I haven't posted in awhile, I have been very sick. I just got out of the hospital on Friday eveining. I received 2 infusions of Albumin and 2 injections of Epogen.

There have been many discussions in the past that eating eggs and peanut butter made some of us feel better. I understand why now.

Those of us that are hypovolemic are low in volume and blood plasma. Albumin is the protein component in blood that helps build your plasma. So when we eat items high in protein such as eggs, peanut butter it is helping to build our plasma level. There is a dramatic difference in the way I feel after having the infusions.

Epogen also helps with raising the Red Blood Cell count and blood plasma. I am currently fighting the insurance company to get Epogen injections so I can inject at home.

My doctor told me to purchase native whey protein and powdered egg whites and make shakes to drink. I just wanted to pass this information along to others that may be going through this. My order hasn't came in yet, but I will let you know how it goes.

I knew I liked scrambled eggs for a reason. I eat them alot and do feel better in the mornings when I have them for breakfast. I thought it might be the protein but didn't know about the connection to the albumin. Thanks for the great info!

Xena,
Sorry to hear you were in the hospital but am glad you are feeling a bit better now. Thanks for the info - keep us posted.

As a side, any idea is soy protein would do it as well? I can't do whey...

dsdmom.....I will check on the soy protein and get back to you on it.

I've had a really hard time getting my medication regimen adjusted but yesterday I finally found the solution for me. I cut my Midodrine doses in 1/2 and also my Mestinon. This morning my blood pressures are really good. I still take a dramatic drop after standing for 10 min but I can function with that drop. As long as I sit down for a little while for the B/P to recover.

Thanks all, I am so excited that there are still options that work for me and maybe for others also.

Xena--- Thanks for sharing that info. I knew the eggs had to be helping me!

Side note--- I went for a period of a few months when I didn't eat as many eggs. During that time my blood was tested. I was abnormally low on Albumin. The cardiologist just blew off the lab result though.

While both soy and whey proteins provide very good benefits, the benefits are different.

Here are the benefits of Whey Protein

Like soy protein, whey protein has been shown to provide a number of benefits. For example, clinical studies have shown whey protein can:

Act as a natural antibacterial or anti-viral
Assist in maintaining the proper weight
Reduce the symptoms of Chronic Fatigue Syndrome
Reduce liver damage
Improve the function of the immune system
Improve blood pressure
Improve athletic performance
Improve the function of the digestive system
Reduce gastric mucosal injury

Whey protein is the name for a collection of globular proteins that can be isolated from whey, a by-product of cheese manufactured from cow's milk. It is typically a mixture of beta-lactoglobulin (~65%), alpha-lactalbumin (~25%), and serum albumin (~8%), which are soluble in their native forms, independent of pH. Whey has the highest Biological Value (BV) of any known protein.

Soy protein DOES NOT have the albumin & globulin components.

If you are considering purchasing whey protein to build blood plasma and improve B/P make sure you purchase:

Microfiltered whey isolate

Microfiltered whey isolate is the most undenatured form of whey. Its native protein structures are kept intact to a large degree. It has 90% higher protein content. It is virtually lactose, fat and cholesterol free..


Micro- (and ultra-) filtered whey isolate is the protein with the highest biological value of all proteins. Its characteristics are:


It stimulates the production of glutathione

It strengthens the immune system

It has antioxidant and anti-cancer properties

I returned to the doctor this past Wednesday and he said the Epogen really didn't help me. It was the Albumin, my hemoglobin was up and I am feeling so much better. I will now be going to the hospital on an out-patient basis to get Albumin infusions, my first one is this Wednesday. Then we are going to recheck my blood plasma volume again.

I still have crashes, I had one this past Sunday. We just started IV fluids and ran in 4 liters. I have a month supply delivered to my house at a time.

I was also started on DDVAP, it seems to be working well. It is a man-made vasopressin, it is suppose to make you urinate less. If we urinate less then we hold on to more fluids.

I will try and keep everyone updated on my progress, I think this might help others.

Xena,
You are very caring and kind AND brave. We hope these treatments help YOU and many more. Take care and thanks for the info.

Xena,
That's interesting that you're on DDAVP. I tried to get my doctor to prescribe it but he wouldn't since it could cause water intoxication. I read a lot about this drug since I thought I might have diabetes insipidus (water diabetes) for a while because of my constant thirst and urination. My doctor didn't seem to think that I had it.

How long have you been on the DDAVP now and how are you feeling? Are you using it in order to retain more fluid?

Erin

Xena--
has your doctor said whether you'll need albumin injections for life? Or is his strategy to up the albumin now through injection, while having you change your diet so that you can in the future have an adequate albumin level on your own?

Also, do you happen to know just how low your albumin was? Mine was abnormally low last time but I wonder at what point it's necessary for injection.

Erin......I have been on the DDVAP for 3 weeks now. The plan is to help me hold on to more fluids and I do believe it is working. My fluids used to just go straight through me. But now I'm holding on to more of them and my urine is concentrated.

nitekitty..... The plan for now is to increase my blood plasma volume, red blood cell count, hemoglobin and hematocrit with the albumin transfusions. I don't know how long I will be getting them. My albumin was 4, which is within normal range but my doctor would like it to be over 5.

If we can get my levels to come up then I think we are going to watch and wait to see how long it takes for it to go back down.
I had my second transfusion last Wednesday and I'm still running a fever and feel like I have the flu. I hope this goes away soon.

cool. thanks!

Funny. I believe my last albumin reading was 3.6. My cardiologist completely blew it off.

Sorry, I'll have to edit the formatting when I get a chance.
My cardiologist recommended against the albumin shots. So I did some digging and found a bunch of info. Weighing pros and cons. A lot of confusing conclusions, or no set ones it seems. Other than certain combos of large doses of amino acids increase Albumin synthesis.
See below.
May be easier to just click on the links and go directly to them then to try to read the terrible formatting on my post.



http://www.mercola.com/article/colds/hygiene_systems.htm

Doctors can infuse albumin into the body, and may do so for patients suffering from cancer and other serious diseases associated with low albumin. Unfortunately, "albumin shots" don't work. When albumin is infused into the body, it upsets the carefully calibrated concentration of proteins (osmotic pressure). The liver attempts to get the concentration back to normal levels by halting its own production of albumin. And if that doesn't work quickly enough, it starts destroying albumin in a frantic attempt to get things back to normal in the body. The liver doesn't understand that the extra albumin may be helpful; it only knows that something is out of balance, and balance must be restored.

[I didn't understand this because then how is it good for "cancer and other serious diseases"? And just what is a "serious disease"?]


http://www.4um.com/tutorial/currents/albumin.htm

What's all this fuss about Albumin?
By Pat Neligan 1998


--------------------------------------------------------------------------------

All tutorials located on this site are the property of Patrick Neligan and are for personal study purposes only. They are not peer reviewed and no responsibility is taken for inaccuracies. These tutorials must not be reproduced without permission or used in any other publication.

Contents

What is albumin?
Why is it important?
What causes serum albumin to decrease?
Consequences of decreased plasma albumin
Disease processes associated with Hypoalbuminaemia
Albumin as a prognostic index
Correcting Hypoalbuminaemia
The recent fuss about albumin
Key Points

--------------------------------------------------------------------------------

What is albumin?

Single polypeptide, 585 amino acids.
MW 66,248; IgG is 150,000
Highly soluble
Strong negative charge -17
Manufactured in the liver @ 9-12g/day
No storage, no reserve
Rate of production controlled by changes in colliod osmotic pressure and osmolality of extravascular liver space.
Production can only increase by a factor of 2 or 3.
Synthesis is increased by insulin / T4 or cortisol.
Catabolism is at a rate of 9 - 12 g/day by pinoctosis in cells adjacent to the vascular endothelium.
Albumin is not catabolised in starvation.
Albumin is an intravascular protein with a concentration of approx 40 g/l.
Ablumin also exists in the extavascular [interstitial] space. In fact the total extravascular albumin exceeds the total intravascular amount by 30%.
Albumin leaves the circulation via interstitium to lymph system back to the circulation via thoracic duct.
Circulation t1/2 is 16 -18 hours.
4 - 5% of total intravascular albumin extravascates per hour: this rate of movement is known as the Transcapillary Escape Rate (TER), and this is determined by:
Capillary and interstitial free albumin concentration.
Capillary permeability to albumin.
Movements of solvent / solute.
Electrical charges across the capillary wall.
Lymph protein content is 80% that of plasma.
Measurement of serum albumin is by using a dye binding technique using bromocresol green or purple: this tends to overestimate albumin concentration when the serum albumin is low - especially when there is increased levels of a or b globulin. Because of this overestimation, is rare to see a serum albumin < 10 - 15g/l.

BCP is more sensitive than BCG.


--------------------------------------------------------------------------------


Why is albumin important?
1. Binding and transport.

2. Maintenance of colloid osmotic pressure.

3. Free radical scavenging.

4. Platelet function inhibition and antithrombotic effects.

5. Effects on vascular permeability.

Binding and transport

There are actually four binding sites on albumin and these have varying specificity for different substances.

Competitive binding of drugs may occur at the same sit or at different sites (conformational changes) [eg. warfarin and diazepam].

The drugs that are important for albumin binding are: warfarin, digoxin, NSAIDS, midazolam, thiopentone.

The relevence of a low albumin and drug binding is unknown.

Osmotic pressure

Albumin is responsible for 75 - 80 % of osmotic pressure.

Starling's equation: Transcapillary Flow = k [(Pcap + p i) - (Pi + p cap )]

Remember that albumin is the main protein both in the plasma and in the interstitium and it is the COP gradient rather than the absolute plasma value that is important: this is what distinguishes hypoalbuminaemia derived from redistribution (capillary leak) from that of pure full body deficiency.

Free Radicals

Albumin is a major source of sulphydryl groups, these "thiols" scavenge free radicals (nitrogen and oxygen species).

Albumin may be an important free radical scavenger in sepsis.

Anticoagulant effects

The anticoagulant and antithrombotic effects of albumin are poorly understood this may be due to binding nitric oxide radicals inhibiting inactivation and permitting a more prolonged antiaggregatory effect.

In diabetes, glycosylated albumin may increase the incidence of thrombotic events and atherosclerosis.

Capillary Membrane Permeability

In sepsis there is an increased rate of albumin loss into the tissues - this is probably related to increased capillary membrane permeability.


--------------------------------------------------------------------------------

What causes serum albumin to decrease?

Plasma albumin concentation = intravascular albumin mass / plasma volume

Decreased plasma albumin:

1. Decreased synthesis.

2. Increased catabolism [ very slow ]

3. Increased loss:

Nephrotic syndrome
Exudative loss in burns
Haemorrhage
Gut loss
4. Redistribution:

Haemodilution
Increased capillary permeability (Increased interstitial albumin)
Decreased lymph clearance.

--------------------------------------------------------------------------------

Consequences of decreased plasma albumin

1. Decreased ligand binding.

2. Decreased plasma colloid pressure: decreased colloid oncotic pressure, and oedema formation.

The formation of oedema is determined by:

The rate of fluid flux

The clearance of fluid by lymphatics.

In critical illness, there is a stronger correlation between colloid oncotic pressure and Total protein than with albumin.
In these patients the decreased albumin is compensated for by an increase in acute phase proteins.
Unquestionably there is increased leakage of albumin and this drags fluid with it .
Lymphoid function is important - if it is overwhelmed by increased capillary permeability or fluid flux then oedema will occur.
It is likely that lymphoid dysfunction plays a significant role in oedema formation in critical illness. ?? do free radicals cause this lymphoid dysfunction?
Bottom line: low serum albumin does not necessarily mean low plasma oncotic pressure.


--------------------------------------------------------------------------------


Disease processes associated with Hypoalbuminaemia
Malnutrition
Serum albumin does not appear to decrease in starvation.

The body maintains the serum albumin at the expense of muscular protein:

Decreased synthesis increased redistribution decreased catabolism.

Bottom line: decreased albumin in adults is a marker of associated disease not a feature of isolated protein-energy malnutrition.

Liver Dysfunction
Albumin is a poor marker of liver dysfunction; Prothrombin time is more reliable.

Renal disease
Albumin loss occurs in nephropathies (nephrotic syndrome).

There is a small loss of albumin in dialysis circuits.

Pre-Eclampsia
In normal pregnancy there is an increase in plasma volume. In PET there is a paradoxical decrease in plasma volume and capillary leak syndrome.

Stress response

Interleukins cause a marked decease in synthesis of plasma proteins other than albumin.

In fact Albumin and Transferrins decrease in the stress response, a process often termed "negative acute phase proteins".

IL6 directly decreases the expression of albumin messenger RNA.

Overall, the picture in the stress response is:

1. Initial decrease in albumin associated with increase in acute phase proteins.

2. Subsequent global increase in hepatic protein synthesis; including albumin.

Burns

There is massive protein loss from the burn site & increased vascular permeability & decreased albumin synthesis & protein losing nephropathy.

Trauma

Increased redistribution and transcapillary escape of albumin.

Surgery

Decreased serum albumin preoperatively is an independent indicator of poor outcome.

Sepsis

SIRS - associated with increased capillary permeability, due to the effects, amongst others, of bacterial endotoxin and cytotoxic T cells.

In sepsis there is a profound reduction in plasma albumin associated with marked fluid shifts.

Albumin as a prognostic index

Low albumin is associated with dozens of diseases.

Controversy regarding whether or not albumin is a good indicator of prognosis in critical illness. One recent study suggests:

"In patients with acute and chronic illness serum albumin concentration is inversely related to risk of death. A systematic review of cohort studies meeting specified criteria estimated that for each 2.5 g/l decrement in serum albumin concentration the risk of death increases by between 24% and 56%."

Journal of Clinical Epidemiology 1997; 50; 693-703.

Following serum albumin levels may be of value - intial decrease associated with deterioration, later gradual increase signifies recovery in process.

Correcting Hypoalbuminaemia

Low serum albumin concentrations are the consequence of a disease process and successful treatmen of the underlying disease should result in a gradual return to normal serum albumin concentrations.

Studies have not shown that the theraputic "normalisation" of albumin levels in critically ill patients is beneficial. Indeed the Cochrane group's recent "meta" analysis suggests a higher mortality rate in critically ill patients treated with albumin.

Previous strategies have involved administering albumin to decrease the loss of intravascular volume by enhancement of collloid oncotic effect. However, in sepsis, 2/3 of administered albumin has been shown to extravascate within 4 hours of administration.

Debunked Myths (by randomised controlled trials):

The use of 20% albumin and frusemide to reduce oedema in SIRS.
The administration of albumin following paracentesis for ascites.
The use of replacement albumin in nephrotic syndrome.
It is very questionable whether or not albumin should remain the colloid of first choice in paediatric practice.

Commercially available albumin is fractionated in ethanol and purified and heat treated for 10 hours at 60 degrees celcius.

This process:

Probably alters the charge on albumin - making it more permeable.

Contains significant quantities of residual ions - aluminium and vanadium.


--------------------------------------------------------------------------------


Recent controversies
Cochrane Injuries Group Albumin Reviewers

BMJ

1998;317:235-240 ( 25 July )
Objective:

To quantify effect on mortality of administering human albumin or plasma protein fraction during management of critically ill patients.

Design: Systematic review of randomised controlled trials comparing administration of albumin or plasma protein fraction with no administration or with administration of crystalloid solution in critically ill patients with hypovolaemia, burns, or hypoalbuminaemia.


Subjects: 30 randomised controlled trials including 1419 randomised patients.


Main outcome measure: Mortality from all causes at end of follow up for each trial.

Key messages

Human albumin solution has been used in the treatment of critically ill patients for over 50 years
Currently, the licensed indications for use of albumin are emergency treatment of shock, acute management of burns, and clinical situations associated with hypoproteinaemia
Our systematic review of randomised controlled trials showed that, for each of these patient categories, the risk of death in the albumin treated group was higher than in the comparison group
The pooled relative risk of death with albumin was 1.68 (95% confidence interval 1.26 to 2.23) and the pooled difference in the risk of death was 6% (3% to 9%) or six additional deaths for every 100 patients treated
We consider that use of human albumin solution in critically ill patients should be urgently reviewed


Readers' criticisms:

Neil Soni, Consultant in intensive care.
"I was asked to review the Cochrane Injuries Group's paper for the BMJ. I quote from my covering letter: "It should not be published."
Altogether 30 randomised studies with population sizes ranging from 12 to 219 (over half had fewer than 30 patients) were assessed, with a total of 1419 patients. No account taken of the purpose, design, or specific end points of the studies.
The end point of the review mortality was not an end point in most studies, many of which were over less than five days.
Most deaths occurred outside the study times.
Variables ignored included age, medical conditions, severity of disease, dose of albumin, mode of administration, and attributable mortality of the states of disease that were treated.
The evolution of fluid management between the 1970s and now was also dismissed. Common factors were randomised controlled trials that compared administration of albumin with no administration or administration of crystalloid, and, of course, the term "critically ill."
The message, presented with the combined weight of Cochrane and the BMJ, is that albumin, whether used in neonates or adults, whether for volume replacement or the support of biochemical variables, whether given intraoperatively as a single dose or long term over days or weeks, is potentially hazardous.
Practice is already changing. Change, with its potential hazards, is entirely justifiable if the evidence is powerful enough to decree change but it is not.
The review is a tribute to an association of key words and modern computer technology, and the results are serendipitous and amount to evidence that is at best circumstantial.
The authors talk of totality of available evidence, but is that totality synonymous with adequacy?
Evidence should lead to change, but surely there is a responsibility to ensure that the weight of evidence published by august bodies is adequate to justify that change.
Does the responsibility lie with the researcher, the reviewer, or the journal? When does a strongly negative peer review become negative? Surely negative reviews should be acknowledged by the journal, otherwise publication fraudulently implies positive peer review.
Finally, are these review methods valid? It is time to define their value because I believe that otherwise such studies will damage the credibility of not only the methods used, which are potentially powerful and useful, but also of the journals that carry them."
Authors Response:

"On the basis of our systematic review of randomised trials we concluded that "there is no evidence that albumin administration reduces mortality in critically ill patients, and a strong suggestion that it may increase mortality." We read with anticipation the letters in response to our review, but note with concern that none of the correspondents provide any evidence that albumin is beneficial in critically ill patients, in which case our conclusions stand."

Ian Roberts

, Director, Child Health Monitoring Unit.
Department of Epidemiology and Public Health, Institute of Child Health, London WC1N 1EH
--------------------------------------------------------------------------------


KEY POINTS
What is albumin?

Albumin is an important intravascular and extravascular protein; it contributes strongly to the maintenance of colloid osmotic pressure.

Why is it important?

Binding and transport, osmotic pressure, free radical scavenging, platelet function inhibition and antithrombotic effects.

What causes serum albumin to decrease?

Decreased synthesis, increased catabolism, increased loss & redistribution.

Consequences of decreased plasma albumin
1. Decreased ligand binding.

2. Decreased plasma colliod pressure

Disease processes associated with Hypoalbuminaemia
In critical illness, there is a stronger correlation between colloid oncotic pressure and Total protein than with albumin.

Albumin decreases in burns, liver disease, renal disease, pre-eclampsia, stress and sepsis.

Albumin as a prognostic index
Serum albumin concentration in critical illness is inversely related to the risk of death.

Correcting Hypoalbuminaemia
The "normalisation" of plasma albumin concentrations has nor been shown to improve outcome in critical illness and in many of the traditional theraputic roles of albumin

The recent fuss about albumin
The Cochrane report in the BMJ in July 1998 suggested that treatment with albumin was related to a 6% excess of deaths above control. Although this study was flawed in many ways, it has illustrated what many have believed for some time: that theraputic albumin therapy has little role in the management of most patients. Nevertheless, where albumin's use is well defined - in paediatrics / burns, it's abandonment does not appear justified at this time.


--------------------------------------------------------------------------------


http://www.emedicine.com/Med/topic1116.htm

Serum albumin levels are dependent on the rate of synthesis, the amount secreted from the liver cell, the distribution in body fluids, and the level of degradation. Hypoalbuminemia results from a derangement in one or more of these processes.

Synthesis

Albumin synthesis begins in the nucleus, where genes are transcribed into messenger ribonucleic acid (mRNA). The mRNA is secreted into the cytoplasm, where it is bound to ribosomes, forming polysomes that synthesize preproalbumin. Preproalbumin is an albumin molecule with a 24 amino acid extension at the N terminus. The amino acid extension signals insertion of preproalbumin into the membrane of the endoplasmic reticulum. Once inside the lumen of the endoplasmic reticulum, the leading 18 amino acids of this extension are cleaved, leaving proalbumin (albumin with the remaining extension of 6 amino acids). Proalbumin is the principal intracellular form of albumin. Proalbumin is exported to the Golgi apparatus, where the extension of 6 amino acids is removed prior to secretion of albumin by the hepatocyte. Once synthesized, albumin is secreted immediately; it is not stored in the liver.

Causes
Hypoalbuminemia can result from decreased albumin production, defective synthesis because of hepatocyte damage, deficient intake of amino acids, increased losses of albumin via GI or renal processes, and, most commonly, acute or chronic inflammation. Some of the many causes are as follows:



Protein malnutrition: Deficient protein intake results in the rapid loss of cellular ribonucleic acid and disaggregation of the endoplasmic reticulum–bound polysomes and, therefore, decreased albumin synthesis. Albumin synthesis can decrease by more than one third during a 24-hour fast. Albumin synthesis may be stimulated by amino acids produced in the urea cycle, such as ornithine.
Defective synthesis: In patients with cirrhosis, synthesis is decreased because of the loss of hepatic cell mass. Also, portal blood flow is often decreased and poorly distributed, leading to maldistribution of nutrients and oxygen. The flow of substrate may affect certain functions of the liver, including protein synthesis, which is decreased in patients with cirrhosis who lack ascites. Albumin synthesis may actually increase in patients with cirrhosis who have ascites, possibly because of a change in hepatic interstitial colloid levels, which may act as an overriding stimulus for albumin production. Although synthesis is increased, the concentration of albumin is decreased because of dilution.
Extravascular protein loss

Nephrotic syndrome: This can produce hypoalbuminemia by massive proteinuria, with 3.5 g or more of protein lost within 24 hours. Albumin is filtered by the glomerulus and catabolized by the renal tubules into amino acids that are recycled. In patients with chronic renal disease, in whom both glomerular and tubular diseases are present, excessive protein filtration may lead to both increased protein loss and increased degradation. Only at higher rates of albuminuria (>100 mg/kg/d) and only when the diet is adequate is albumin synthesis increased.
Protein-losing enteropathy: Under normal conditions, less than 10% of the total albumin is lost through the intestine. This fact has been confirmed by comparing albumin labeled with chromium-51, which helps measure intestinal losses, to albumin labeled with iodine-125, which helps measure overall degradation. In cases of protein-losing enteropathy related to bacterial overgrowth, hypoalbuminemia is exacerbated by peripheral factors that inhibit albumin synthesis by mechanisms similar to those observed with burns, trauma, infection, and carcinoma.
Extensive burns: The skin is the major site for extravascular albumin storage and is the major exchangeable albumin pool needed to maintain plasma levels. Hypoalbuminemia results from direct losses of albumin from tissue damage, from compromised hepatic blood flow due to volume loss, and from inhibitory tissue factors (eg, tumor necrosis factor, interleukin-1, interleukin-6) released at the burn sites.
Lymphatic blockage or mucosal disease: Diseases that result in protein loss from the intestine are divided into 2 main types. The first is lymphatic blockage, which can be caused by constrictive pericarditis, ataxia telangiectasia, and mesenteric blockage due to tumor. The second is mucosal disease with direct loss into the bowel, which is observed with (1) inflammatory bowel disease and sprue and (2) bacterial overgrowth, as in blind loop syndrome after intestinal bypass surgery.
Hemodilution: In the presence of ascites from any cause, the serum albumin level is not a good index of the residual synthetic capacity of the liver unless actual radioisotopic measurements of production are used. With ascites, synthesis may be normal or even increased, but serum levels are low because of the larger volume of distribution. This is true even for ascites due to cirrhosis.
Congestive heart failure: The synthesis of albumin is normal in patients with congestive heart failure. Hypoalbuminemia results from an increased volume of distribution.

Oncotic pressure increase: The serum oncotic pressure partially regulates albumin synthesis. The regulation site may be the oncotic content in the hepatic interstitial volume because albumin synthesis is inversely related to the content of this volume. Conditions that increase other osmotically active substances in the serum tend to decrease the serum albumin concentration by decreasing synthesis. Examples include elevated serum globulin levels in hepatitis and hypergammaglobulinemia.
Acute and chronic inflammation: Albumin levels that are low because of acute inflammation should normalize within weeks of resolution of the inflammation. Persistent hypoalbuminemia beyond this point should prompt an investigation for an ongoing inflammatory process. The cytokines (TNF, IL-6) released as part of the inflammatory response to physiologic stress (infection, surgery, trauma) can decrease serum albumin by the following mechanisms:

Increased vascular permeability (allowing albumin to diffuse into the extravascular space)
Increased degradation
Decreased synthesis (among other mechanisms, by activating TNF-a, which decreases transcription of the albumin gene)
Lab Studies

Clinical suspicion of the underlying disease process should guide appropriate laboratory studies, some of which are outlined below.

Malnutrition: Lymphocyte count and blood urea nitrogen levels are decreased. Transferrin, prealbumin, and retinol-binding protein have shorter half-lives compared with albumin and better reflect short-term changes in nutritional status than albumin, which has a long half-life.
Inflammation: C-reactive protein levels and increased erythrocyte sedimentation rate are elevated.
Nephrotic syndrome: The 24-hour urine collection contains more than 3 g of protein in 24 hours.
Cirrhosis: Liver function test findings (transaminase levels) may be elevated or normal in patients who are cirrhotic. Coagulation studies may be abnormal. Cirrhosis has numerous potential etiologies, and more specific studies, such as hepatitis screening, may be needed.
Malabsorption: Fecal fat studies including Sudan qualitative stain for fat, 72-hour quantitative fecal fat collection, and fecal a-1-antitrypsin clearance are needed.
Serum protein electrophoresis results help to determine if hypergammaglobulinemia is present.
None of the various correction factors for determining the effects of hypoalbuminemia on the plasma calcium concentration has proven reliable. Corrected calcium (mg/dL) is equal to measured total calcium (mg/dL) plus 0.8 (average normal albumin level of 4.4 minus serum albumin [g/dL]). The only method of identifying true (ionized) hypocalcemia in the presence of hypoalbuminemia is to measure the ionized fraction directly.
Elderly patients living in nursing homes or other institutionalized settings who have hypoalbuminemia should be evaluated for treatable co-morbid conditions contributing to the malnutrition (eg, medications causing decreased appetite, thyroid dysfunction, diabetes, malabsorption, depression, cognitive impairment).

CONCLUSION

Hypoalbuminemia is a common phenomenon in patients with serious illness. Treatment should focus on the underlying cause rather than simply replacing albumin. Exogenous albumin is not used for the purpose of raising serum albumin levels.
Indications and the use of albumin administration in critically ill patients is an area of controversy; studies to clarify these issues are ongoing.

Although prior meta-analysis of small studies suggested that albumin infusions may be harmful (increasing the mortality rate by 6% as compared with crystalloid), a large multicenter clinical trial (SAFE) documented that, except in patients with neurotrauma, albumin infusions did not measurably affect outcome.1 In patients with neurotrauma, these trials found a small, but significant, increase in mortality as compared with crystalloid therapy.
Outcomes are similar regardless of baseline serum albumin concentration; albumin administration for patients with hypoalbuminemia has no added benefit. Based on these studies of patients with septic shock, the benefit of colloid versus crystalloid administration for critically ill patients is not clearly demonstrated. Furthermore, the relative amount of albumin that can be effectively replenished by infusion is minimal, considering the normal albumin turnover rate.
These findings are in contrast to prior studies that also found no difference or increased mortality among those receiving albumin. Preliminary studies, including a favorable study by Dubois (2006), examined the effect of albumin on organ function in critically ill patients, but additional work is needed in this area.2
Limited indications for albumin supplementation exist, and considerable clinical judgment is required when albumin is administered. Albumin has been used as one part of regimens designed to prevent hepatorenal syndrome in patients with cirrhosis; however, this is controversial and survival benefit has not been clearly established. However, in general, albumin is not given specifically to treat hypoalbuminemia, which is a marker for serious disease.
Like crystalloids, colloids produce a dilutional effect on hemoglobin and clotting factors. Clinicians need to monitor the appropriate parameters to safeguard against iatrogenic complications.
Considering fluid resuscitation more generally, recent investigation found that 6% hydroxyethyl starch used for resuscitation in patients with severe sepsis was associated with a significant increase in acute renal failure, calling this approach into question.
The most effective method of minimizing hypoalubinemia and restoring serum oncotic pressure is by creating a positive nitrogen balance. This is usually accomplished by enteral protein feeding and reversing the inflammatory state, if present. Clearly, those patients with nephrotic syndrome need the nephrosis treated as a primary problem. The importance of enteral nutrition as an early and continued treatment for hypoalbuminemia cannot be overemphasized.

http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1174225


Albumin

synthesis was measured in the isolated perfused rat liver by using the livers of both well-fed and starved rats. Starvation markedly decreased albumin synthesis. The livers from starved rats were unable to increase synthesis rates after the addition to the perfusates of single amino acids or the addition of both glucagon and tryptophan. Arginine, asparagine, isoleucine, leucine, lysine, methionine, phenylalanine, proline,threonine, tryptophan and valine, added together to ten times their normal peripheral blood concentrations, restored synthesis rates to normal. The plasma aminogram (i.e. the relative concentrations, of amino acids) was altered by depriving rats of protein for 48h. The use of blood from the deprived rats as perfusate, instead of normal blood, decreased albumin synthesis rates significantly by livers obtained from well-fed rats.

The addition of single amino acids, including the non-metabolizable amino acid, a-aminoisobutyric acid, to the above mixture increased albumin synthesis rates to normal values. It is concluded that amino acids play an important role in the control ofalbumin synthesis and that more than one mechanism is probably involved.

---------------

The addition of lysine, glycine, the 11 amino acids given together or a combination of methionine, lysine and threonine significantly increased urea synthesis. However, theaddition of tryptophan, isoleucine and x-aminoisobutyric acid had no effect on urea production despite an increase in albumin synthesis rates.



http://jn.nutrition.org/cgi/reprint/98/4/395.pdf



http://ajpendo.physiology.org/cgi/content/abstract/252/3/E291
Regulation of albumin synthesis by hormones and amino acids in primary cultures of rat hepatocytes
S. M. Hutson, C. Stinson-Fisher, R. Shiman and L. S. Jefferson


Culture conditions necessary for optimizing albumin secretion were studied in rat hepatocytes maintained in a chemically defined, serum-free medium. Amino acid analysis of the culture medium, which was based on a 1:1 mixture of Ham's F12ulbecco's modified Eagle's medium (unsupplemented medium), revealed that certain essential amino acids were depleted from this medium over a 24-h incubation. Rates of albumin secretion were significantly higher and better maintained when the medium was supplemented with additional amino acids (supplemented medium). Moreover, selective removal of an essential amino acid resulted in an immediate decrease in total protein and albumin synthesis and after 48 h a further selective decrease in albumin synthesis. Linear rates of albumin secretion were observed over a wide variety of experimental conditions, but secretion was not strictly proportional to cell number. Maximal rates of secretion were obtained at plating densities of 2-3 X 10(6) cells/60 mm culture dish. Albumin secretion also increased with time in culture reaching a maximum on days 3 and 4. When added singly, either insulin or dexamethasone increased rates of albumin secretion in a dose-dependent manner, but both hormones and an adequate supply of amino acids were necessary for maximal rates of secretion as well as long-term maintenance of the hepatocytes (greater than 3-4 days). In the presence of dexamethasone the dose-response curve for insulin was shifted toward physiological insulin concentrations. Changes in rates of albumin secretion in response to added hormones in supplemented media were found to parallel changes in albumin synthesis and relative amounts of albumin mRNA. Changes in gene transcription were probably involved.

http://bja.oxfordjournals.org/cgi/content/full/85/4/599

This review will examine the role of serum albumin in health and critical illness. It will also review aspects of the physiology of this protein that may be expected to lead to significant dysfunction in critical illness. Finally, the case for and against the use of exogenous albumin in the management of critically ill patients will be discussed.

Hi Xena,

Sorry to hear you have been doing it so tough but thank you for the post.

I've been eating 2 eggs every 2nd day for some years now. I didn't feel 'right' (well, at least 'right' for me) unless I had my eggs. I found your post really interesting.

Strangely I can rarely tolerate them in the morning but can eat them for dinner. I have no idea what that is about but the more I realize that part of my body is trying to do the right things by me by prompting me to eat certain things the more I've come to believe this sort of stuff (like the benefits of eggs) is just not 'all in the head' but rather my mind/body prompting me.

Now, if only I could explain my on/off addiction to chocolate. I will go for days eating it and then it really starts to cause my skin and inside my mouth to burn and I will stop eating it and not miss it -- I forget about it. Then suddenly the craving becomes overwhelming and I'm eating it again. This has happened over and over again. I think if chocolate was a 'true addiction' I'd be eating it all the time but I stop and start on it and it's not emotionally driven. It's something my body seems to need at times.

I'm sure there is something in chocolate. I'm going to try and get hold of the 'purer chocolate' and learn to cook with it. The stuff without any artificial/or natural flavours or sugar added. I've got a hunch that the basic chocolate (it comes from some weird plant -- called the Theobroma cacao -- but don't quote me on that as my source may not be correct, I havn't checked it out yet)...well, I have this feeling that there is something in it that does me good.