Hematology

maximum hemoglobin synthesis

has ejected nucleus

gives cell characteristic biconcave shape when mature

ease of responding rapidly to applied stresses of fluid forces

capable of undergoing large membrane extensions without fragmentation

permeable 

very pliable

lose or absorb fluid readily

binds with other membrane proteins to form a skeletal network of microfilaments.

-controls biconcave shape

-controls pliability

- provides stability to lipid bilayer

9

WBC, HgB, MCV, MCHC, PLT, RBC, Hct, MCH, RDW, retic

provides a cell count of the number of red blood cells present in a specimen

-also serves as indirect estimate of the hemoglobin contents of the blood

average RBC volume

-useful in classifying anemias as normocytic, microcytic, or macrocytic

estimates the concentration of Hgb in each RBC

-provides a ratio of the weight of Hgb to the volume of RBC

reticulocytosis

-elevated reticulocytes

reticulocytopenia

-lowered RBC

carry O2 to tissues and CO2 to lungs

help with acid/base balance

in RBC in stored form

2/3 present in Hgb

1/3 as stored tissue iron

ferrous state Fe2+

if in the ferric state it must be reduced before it can be absorbed

1/3

-important bc has binding sites that are readily available to grab iron when needed

metal-free tertapyrroles found in greatest quantity in bone marrow and liver

-serve as intermediates in heme synthesis

one way 

-if deficient in one process the process is halted from there after

-glycine + succinyl CoA under the presence of ALA synthase cofactor w/ vitamin B6 in the mitochondria

-moves out to the cytosol

-back to the mitochondria as protoporphyrin IX where Fe2+ added to produce heme

-adequate iron delivery and supply

-adequate synthesis of Protoporphyrin IX

-adequate globin chain synthesis

-uptake and delivery of O2

-controlling accumulation of hydrogen ions in the RBC

-as Hgb unloads O2 in tissues it binds free H ions generated by dissociation of H2CO3 inside RBC

globin chains broken down and ammino acids are recycled into new protein synthesis

-iron recycled for new hemoglobin synthesis

-protoporphyrin IX biproduct of RBC catabolism

inadequate dietary intake of iron

decreased absorption

chronic bleeding

gastrointestinal bleeding

heavy menstration

pregnancy

lactation

chronic hemoglobinuria

less hemoglobin

microcydic

less stained

wider central palor

chronic infection or inflammation

cancer

liver disease

renal disease

sex-linked or autosomal recessive (inherited)-rare

myelodysplasia (RARS)- primary

acquired (secondary)- alcohol abuse, exposure to certain drugs which inhibit vit B6, lead poisoning

interfering with normal heme synthesis prevents iron's insertion into prophyrin structure with sunsequent accumulation of iron in mitochondria of RBC precursors

inherited autosomal recessive disorder causing idiopathic excess intestinal iron absorption not matched by increased excretion

-slow chronic buildup of iron results in accumulation of iron and injury to many orans (liver, kidney, heart, pancreas, testes, adrenals, and pituitary.

caused by frequent blood transfusions adding 200-250 mg of iron to the body per transfusion

causes iron overloading 

serum iron- decreased

serum transferrin- increased

serum ferritin- decreased

TIBC- increased

% saturation- decreased

serum iron- decreased

serum transferrin- decreased

serum ferritin- normal to increased

TIBC- decreased

% saturation- decreased

serum iron- increased

serum transferrin- normal

serum ferritin- increased

TIBC- normal to decreased

% saturation- normal to increased

serum iron- increased

serum transferrin- decreased

serum ferritin- increased

TIBC- decreased

% saturation- increased

serum iron- increased

serum transferrin- decreased

serum ferritin- increased

TIBC- decreased

% saturation- increased

quality not there

amino acid sequence of one othe globin chain types is altered as a result of an incorrect DNA code caused b a point mutation

-single nucleotid substitution

SS- disease

AS- trait

blockage 

tissue hypoxia

extreme pain in area of blockage

finally tissue death

autosomal dominant disorder with decreased production of alpha globin chains due to deletion of a globin genes

-autosomal dominant caused by genetic point mutation

silent- deletion of one gene

trait- deletion of 2 genes

hemoglobin H disease- deletion of 3 genes

deletion of all 4 genes is incompatible with life

1-75%

2-50%

3-75%

4-0%

chain formation decreases together accordingly until reaches 75% then the B chains will try and make up the difference but the difference in hemeglobin affinity makes it inefficient

b-thalassemia minor

(null or plus)

-heterozygous

b-thalassemia major

(null or plus)

-homozygous

Hgb electrophoresis

screening

Kleihauer-Betke test