LAB VALUES Flashcards
The erythrocyte sedimentation rate (ESR),
also called a sedimentation rate or Westergren ESR, is the rate at which red blood cells sediment in a period of one hour. It is a common hematology test, and is a non-specific measure of inflammation. To perform the test, anticoagulated blood was traditionally placed in an upright tube, known as a Westergren tube, and the rate at which the red blood cells fall was measured and reported in mm/h.
The ESR is governed by the balance between pro-sedimentation factors, mainly fibrinogen,
The erythrocyte sedimentation rate (ESR),
The ESR is increased in inflammation, pregnancy, anemia, autoimmune disorders (such as rheumatoid arthritis and lupus), infections, some kidney diseases and some cancers (such as lymphoma and multiple myeloma).
The ESR is decreased in polycythemia, hyperviscosity, sickle cell anemia, leukemia, low plasma protein (due to liver or kidney disease) and congestive heart failure. The basal ESR is slightly higher in females.
Aspartate
is non-essential in mammals, being produced from oxaloacetate by transamination. It can also be generated from ornithine and citrulline in the urea cycle. In plants and microorganisms, aspartate is the precursor to several amino acids, including four that are essential for humans: methionine, threonine, isoleucine, and lysine. The conversion of aspartate to these other amino acids begins with reduction of aspartate to its “semialdehyde,” O2CCH(NH2)CH2CHO.[5] Asparagine is derived from aspartate via transamidation:
Valine (abbreviated as Val or V)[3]
is an α-amino acid with the chemical formula HO2CCH(NH2)CH(CH3)2. L-Valine is one of 20 proteinogenic amino acids. Its codons are GUU, GUC, GUA, and GUG. This essential amino acid is classified as nonpolar. Human dietary sources are any proteinaceous foods such as meats, dairy products, soy products, beans and legumes.
Along with leucine and isoleucine, valine is a branched-chain amino acid. It is named after the plant valerian. In sickle-cell disease, valine substitutes for the hydrophilic amino acid glutamic acid in hemoglobin. Because valine is hydrophobic, the hemoglobin is prone to abnormal aggregation.
Aspirin
may be effective at preventing certain types of cancer, particularly colorectal cancer.
pericardiocentesis
It is generally done under ultrasound guidance, to minimize complications. There are two locations that pericardiocentesis can be performed without puncturing the lungs.[2]
One location is through the 5th or 6th intercostal space at the left sternal border at the cardiac notch of the left lung and is also called as parasternal approach.
The other location is through the infrasternal angle and is also called subxiphoid approach.[3]
medial malleolus
Structures that pass behind medial malleolus deep to flexor retinaculum:
Tibialis posterior tendon Flexor digitorum longus Posterior tibial artery Posterior tibial vein Tibial nerve Flexor hallucis longus
Increased capillary permeability
is the pathophysiologic mechanism of pleural effusion
TGF-B
stimulates collagen synthesis,
IL-1
stimulates fever as well as TNF, VEGF causes angiogenesis,
PDGF
causes collagenase secretion.
Th1/Th2 Model for helper T cells
Proliferating helper T cells that develop into effector T cells differentiate into two major subtypes of cells known as Th1 and Th2 cells (also known as Type 1 and Type 2 helper T cells, respectively).
Th1 helper cells are the host immunity effectors against intracellular bacteria and protozoa. They are triggered by IL-12, IL-2 and their effector cytokine is IFN-γ. The main effector cells of Th1 immunity are macrophages as well as CD8 T cells, IgG B cells, and IFN-γ CD4 T cells. The key Th1 transcription factors are STAT4 and T-bet. IFN-γ secreted by CD4 T cells can activate macrophages to phagocytose and digest intracellular bacteria and protozoa. In addition, IFN-γ can activate iNOS to produce NOx free radicals to directly kill intracellular bacteria and protozoa. Th1 overactivation against autoantigens will cause Type4 delayed-type hypersensitivity. Tuberculin reaction or Type 1 diabetes belong to this category of autoimmunity.[1]
Th2 helper cell are the host immunity effectors against extracellular parasites including helminths. They are triggered by IL-4 and their effector cytokines are IL-4, IL-5, IL-9, IL-10 and IL-13. The main effector cells are eosinophils, basophils, and mast cells as well as B cells, and IL-4/IL-5 CD4 T cells. The key Th2 transcription factors are STAT6 and GATAs. IL-4 is the positive feedback cytokine for Th2 cells differentiation. Besides, IL-4 stimulates B-cells to produce IgE antibodies, which in turn stimulate mast cells to release histamine, serotonin, and leukotriene to cause broncho-constriction, intestinal peristalsis, gastric fluid acidification to expel helminths. IL-5 from CD4 T cells will activate eosinophils to attack helminths. IL-10 suppresses Th1 cells differentiation and function of dendritic cells. Th2 overactivation against autoantigen will cause Type1 IgE-mediated allergy and hypersensitivity. Allergic rhinitis, atopic dermatitis, and asthma belong to this category of autoimmunity.[1] In addition to expressing different cytokines, Th2 cells also differ from Th1 cells in their cell surface glycans (oligosaccharides), which makes them less susceptible to some inducers of cell death.
The splenorenal ligament (or lienorenal ligament),
is derived from the peritoneum, where the wall of the general peritoneal cavity comes into contact with the omental bursa between the left kidney and the spleen; the lienal vessels (splenic artery and vein) pass between its two layers. It contains the tail of the pancreas, the only intraperitoneal portion of the pancreas, and splenic vessels.
As splenectomy
causes an increased risk of sepsis due to encapsulated organisms (such as S. pneumoniae and Haemophilus influenzae) the patient should receive the pneumococcal conjugate vaccine (Prevnar), Hib vaccine, and the meningococcal vaccine; see asplenia. These bacteria often cause a sore throat under normal circumstances but after splenectomy, when infecting bacteria cannot be adequately opsonized, the infection becomes more severe.
An increase in blood leukocytes can occur following a splenectomy.[2][3] The post-splenectomy platelet count may rise to abnormally high levels (thrombocytosis), leading to an increased risk of potentially fatal clot formation. There also is some conjecture that post-splenectomy patients may be at elevated risk of subsequently developing diabetes.[4] Splenectomy may also lead to chronic neutrophilia. Splenectomy patients typically have Howell-Jolly bodies[5][6] and less commonly Heinz bodies in their blood smears.[7] Heinz bodies are usually found in cases of G6PD (Glucose-6-Phosphate Dehydrogenase) and chronic liver disease.[8]
IgM
has 10 binding sites
forms polymers where multiple immunoglobulins are covalently linked together with disulfide bonds, mostly as a pentamer but also as a hexamer. IgM has a molecular mass of approximately 970 kDa (in its pentamer form).[5] Because each monomer has two antigen binding sites, a pentameric IgM has 10 binding sites. Typically, however, IgM cannot bind 10 antigens at the same time because the large size of most antigens hinders binding to nearby sites.
The J chain is found in pentameric IgM but not in the hexameric form, perhaps due to space constraints in the hexameric complex. Pentameric IgM can also be made in the absence of J chain. At present, it is still uncertain what fraction of normal pentamer contains J chain, and to this extent it is also uncertain whether a J chain-containing pentamer contains one or more than one J chain.[6] Although hexameric IgM without J chain has higher efficiency of complement fixation than pentameric IgM with J chain.[7][6]
Because IgM is a large molecule, it cannot diffuse well, and is found in the interstitium only in very low quantities. IgM is primarily found in serum; however, because of the J chain, it is also important as a secretory immunoglobulin.[8]
Due to its polymeric nature, IgM possesses high avidity, and is particularly effective at complement activation. By itself, IgM is an ineffective opsonin; however it contributes greatly to opsonization by activating complement and causing C3b to bind to the antigen.
