RBC Synthesis and Breakdown, Hemoglobin, Myoglobin Flashcards
Macrophages
eat bacteria and present them to T helper cells
called the soldier or the marine
presents antigen to T cells using ILE-1 (interleukin 1)
Monocyte
called monocyte in the blood, but in the tissue, are called macrophages
Basophils
called basophils when in the blood but mast cells if in the tissue
Eosinophils
allergies and parasitic infections
Neutrophils
bacterial infections, granules that can kill bacteria
B cells
comes from the bone marrow
‘Bobo’ cells, do their work once out of the bone marrow
T cells
comes from the bone marrow but goes to the thymus for maturation. If does not mature, commits apoptosis. Must not react against the body’s own antigens to ‘pass’. If they do not recognize the body’s antigens, they will commit apoptosis
‘Talino’ cells, thymus university (lol), ‘general’
T helper cells
help B cells and T cells mature
cytotoxic T cells
specific targets: virally infected cells, tumor cells, transplanted / grafted cells
suppressor T cells
‘medic’, makes sure that healthy cells are not attacked
memory T cells and memory B cells
records events to make sure that future infection will not happen again
B cell activation by T helper cell
ILE-4, 5, 6 are needed to activate B cell by T helper cell
plasma cell
transformed B cell upon activation by T helper cells. Produces antibodies / immunoglobulins
Immunoglobulins
5 types: GAMED. IgG is the smallest, IgM is the largest, first response. IgE involved in parasitic infections and allergies. IgA in secretions (i.e. mucus)
Complement proteins
secreted by the liver, found in places with antigen-antibody complexes. ‘like homing missles’ / dog of war
forms membrane attack complex (MAC), causes rupture and activate inflammation, can also recruit macrophages and neutrophils
bag pliability of RBC
means that RBC can compress; they are not permanently in biconcave shape
after 120 days, they lose their bag pliability. Once they go to narrow capillaries, they rupture and die (spleen)
Hemoglobin
oxygen transport
acts as an acid-base buffer
contains carbonic anhydrase
RBC does not utilize oxygen
Hematocrit
percentage of cells in the blood; 40-45% blood volume
Young liver synthesizes blood
most of the 2nd trimester RBC production happens in liver.
Erythropoeitin
mostly produced in kidneys in response to hypoxia
Anaerobic glycolysis
source of energy for RBCs
Vitamin B12 and Folic acid
needed for maturation of RBC. Without it, will have megaloblastic anemia (large, fragile, RBC)
folic acid deficiency causes neural tube disorders (froccoli and cauliFlower)
vitamin B12 deficiency: causes neural deficits (baboy, beef)
Reticulocytes
immature RBC released into blood. no nucleus, remnants of golgi, mitochondria, other organelles
hemolytic anemia (higher reticulocytes) because of massive death of RBC
Orthochromatic Erythroblast
with nucleus, stage of RBC, ER reabsorbed
succinyl CoA
from Krebs cycle
hemoglobin alpha and beta
most common hemoglobin chains
Porphyrin
attaches to iron and formed heme
made up of pyrrole rings
methyne bridges
iron porphyrins - animals
magnesium-containing porphyrins - chlorophyll
Ferrous form
active hemoglobin, Fe2+
Transferrin
transfers iron from the intestines (duodenum) to the plasma
Ferritin
1 storage protein for iron
Hemosiderin
storage protein for iron, additional storage area
spleen
graveyard of RBC
bilirubin
poryphyrin is transformed into this when RBC dies
cytochrome P450
found in liver, can degrade poison and drugs, contained in heme
heme
not only found in hemoglobin but also in other enzymes
mostly synthesized in bone marrow, but the rest in hepatocytes
Mast cells
inflammation, histamine and heparin
Uroporphyrinogen III and Coproporphyrinogen III pathway
more common than the 1
Heme synthesis
begins and ends in mitochondria. Intermediate steps in cytoplasm
- Formation of gamma aminolevulinic acid (rate limiting step)
- Formation of porphobilinogen
- Formation of uroporphyrinogen
- Formation of heme
Uroporphyrinogen decarboxylase
turns uroporphyrinogen into coproporphyrinogen, something about acetyl group
Ferrochelatase
Changes protoporphyrinpgen III into protoporphyrin III
Porphyrias
abnormalities in heme synthesis pathway
need heme, iron
symptoms:
abdominal pain
photosensitivity
neuropsychiatric symptoms
Porphyria Cutanea Tarda
Photosensitivity, blistering
Photosensitivity
abnormalities in late heme synthesis pathway
Abdominal pains
Abnormalities in early heme synthesis pathway
Sideroblastic anemia with ringed sideroblasts
mitochondria that is iron-laden, iron is not utilized. Lacking function in ALA synthase. RBC is not properly developed, iron is in the wrong place
Iron deficiency
not extremely red, RBCs are small.
Protoporphyrin 9 / protoporphyrin 3
where iron attaches to, using the enzyme ferrocheletase
ALA dehydratase
responsible for ?
Lead poisoning
heme not formed
basophilic stippling
micrositic hypochromic anemia
zinc in ALA dehydratase exchanged for lead
Bilirubin metabolism
Bilirubin is nonpolar, attaches with albumin. Conjugation happens in liver. Transfer glucoronic acid
Conjugated bilirubin
becomes component of bile
goes to small intestines
Bile
produced in the liver and stored in the gallbladder
water, cholesterol, bilirubin, bile salts
Bile salts
Active component of bile, emulsifies fats
Bilirubin
comes from dead red blood cells cannot emulsify enter the liver heme is converted into this. bilirubin = basura (in pee or in poop)
Urobilinogen
can be reabosorbed in the intestines or turns up in feces once converted into stercobilin (gives it the yellow / brown color). some are excreted in urine
turns into urobilin upon exposure to air and gives yellow color to urine
Urobilin
Product of urobilinogen, gives yellow color to urine
Stercobilin
product of urobilinogen, gives brown color to feces
Indirect / unconjugated hyperbilibirunemia
cannot be measured directly
total bilib-direct to get the value
indirect reacting, need to add methanol para makita siya
high rbc destruction (hemolytic anemia)
direct/conjugated hyperbilibirunemia
direct reacting caused by bile duct obstruction can be seen in the blood why? because veins are forced open (regurgitated in the veins) because of bile duct obstruction CDR
kernicterus
unconjugated bilirubin penetrated the blood brain barrier
yellowing of brain of newborns resulting in encephalopathy
Hb Gower 1
Made up of zeta chains and epsilon chains
HbF
alpha 2, gamma 2. persists for several weeks and months after birth
HbA
Seen 8 months onwards. produced in bone marrow
HbA2
bone marrow
Taut form of hemoglobin
low oxygen affinity
many salt bridges
Relaxed form of hemoglobin
high oxygen affinity
little salt bridges
positive cooperativity
once 1 oxygen attaches, it is much easier for the other oxygens to attach
why? destruction of salt bridges
myoglobin
heart and skeletal muscles reservoir of oxygen single chain oxygen carrier histidine residues will only release oxygen if cell is hypoxic already hyperbolic curve
myoglobinuria
following massive crush injury, myoglobin escapes into urine and colors urine dark red (tea colored)
hemoglobin
sigmoidal curve
allosteric effectors
factors found in hemoglobin that will affect binding of oxygen
for hemoglobin only
Shifting to the right of the oxy-hemoglobin dissociation curve
increase unloading of oxygen by hemoglobin
CABET face right (increase lahat ng factors)
except for: carbon monoxide, fetal hemoglobin (will cause increase binding of oxygen to hemoglobin)
shifting to the left of oxy-hemoglobin dissociation curve
opposite, increased binding of oxygen to hemoglobin
Bohr effect
inc in protons cause oxygen to dissociate (increase in acidity)
transport CO2 out of the body
H+ displacing oxygen
high carbon dioxide levels = high metab rates = high demand for oxygen.
2,3- Biphosphoglycerate
intermediate of glycolysis
BPG mutase converts 1,3 BPG to 2,3 BPG if there is low oxygen in the peripheral tissues
high 2,3 BPG cause unloading of oxygen
found inside RBC
Hypoxia causes erythropoeitin to be released from kidneys, stimulating increase of RBC production. High BPG mutase, high 2,3 BPG, more unloading of oxygen
Methemoglobin
binds to ferric form
affinity to cyanide
treatment for cyanide poisoning: induce methemoglobinia and the administer methylene blue so patient urinates cyanide
Carboxyhemoglobin
cherry pink patient
high carbon monoxide. shift to the left, oxygen bound tightly to hemoglobin
Glycosylated hemoglobin
attachment of glucose to HbA1C
Sickle cell disease
glutamate substituted for valine (polar substituted for nonpolar)
Alpha thalassemia
alpha chain. 4 genes encodes for the chains. 1 affected = silent carrier 2: alpha thalassemia trait 3: Hb H Disease 4: Hydrops fetalis
Beta Thalassemia
only 2 genes
manifestations only after birth
