Reading...
Play button
Play button
Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
158 Cards in this Set
- Front
- Back
|
Name functions of blood
|
Distribution (of O2, nutrients, wastes, and hormones.
Regulation (of temperature, pH, and fluid volume) Protection (from fluid loss (clotting), infection (immunity)) |
|
|
What does plasma contain?
|
Water, proteins, hormones, nutrients, electrolytes (What plants crave! lol j/k)
|
|
|
What are formed elements?
|
Red cells, white cells, and platelets
|
|
|
What is plasma?
|
Fluid fraction of blood
|
|
|
What is serum?
|
Fluid fraction of blood after coagulation
|
|
|
Plasma contains over _____ proteins.
Constitutes ____ of total blood volume. |
300
~7% |
|
|
Most plasma proteins have a specific biochemical role; what are they?
|
Maintenance of oncotic pressure.
Transport Defense reactions Coagulation and fibrinolysis |
|
|
What plasma proteins appear as a result of disease?
|
Intracellular enzymes and tumor markers
|
|
|
Where is albumin produced?
|
In the liver
|
|
|
Albumin accounts for what % of total plasma protein?
|
~50%
|
|
|
Albumin represents how much of body weight?
|
4-5 g/kg of body weight
|
|
|
How much albumin is synthesized daily?
|
14-15g
|
|
|
How long is the half-life of albumin?
|
~20 days
|
|
|
Name the functions of albumin (broad).
|
Maintains oncotic pressure.
Transport Free radical scavenging Buffer |
|
|
What does albumin transport?
|
Fatty acids (FFAs)
Unconjugated bilirubin Metal ions: Ca2+, Fe2+, and Cu2+ Drugs, thyroid, and steroid hormones |
|
|
Albumin is an important free radical scavenger in _____. Why?
|
Sepsis
Due to sulphydryl groups |
|
|
What is hypoalbuminemia?
|
Low blood albumin level
|
|
|
Hypoalbumninemia can be caused by...
|
Liver disease
Starvation, malnutrition Excess excretion by kidneys (i.e. nephrotic syndrome) Sepsis |
|
|
What is hyperalbuminemia?
What is it typically a sign of? |
High blood albumin level.
Severe dehydration |
|
|
In capillaries, what direction does fluid move?
|
From intravascular to interstitial space
|
|
|
Hydrostatic pressure is highest in the arteriorlar capillary or venous capillary?
|
Arteriorlar is highest with ~37 mm Hg
Venous is lowest with ~17 mm Hg |
|
|
In the arteriorlar capillaries, water enters or leaves the capillary? Why?
|
Water leaves the arteriorlar capillaries, because the hydrostatic pressure is higher than the oncotic pressure
|
|
|
How can albumin transport hydrophobic molecules, yet still be water soluble?
|
It has hydrophobic clefts, but has hydrophillic properties (i.e. COO-)
|
|
|
In venous capillaries, water enters or leaves the capillary? why?
|
Enters the venous capillaries, because the hydrostatic pressure is lower than the oncotic pressure.
|
|
|
What is the main force of bringing water back from tissues?
|
The osmotic pressure of plasma proteins, or oncotic pressure
|
|
|
What is kwashiorkor?
|
childhood protein malnutrition
|
|
|
What causes kwashiorkor?
|
Malnutrition (particularly protein deficiency). Plasma protein concentration is decreased.
This leads to decreased osmotic pressure of blood. Ultimately, leads to fluid being unable to be brought back in to the blood and accumulates in the interstitial space. EDEMA |
|
|
What is the hallmark symptom of kwashiorkor, and why is does this happen?
|
Distained bellies; due to fluid accumulation in extravascular tissues
|
|
|
What is nephrotic syndrome?
|
Damage to glomerular basement membrane in nephritis
|
|
|
What results due to nephrotic syndrome?
|
Leak of albumin
|
|
|
If loss of albumin exceeds synthetic capacity of liver, what happens?
|
Hypoalbuminemia
Leads to peripheral (leg) edema and pulmonary edema (breathlessness) |
|
|
Increased glomerular damage results in loss of which large proteins?
|
Immunoglobulins and complement
|
|
|
What is the classic triad of nephrotic syndrome?
|
Hypoalbuminemia
Proteinuria Edema |
|
|
What does haptoglobin bind to?
|
Hemoglobin
|
|
|
What are the functions of haptglobin?
|
Inhibits hemoglobins oxidative activity
Prevents loss of iron through kidney Prevents kidney damage by hemoglobin |
|
|
What removes the hemoglobin-haptoglobin complex
|
Reticuloendothelial system
|
|
|
In hemolytic anemia, the haptoglobin level increases or decreases?
|
Decreases
|
|
|
What does hemopexin bind to?
|
Free heme released from hemoglobin
|
|
|
What are the highly toxic activities of heme?
|
Intercalates into membrane
Produces free radicals |
|
|
The heme-hemopexin complex is taken by ______
|
Liver cells
(P.S.: in the liver, the released iron binds to ferritin) |
|
|
What is the indicator of intravascular hemolysis.
|
Depletion of unsaturated hemopexin
|
|
|
What are the functions of transferrin?
|
Transports iron in plasma as ferric ions (Fe+3)
Protects against the toxic effects of free iron |
|
|
Fransferrin is normall _____ saturated with Fe3+?
|
30%
|
|
|
_____ saturation is indicative of iron overload.
|
Increased
|
|
|
Decreased saturation is indicative of iron _____
|
deficiency
|
|
|
Transferrin is increased/decreased in inflammatory states. Why?
|
Decreased, due to excessive degradation of transferrin-Fe3+ complexes
|
|
|
What is ferritin?
|
The main intracellular iron storage protein.
|
|
|
What are the functions of ferritin?
|
Keeps iron in soluble, nontoxic form
Iron is released when it is needed. |
|
|
What is apoferritin?
|
Iron-free ferritin
|
|
|
What is used to measure the total amount of iron stored in the body?
|
Ferritin
|
|
|
What is hemosiderin?
|
Another iron-storage complex
|
|
|
Where is hemosiderin found?
|
Always found within cells
|
|
|
What is hemosiderin composed of?
|
Ferritin, denatured ferritin, and other material
|
|
|
During what situation is hemosiderin usually found?
|
After hemorrhages
|
|
|
Is hemosiderin a good supply of iron?
|
No, the iron within hemosiderin is poorly available to supply iron when needed
|
|
|
Iron content in the body is regulated on the level of.....
|
Absorption
|
|
|
Defects in protein regulating absorption may lead to what?
|
Iron overload
(Hereditary hemochromatosis) |
|
|
Iron overload can be caused by mutation of what gene?
|
HFE
|
|
|
What are the consequences of iron overload?
|
Hinders immune system (prone to infections and illnesses)
Pancreases can be affected (diabetic complications) Heart problems (angina and poor heart rhythm) Liver (cirrhosis and cancer) Depression and infertility |
|
|
What are ways to treat iron overload?
|
Therapeutic phlebotomy (1-2/week; de-ironing may take 6 mo - 3 yrs))
Chelation (in the case of extreme anemia) (Desferal infusion) |
|
|
What are ways to maintain iron overload?
|
Low iron diet
Less extreme phlebotomy or chelation |
|
|
What is ceruloplasmin?
|
Major copper transport protein
|
|
|
What is the function of ceruloplasmin?
|
Regulates oxidation-reduction, transport, and utilization of iron (oxidation of ferrous form into ferric form)
|
|
|
Increased concentration of ceruloplasmin are found in what disorders?
|
Active liver disease
Tissue damage |
|
|
Decreased levels of ceruloplasmin are found in what disorder?
|
Wilson's disease
|
|
|
Wilson's disease is a(n) _______ _______ hereditary disease
|
autosomal recessive
|
|
|
Wilson's disease is caused by a mutation of what?
|
Mutation in ATPase involved in transport of copper into the bile
|
|
|
The mutation in Wilson's disease leads to what disorders in the body?
|
Deficiency in the ATPase leads to accumulation of copper in the liver that damages liver tissue.
Low plasma concentration of ceruloplasmin, leads to increased urinary and plasma copper |
|
|
Normally, what percentage of T4 and T3 are found in the free/unbound form?
|
T4: 0.03%
T3: 0.3% |
|
|
What are the 3 major serum thyroid hormone binding proteins
|
Thyroxine Binding globulin (TBG)
Transthyretin (TTR; Transports thyroxine and retinol) Albumin |
|
|
From highest to lowest, list the three thyroid binding proteins most present in the blood
|
1. Albumin (100 fold the molar concentration of TTR; 2,000 fold that of TBG)
2. TTR 3. TBG |
|
|
From highest to lowest, list the three thyroid binding proteins that have the highest affinity for thyroid hormones
|
1. TBG
2. TTR 3. HSA |
|
|
What is the major corticosteroid transport protein
|
Transcortin
|
|
|
Where is transcortin produced?
|
Liver
|
|
|
How is transcortin regulated?
|
By estrogen (plasma transcortin level increase during pregnancy, and decrease during cirrhosis)
|
|
|
What percentage of cortisol and other corticosteroids in circulation are bound to transcortin?
In albumin? |
~75%
~25% |
|
|
Transcortin also binds and transports _____
|
Progesterone
|
|
|
Where is Sex hormone binding globulin (SHBG) mainly produced?
|
Liver
|
|
|
SHBG is also produced in what organs
|
brain, uterus, testes, and placenta
|
|
|
High SHBG is associated with what conditions?
|
Pregnancy, hyperthyroidism, anorexia nervosa, and some cancers
|
|
|
What is "steady state?"
|
Relatively constant levels of intracellular enzymes; results from normal tissue turnover
|
|
|
Elevated intracellular enzyme levels in plasma is an indication of what?
|
Extended tissue damage
|
|
|
T/F Laboratory assays usually use plasma
|
False!
They use serum |
|
|
What is the diagnostic significance of enzymes being specific for one or a few tissues
|
Their increased level in plasma reflects damage of the corresponding tissues
|
|
|
Alanine aminotransferase (ALT)
|
Liver disease, hepatitis (if AST/ALT <1), (Liver, kidney and muscle)
|
|
|
Aspartate aminotransferase (AST)
|
Liver disease, (liver, muscle, and RBCs)
|
|
|
Alkaline phosphatase
|
Primary biliary cirrhosis
|
|
|
Troponin I (TnI)
|
Myocardial infarction
|
|
|
Lactate dehydrogenase (LDH)
|
Liver, muscle and late phase of myocardial infarction
|
|
|
Creatine kinase (CK)
|
CK-MB - heart muscle damage
CK-MM - heart muscle damage |
|
|
Prostate acid phosphatase (PAP)
Prostate specfici antigen (PSA) |
Elevated levels is a marker of prostate cancer
|
|
|
a-Amylase
|
Acute pancreatitis
|
|
|
Where is prostatic acid phosphatase, PAP, produced
|
Prostate
|
|
|
Physiological function of PAP
|
Liquefaction of semen
|
|
|
Highest levels of PAP are found where?
|
Metastasized prostate cancer
|
|
|
Why should you not do a rectal exam before testing for PAP?
|
Manipulation of prostate gland through massage or rectal exam before test may increase its level
|
|
|
Where is Prostate specific antigen produced?
|
Prostate
|
|
|
PSA is elevated in the presence of what disorder?
|
Prostate cancer and in other prostate disorders
|
|
|
What enzyme is the most effective test for early detection of prostate cancer?
|
PSA (prostate specific antigen)
|
|
|
Increased a-amylase may be caused by what disorders?
|
Pancreatitis (these cells produce amylase)
Trauma of salivary glands Mumps (due to inflammation of salivary glands) |
|
|
When should a-amylase be tested, and why is timing critical?
|
Soon after bout of pancreatitis pain; timing is critical due to being excreted rapidly by kidneys
|
|
|
Amylase may be measured by what other body fluids?
|
Urine and peritoneal fluid
|
|
|
What is acute phase response?
|
Set of nonspecific host responses to cytokines released due to:
1. tissue injury 2. infection 3. inflammation |
|
|
Acute phase response causes what functional liver changes
|
Increase in synthesis of acute phase proteins
Decrease albumin synthesis |
|
|
What is C-reactive protein (CRP)?
|
Major component of acute phase response, and is a marker of inflammation
|
|
|
When is CRP produced?
|
In response to bacterial infection, inflammation, or injury
|
|
|
What is the function of CRP
|
Mediates the binding of foreign polysaccharides, and activation of complement
|
|
|
Positive CRP results may also occur in which conditions?
|
Last half of pregnancy, or use of birth control pills
|
|
|
Slightly elevated levels of CRP has been correlated with what?
|
Increased risk of cardiovascular disease.
Low risk: <1 mg/L Overage risk: 1-3 mg/L High risk: >3 mg/L |
|
|
What is alpha 1-antitrypsin?
|
Natural inhibitor of proteases produced by the liver
|
|
|
Manifold increase of alpha 1-antitrypsin is an indicator of what?
|
Acute inflammation
|
|
|
Alpha 1-antitrypsin (AAT) is the most important inhibitor of what?
|
Leukocyte elastase
|
|
|
What is the function of alpha 1 antitrypsin?
|
Breaks down the outer membrane protein A (OmpA) of E. coli and other gram negative bacteria
|
|
|
What secretes alpha 1 antitrypsin?
|
Activated neutrophils and macrophages
|
|
|
If alpha 1 antitrypsin goes unchecked, what could happen?
|
Extensive destruction of connective tissue
|
|
|
What does Bacterial elastase do?
|
Breaks down cytokines, IgA and IgG
Cleave a component of complement, and a receptor on neutrophils that contributes to a decrease of their ability to kill bacteria by phagocytosis |
|
|
Inherited disorders of alpha 1 antitrypsin (AAT) synthesis, where concentration is reduced to 10-15% of normal, can result in what disorders?
|
Emphysema, or COPD
|
|
|
Alpha 1 antichymotrypsin belongs to what family of human plasma proteins?
|
a 1-globulin family
|
|
|
What is the function of alpha 1 antichymotrypsin (ACT)?
|
Specific inhibitor of chymotrypsin and other related serine proteases
|
|
|
What is the major component of amyloid deposits associated with Alzheimer's disease?
|
Alpha 1 antichymotrypsin (ACT)
|
|
|
Elevated serum levels of ACT are found in what disorders?
|
Various inflammatory conditions
Crohn's disease Ulcerative colitis and burn injuries |
|
|
What are the Fab regions of antibodies Ab
|
2 identical fragments; bind to specific antigen
|
|
|
What are the Fc regions
|
Bind to specific proteins modulating immune cell activity
|
|
|
How many polypeptide chains are in an antibody?
|
4
|
|
|
IgG % of total antibody
|
75-80
|
|
|
IgA % of total antibody
|
7-15
|
|
|
IgM % of total antibody
|
5-10
|
|
|
IgD % of total antibody
|
~1
|
|
|
IgE % of total antibody
|
0.002
|
|
|
IgG avg. life (Days)
|
23
|
|
|
IgA avg. life (Days)
|
6
|
|
|
IgM avg. life (Days)
|
5
|
|
|
IgD avg. life (Days)
|
3
|
|
|
IgE avg. life (Days)
|
2.5
|
|
|
IgG cross placenta?
|
Yes
|
|
|
IgA cross placenta?
|
No
|
|
|
IgM cross placenta?
|
No
|
|
|
IgD cross placenta?
|
No
|
|
|
IgE cross placenta?
|
No
|
|
|
IgG biological function
|
Long term immunity
|
|
|
IgA biological function
|
Secretory antibody; on mucous membranes
|
|
|
IgM biological function
|
First response to antigen
|
|
|
IgD biological function
|
B cell receptor
|
|
|
IgE biological function
|
Allergy and worm infection
|
|
|
What is the primary immune response?
|
after first exposure to Ag, immune system produces IgM leading to gradual increase in Ab titer
|
|
|
What is the secondary immune response?
|
After second contact with same Ag, immune system produces a more rapid, stronger response due to Abs production by memory cells
|
|
|
What is multiple myeloma?
|
Cancer of plasma cells
|
|
|
Who does multiple myeloma affect?
|
Men and women after 50
|
|
|
How is the prognosis of multiple myeloma?
|
Poor, despite treatment
|
|
|
What are the treatments for multiple myeloma?
|
Chemotherapy and stem cell transplant
|
|
|
What group of diseases does multiple myeloma belong to?
|
Hematological malignancies
|
|
|
How does multiple myeloma cause renal failure?
|
Excess production of light chains and its deposition in renal tubules
|
|
|
Bone lesions of multiple myeloma may affect what regions?
|
Skull, vertebrae, ribs and pelvis
|
|
|
How does multiple myeloma cause hypercalcemia?
|
The bone lesions/breakdown of bone leads to release of calcium in the blood
|
|
|
How does multiple myeloma cause anemia?
|
It inhibits normal red blood cell production
|
|
|
What is the common tetrad of multiple myeloma, and its mnemonic?
|
C: Calcium (elevated)
R: Renal failure A: Anemia B: Bone lesions |
|
|
What are hybridomas?
|
They are single specificity Ab, that recognise specific antigen, and are formed by fusing a mouse B cell with a myeloma cell
|
|
|
How are hybridomas used?
|
Diagnosis of disease, identification of microbes and therapy
|
