of the antigen

concentration that produces half-maximal binding is equal to the affinity

constant of the antibody for the antigen. Common values range from as low as

5 x 104 to as high as 1011 liters/mole. The affinity constant at which an

immunoglobulin molecule ceases to be considered an antibody for a particular

antigen is somewhat arbitrary, but it is unlikely that an antibody with a Ka

below 104 would be biologically effective; moreover, B cells with receptors

that have such a low affinity for an antigen are unlikely to be activated by

the antigen.

The affinity of an antibody for an antigenic determinant describes the

strength of binding of a single copy of the antigenic determinant to a

single antigen-binding site, and it is independent of the number of sites.

When, however, an antigen carrying multiple copies of the same antigenic

determinant combines with a multivalent antibody, the binding strength is

greatly increased because all of the antigen-antibody bonds must be broken

simultaneously before the antigen and antibody can dissociate. Thus a

typical IgG molecule can bind at least 50-100 times more strongly to a

multivalent antigen if both antigen-binding sites are engaged than if only

one site is engaged. The total binding strength of a multivalent antibody

with a multivalent antigen is referred to as the avidity of the interaction.

If the affinity of the antigen-binding sites in an IgG and an IgM molecule

is the same, the IgM molecule (with 10 binding sites) will have a very much

greater avidity for a multivalent antigen than an IgG molecule (which has

two sites). This difference in avidity, often 104 -fold or more, is

important because antibodies produced early in an immune response usually

have much lower affinities than those produced later. (The increase in the

average affinity of antibodies produced with time after immunization, called

affinity maturation, is discussed later.) Because of its high total avidity,

IgM - the major Ig class produced early in immune responses - can function

effectively even when each of its binding sites has only a low affinity.

Antibodies Recruit Complement to Help Fight Bacterial Infections 16

Complement, so called because it complements and amplifies the action of

antibody, is one of the principal means by which antibodies defend

vertebrates against most bacterial infections. Individuals with a deficiency

in one of the central complement components (called C3) are subject to

repeated bacterial infections, just as are individuals deficient in

antibodies themselves.

The complement system consists of about 20 interacting soluble proteins that

are made mainly by the liver and circulate in the blood and extracellular

fluid. Most are inactive until they are triggered by an immune response or,

more directly, by an invading microorganism itself. The ultimate consequence

of complement activation is the assembly of the so-called late complement

components into large protein complexes, called membrane attack complexes,

that form holes in the membrane of a microorganism and thereby destroy the

microorganism.

Because one of its main functions is to attack the membrane of microbial

cells, the activation of complement is focused on the microbial cell

membrane, where it is triggered either by antibody bound to the

microorganism or by microbial envelope polysaccharides, both of which

activate the early complement components . There are two sets of early

components belonging to two distinct pathways of complement activation, the

classical pathway and the alternative pathway. The early components of both

pathways act locally to activate C3, which is the pivotal component of

complement, whose cleavage leads not only to the assembly of membrane attack

complexes but also to the recruitment of various white blood cells ( Figure

23-26 ).

The early components and C3 are proenzymes that are activated sequentially

by limited proteolytic cleavage: the cleavage of each proenzyme in the

sequence activates the component to generate a serine protease, which

cleaves the next proenzyme in the sequence, and so on. Since each activated

enzyme cleaves many molecules of the next proenzyme in the chain, the

activation of the early components consists of an amplifying proteolytic

cascade . Thus each molecule activated at the beginning of the sequence

leads to the production of many active components, including many membrane

attack complexes.

Many of these cleavages liberate a small peptide fragment and thereby expose

a membrane-binding site on the larger fragment, which binds tightly to the

target cell membrane and helps to carry out the next reaction in the

sequence, eventually leading to the formation of membrane attack complexes.

In this way complement activation is confined largely to the particular cell

surface where it began. The larger fragment of C3 is called C3b. It binds

covalently to the surface of a target cell. There it not only acts as a

protease to catalyze the subsequent steps in the complement cascade, but

also is recognized by specific receptor proteins on macrophages and

neutrophils that enhance the ability of these cells to phagocytose the

target cell. The smaller fragment of C3 (called C3a) acts independently as a

diffusible signal that promotes an inflammatory response by encouraging

white blood cells to migrate into the site of infection.

The classical pathway is usually activated by clusters of IgG or IgM

antibodies bound to antigens on the surface of a microorganism. The first

step in this pathway is illustrated in Figure 23-27 . The alternative

pathway, by contrast, is activated by polysaccharides in the cell envelopes

of microorganisms even in the absence of antibody, although activation of

the classical pathway also activates the alternative pathway through a

positive feedback loop. The alternative pathway therefore provides a first

line of defense against infection before an immune response can be mounted,

and it also amplifies the effects of the classical pathway once an immune

response has begun.

Membrane-immobilized C3b, produced by either the classical or alternative

pathway, triggers a further cascade of reactions that leads to the assembly

of membrane attack complexes from the late components ( Figure 23-28 ).

These complexes form in the membrane near the site of C3 activation and have

a characteristic appearance in negatively stained electron micrographs,

where they are seen to form aqueous pores through the membrane ( Figure

23-29 ). For this reason, and because they perturb the structure of the

lipid bilayer in their vicinity, they make the membrane leaky. Small

molecules leak into and out of the cell around and through the complexes

while macromolecules remain inside, so that the cell's normal mechanism for

controlling water balance is disrupted. Water is therefore drawn into the

cell by osmosis, causing it to swell and burst. The process is so efficient

that a very small number of membrane attack complexes (perhaps even one) can

lyse a red blood cell. Even an enveloped virus, which does not have a large

osmotic pressure gradient across its membrane and is therefore not

susceptible to such osmotic lysis, can be destroyed by these complexes,

presumably because they disorganize the viral membrane.

The self-amplifying destructive properties of the complement cascade make it

essential that key activated components be rapidly inactivated after they

are generated to ensure that the attack does not spread to nearby host

cells. Deactivation is achieved in at least two ways. First, specific

inhibitor proteins in the blood terminate the cascade by either binding or

cleaving certain components once they have been activated by proteolytic

cleavage. Second, many of the activated components in the cascade are

unstable; unless they bind immediately to either an appropriate component in

the chain or a nearby membrane, they rapidly become inactive.

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[Guest guest]

I raised my IGs dramatically in 2007 by drinking some raw human breast

milk. It's loaded with them. Humans are universal recipients

of human milk. My donor was my physical therapist, she pumped a little

extra for me and froze it, and I took it home and warmed it. She's

a vegetarian 7th Day Adventist, who has only been with one man (her husband)

and she did a blood test for me before she donated to rule out hepatitis.

She's healthy as a horse, is a triathlete. I did this after careful

consideration and after speaking to the doctors who studied breast milk

extensively in Scandanavia for its immune powers. One of these docs

is now working in New York. The downside is that the milk is also

loaded with stem cells and growth factors, and after I had the milk (not

a lot, mind you, just a few ounces for 2 weeks, maybe 8-10 doses tops;

very sporadic) my WBCs started to climb. It was a risk. I had

been completely stable, no progressive cll, for 4 years, but after I drank

the milk, the WBCs very slowly went up, until now I'm considering my tx.

options. I experimented on myself, like the great scientists used

to. I live with the knowledge that perhaps, if I hadn't drunk the

milk, and therefore hadn't gotten the stem cells and growth factors, I'd

still be stable. Or maybe the WBCs would have climbed anyway, I just

don't know. I'm not suggesting that you do this, but you asked what

raises IGs, and this is it. Anyone with a further interest in this

topic may e-mail me privately, and I'll give you the studies. I know

a man who has basically cured his prostate cancer with human milk, which

he now gets from a milk bank in California. The director of the milk

bank told me that lots of cancer patients drink it (it's pasteurized there,

which does remove some of its good properties). I think it would

be great for other cancers, but maybe not for immune system cancers...........again,

I really don't know.

Ellen R.

P.S. Oh, after I stopped the milk, the IGs plunged again.

It wasn't a permanent fix. But while I was on it, the IGs were much

improved.

jimchiello wrote:

My oncologist informed me this week that my immunoglobulins

are ?mildly low.? She doesn't think I need to do anything about it at this

time, but to let her know if I have recurring infections (sinus, bronchitis,

etc.), at which time she'll recommend beginning IV gammaglobulin treatment,

which generally becomes a ?life-long monthly infusion,? once I start. I

dread the thought of having an infusion every month for the remainder of

my life and am wondering if anyone is aware of an alternative procedure

for increasing one's immunoglobulins. Any suggestions would be welcomed.

[i'm 63, have had CLL for 10 years, am refractory to F and R and just finished

two cycles of bendamustine to clear up adenopathy in my neck. Other than

the low immunoglobulins, all other bloodwork is within normal ranges.]

[Guest guest]

Outrageous

From: Ellen <rhudy@...> Sent: Thu, March 11, 2010 5:49:26 PMSubject: Re: Immunoglobulins

I raised my IGs dramatically in 2007 by drinking some raw human breast milk. It's loaded with them. Humans are universal recipients of human milk. My donor was my physical therapist, she pumped a little extra for me and froze it, and I took it home and warmed it. She's a vegetarian 7th Day Adventist, who has only been with one man (her husband) and she did a blood test for me before she donated to rule out hepatitis. She's healthy as a horse, is a triathlete. I did this after careful consideration and after speaking to the doctors who studied breast milk extensively in Scandanavia for its immune powers. One of these docs is now working in New York. The downside is that the milk is also loaded with stem cells and growth factors, and after I had the milk (not a lot, mind you, just a few ounces for 2 weeks, maybe 8-10 doses tops; very sporadic) my WBCs started to climb. It was a risk. I had been

completely stable, no progressive cll, for 4 years, but after I drank the milk, the WBCs very slowly went up, until now I'm considering my tx. options. I experimented on myself, like the great scientists used to. I live with the knowledge that perhaps, if I hadn't drunk the milk, and therefore hadn't gotten the stem cells and growth factors, I'd still be stable. Or maybe the WBCs would have climbed anyway, I just don't know. I'm not suggesting that you do this, but you asked what raises IGs, and this is it. Anyone with a further interest in this topic may e-mail me privately, and I'll give you the studies. I know a man who has basically cured his prostate cancer with human milk, which he now gets from a milk bank in California. The director of the milk bank told me that lots of cancer patients drink it (it's pasteurized there, which does remove some of its good properties). I think it would be great for

other cancers, but maybe not for immune system cancers..... ......again, I really don't know. Ellen R. P.S. Oh, after I stopped the milk, the IGs plunged again. It wasn't a permanent fix. But while I was on it, the IGs were much improved. jimchiello wrote:

My oncologist informed me this week that my immunoglobulins are ?mildly low.? She doesn't think I need to do anything about it at this time, but to let her know if I have recurring infections (sinus, bronchitis, etc.), at which time she'll recommend beginning IV gammaglobulin treatment, which generally becomes a ?life-long monthly infusion,? once I start. I dread the thought of having an infusion every month for the remainder of my life and am wondering if anyone is aware of an alternative procedure for increasing one's immunoglobulins. Any suggestions would be welcomed. [i'm 63, have had CLL for 10 years, am refractory to F and R and just finished two cycles of bendamustine to clear up adenopathy in my neck. Other than the low immunoglobulins, all other bloodwork is within normal ranges.]

[Guest guest]

who cares?

Re: Immunoglobulins

I raised my IGs dramatically in 2007 by drinking some raw human breast milk. It's loaded with them. Humans are universal recipients of human milk. My donor was my physical therapist, she pumped a little extra for me and froze it, and I took it home and warmed it. She's a vegetarian 7th Day Adventist, who has only been with one man (her husband) and she did a blood test for me before she donated to rule out hepatitis. She's healthy as a horse, is a triathlete. I did this after careful consideration and after speaking to the doctors who studied breast milk extensively in Scandanavia for its immune powers. One of these docs is now working in New York. The downside is that the milk is also loaded with stem cells and growth factors, and after I had the milk (not a lot, mind you, just a few ounces for 2 weeks, maybe 8-10 doses tops; very sporadic) my WBCs started to climb. It was a risk. I had been

completely stable, no progressive cll, for 4 years, but after I drank the milk, the WBCs very slowly went up, until now I'm considering my tx. options. I experimented on myself, like the great scientists used to. I live with the knowledge that perhaps, if I hadn't drunk the milk, and therefore hadn't gotten the stem cells and growth factors, I'd still be stable. Or maybe the WBCs would have climbed anyway, I just don't know. I'm not suggesting that you do this, but you asked what raises IGs, and this is it. Anyone with a further interest in this topic may e-mail me privately, and I'll give you the studies. I know a man who has basically cured his prostate cancer with human milk, which he now gets from a milk bank in California. The director of the milk bank told me that lots of cancer patients drink it (it's pasteurized there, which does remove some of its good properties). I think it would be great for

other cancers, but maybe not for immune system cancers..... ......again, I really don't know.

Ellen R.

P.S. Oh, after I stopped the milk, the IGs plunged again. It wasn't a permanent fix. But while I was on it, the IGs were much improved.

jimchiello wrote:

My oncologist informed me this week that my immunoglobulins are ?mildly low.? She doesn't think I need to do anything about it at this time, but to let her know if I have recurring infections (sinus, bronchitis, etc.), at which time she'll recommend beginning IV gammaglobulin treatment, which generally becomes a ?life-long monthly infusion,? once I start. I dread the thought of having an infusion every month for the remainder of my life and am wondering if anyone is aware of an alternative procedure for increasing one's immunoglobulins. Any suggestions would be welcomed. [i'm 63, have had CLL for 10 years, am refractory to F and R and just finished two cycles of bendamustine to clear up adenopathy in my neck. Other than the low immunoglobulins, all other bloodwork is within normal ranges.]

[Guest guest]

I was simply answering a question that someone asked about raising IGs.

I am not promoting drinking breast milk for cll.

Ellen

pstein22@... wrote:

who

cares?

-----Original

Message-----

From: J Mace

<cll2010jeco >

Sent: Thu, Mar

11, 2010 6:25 pm

Subject: Re:

Immunoglobulins

Outrageous

From:

Ellen <rhudy@...>

To:

Sent:

Thu, March 11, 2010 5:49:26 PM

Subject:

Re: Immunoglobulins

I

raised my IGs dramatically in 2007 by drinking some raw human breast milk.

It's loaded with them. Humans are universal recipients of human milk.

My donor was my physical therapist, she pumped a little extra for me and

froze it, and I took it home and warmed it. She's a vegetarian 7th

Day Adventist, who has only been with one man (her husband) and she did

a blood test for me before she donated to rule out hepatitis. She's

healthy as a horse, is a triathlete. I did this after careful consideration

and after speaking to the doctors who studied breast milk extensively in

Scandanavia for its immune powers. One of these docs is now working

in New York. The downside is that the milk is also loaded with stem

cells and growth factors, and after I had the milk (not a lot, mind you,

just a few ounces for 2 weeks, maybe 8-10 doses tops; very sporadic) my

WBCs started to climb. It was a risk. I had been completely

stable, no progressive cll, for 4 years, but after I drank the milk, the

WBCs very slowly went up, until now I'm considering my tx. options.

I experimented on myself, like the great scientists used to. I live

with the knowledge that perhaps, if I hadn't drunk the milk, and therefore

hadn't gotten the stem cells and growth factors, I'd still be stable.

Or maybe the WBCs would have climbed anyway, I just don't know. I'm

not suggesting that you do this, but you asked what raises IGs, and this

is it. Anyone with a further interest in this topic may e-mail me

privately, and I'll give you the studies. I know a man who has basically

cured his prostate cancer with human milk, which he now gets from a milk

bank in California. The director of the milk bank told me that lots

of cancer patients drink it (it's pasteurized there, which does remove

some of its good properties). I think it would be great for other

cancers, but maybe not for immune system cancers..... ......again, I really

don't know.

Ellen R.

P.S. Oh,

after I stopped the milk, the IGs plunged again. It wasn't a permanent

fix. But while I was on it, the IGs were much improved.jimchiello

wrote:

My

oncologist informed me this week that my immunoglobulins are ?mildly low.?

She doesn't think I need to do anything about it at this time, but to let

her know if I have recurring infections (sinus, bronchitis, etc.), at which

time she'll recommend beginning IV gammaglobulin treatment, which generally

becomes a ?life-long monthly infusion,? once I start. I dread the thought

of having an infusion every month for the remainder of my life and am wondering

if anyone is aware of an alternative procedure for increasing one's immunoglobulins.

Any suggestions would be welcomed. [i'm 63, have had CLL for 10 years,

am refractory to F and R and just finished two cycles of bendamustine to

clear up adenopathy in my neck. Other than the low immunoglobulins, all

other bloodwork is within normal ranges.]