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Untitled - D Ank Unlimited

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protein S 599 protoplast<br />

protein S<br />

A 69-kDa vitamin K-dependent plasma protein that serves as<br />

a cofactor for activated protein C. It occurs as an active single<br />

chain protein or as a dimeric protein that is disulfide-linked<br />

and inactive. Protein S, in the presence of phospholipid,<br />

facilitates protein C inactivation of factor Va and combines<br />

with C4b-binding proteins. Protein S deficiency (autosomaldominant<br />

transmission) is characterized clinically by deep<br />

vein thrombosis, pulmonary thrombosis, and thrombophlebitis.<br />

Laurell rocket electrophoresis is used to assay protein S.<br />

protein SAA<br />

A soluble precursor of AA present in minor quantities in<br />

serum. SAA has a molecular weight of 100 kDa and is present<br />

in cord blood and during the first three decades of life at<br />

an average concentration of 50 ± 40 ng/mL. During the next<br />

three decades, SAA shows a slow but steady increase in<br />

concentration, with the level doubling in the eighth decade<br />

of life. Levels of the serum precursor are elevated in most<br />

patients with amyloidosis except in cases of extreme<br />

protein dysfunction due to severe nephrosis. Levels reaching<br />

700 ng/mL are detectable in patients with tuberculosis,<br />

lymphoma, carcinoma, and leukemia, but SAA levels have<br />

no value in the diagnosis of amyloidosis. High levels of<br />

SAA are seen in the secondary form of the disease. SAA<br />

levels may increase transiently during various infections.<br />

protein separation techniques<br />

Proteins may be purified using both electrophoresis and chromatography.<br />

Individual techniques are discussed individually.<br />

Refer to affinity chromatography, isoelectric focusing,<br />

and SDS–polyacrylamide gel electrophoresis (SDS-PAGE).<br />

protein tyrosine kinases<br />

Enzymes that phosphorylate protein tyrosine residues and participate<br />

in signal transduction from several types of cell surface<br />

receptors such as B cell and T cell receptors for antigen.<br />

proteinuria<br />

Protein in the urine.<br />

proteolipid protein (PLP) autoantibodies<br />

Proteolipid protein is a principal structural protein of the<br />

myelin sheath of the mammalian central nervous system<br />

and plays a critical role in myelination. It has been used to<br />

induce experimental allergic encephalomyelitis (EAE) in<br />

rabbits, producing lesions that resemble those formed in<br />

other species following immunization with whole central<br />

nervous system (CNS) tissue or myelin basic protein (MBP).<br />

The PLP antibody response in rabbits correlates with the<br />

clinical and histopathologic severity of experimental and<br />

allergic encephalomyelitis. PLP autoantibodies are correlated<br />

with a specific subset of multiple sclerosis patients.<br />

proteomics<br />

The study of the total proteins encoded by the genome of an<br />

organism. The study of proteins that an organism manifests<br />

is called expression proteomics.<br />

Proteus immunity<br />

Proteus mirabilis administered to mice by the transurethral<br />

route can induce antibodies that react with purified<br />

lipopolysaccharide, flagella, outer membrane protein<br />

(OMP), and mannose-resistant Proteus-like MR/P fimbriae.<br />

Murine vaccination leads to partial immunity. The sera of<br />

patients with rheumatoid arthritis also react with P. mirabilis.<br />

A hexamer peptide within hemolysin is the target of the<br />

immunogenic response, probably due to its close similarity<br />

to susceptibility sequences of HLA-DR1 and DR4. Several<br />

proteins encoded by chromosomal genes serve as P. mirabilis<br />

virulence factors. These help a host evade immune<br />

defenses and lead to cell and tissue injury and include<br />

urease and HPM hemolysin. The latter leads to lysis of<br />

erythrocytes or epithelial cell membrane injury in culture.<br />

The organism also produces four types of fimbriae, surface<br />

proteins that have a role in adherence. It also secretes a<br />

protease that degrades IgA.<br />

prothrombin antibodies<br />

Antibodies against prothrombin or to the prothrombin–<br />

phospholipid complex have been associated with antiphospholipid<br />

(APF) syndrome. The test is based on the ability of<br />

patient sera to inhibit prothrombin activation to thrombin.<br />

Factor Xa or purified snake venom can cleave prothrombin<br />

to produce thrombin. Prothrombin antibodies in patient sera<br />

inhibit the capacity of these proteins to activate prothrombin.<br />

Prothrombin antibodies prevent prothrombin activation<br />

but do not interfere with prothrombin activity on fibrin and<br />

are therefore associated with thrombosis, not bleeding.<br />

Increased concentrations of antibodies against prothrombin<br />

increase the risk of deep venous thrombosis and pulmonary<br />

embolism in middle-aged men.<br />

prothymocytes<br />

Hematopoietic stem cells from the bone marrow migrate to<br />

the thymus via blood circulation and enter through the epithelial<br />

cell lining of the cortex. Prothymocytes (pre-T cells)<br />

differentiate in the thymus microenvironment. They are educated<br />

in the thymus to function as T cells. The four thymic<br />

peptide hormones are thymulin, thymosin α, thymosin β, and<br />

thymopoietin. These hormones are significant in T lymphocyte<br />

proliferation and differentiation. Direct interaction with<br />

the thymus epithelium, which expresses human leukocyte<br />

antigens (HLAs), is necessary for forming functional T lymphocytes<br />

and for learning to recognize major histocompatibility<br />

complex (MHC) antigens. Prothymocytes proliferate<br />

and migrate from the cortex to the medulla. Some are shortlived<br />

and die. The long-lived cells acquire new characteristics<br />

and are called thymocytes. They exit the thymus as immature<br />

cells and seed specific areas of the peripheral lymphoid<br />

organs where they continue to differentiate through a process<br />

driven by an antigen. From these areas, they recirculate<br />

throughout the body.<br />

protooncogene<br />

A cellular gene that shows homology with a retroviral oncogene.<br />

It is found in normal mammalian DNA and governs<br />

normal proliferation and probably also differentiation of<br />

cells. Mutation or recombination with a viral genome may<br />

convert a protooncogene into an oncogene, signifying that it<br />

has become activated. Oncogenes may act in the induction<br />

and/or maintenance of a neoplasm. Protooncogenes united<br />

with control elements may induce transformation of normal<br />

fibroblasts into tumor cells. Examples of protooncogenes<br />

are c-fos, c-myc, c-myb, c-ras, etc. Alteration of the protooncogenes,<br />

leading to synthesis of an aberrant gene product,<br />

is believed to facilitate their tumorigenesis. An elevation in<br />

the quantity of gene product produced is also believed to be<br />

associated with tumorigenesis of protooncogenes.<br />

protoplast<br />

A bacterial cell from which the wall has been removed. It<br />

includes the cell protoplasm and the cytoplasmic membrane.<br />

Lysozyme digestion of Gram-positive bacteria that contain<br />

peptidoglycan cell walls yields protoplasts that require<br />

P

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