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secretory piece 642 selective IgA deficiency<br />

bile may prevent bacterial growth in the small gut. Intestinal<br />

peristalsis also guards against overgrowth of microorganisms<br />

in blind loops.<br />

secretory piece<br />

A 75-kDa polypeptide chain synthesized by epithelial cells<br />

of the gut for linkage to immunoglobulin A (IgA) dimers<br />

present in body secretions. Secretory component facilitates<br />

IgA transport across epithelial cells and protects secretory<br />

IgA released into the lumen of the gut from proteolytic<br />

digestion by enzymes in the secretions. It is not formed by<br />

plasma cells in the lamina propria of the gut that synthesize<br />

the IgA molecules with which it combines. Secretory component<br />

has a special affinity for mucus, thereby facilitating<br />

the attachment of IgA to the mucous membranes. Also<br />

called secretory component.<br />

sedimentation coefficient<br />

The rate at which a macromolecule or particle sediments<br />

that is equivalent to the velocity per unit centrifugal field:<br />

s = (dx/dt)/w 2 x, where s is the sedimentation coefficient,<br />

dx/dt is the velocity, w is the angular velocity, and x is the<br />

distance from the axis of the centrifuge rotor. The size,<br />

shape, and weight of the macromolecule in question and the<br />

concentration and temperature of the solutions (but not the<br />

centrifuge speed) determine the sedimentation coefficient.<br />

Measurement is in Svedberg units.<br />

sedimentation pattern<br />

The configuration of red blood cells on a test tube or plastic<br />

plate bottom at the conclusion of a hemagglutination test.<br />

The formation of a covering mat on the curved bottom of<br />

a tube or well signifies that agglutination has taken place.<br />

The formation of a round button where the red blood cells<br />

settled to the midpoint of the bottom of the tube or well and<br />

were not retained on the curvature constitutes a negative<br />

reaction with no agglutination.<br />

Sedormid purpura (historical)<br />

A form of thrombocytopenic purpura occurring in patients<br />

who received Sedormid (allyl-isopropyl-acetyl carbamide).<br />

The drug served as a hapten complexing with blood platelets.<br />

The resulting platelet–drug complex was recognized as<br />

foreign by the immune system. Antibodies formed against it<br />

lysed blood platelets in the presence of complement, leading<br />

to thrombocytopenia followed by bleeding and purpura<br />

manifested on the skin. This was a type II hypersensitivity<br />

reaction. Sedormid is no longer used, but the principle of<br />

the hypersensitivity it induced is useful for understanding<br />

autoimmunity induced by certain drugs.<br />

segmental exchange<br />

Refer to gene conversion.<br />

selectins<br />

A group of cell adhesion molecules (CAMs) that are glycoproteins<br />

and play an important role in the relationship<br />

of circulating cells to the endothelium. The members of<br />

this surface molecule family have three separate structural<br />

motifs: a single N terminal (extracellular) lectin motif<br />

preceding a single epidermal growth factor repeat and<br />

various short consensus repeat homology units. Selectins<br />

are involved in lymphocyte migration. These carbohydratebinding<br />

proteins facilitate adhesion of leukocytes to<br />

endothelial cells. A single chain transmembrane glycoprotein<br />

located in each selectin molecule has a similar modular<br />

structure including the extracellular calcium-dependent<br />

lectin domain. The three groups of selectins include<br />

Mel-14 (LAM-1)<br />

ELAM-1<br />

Lectin-like domain<br />

EGF-like domain<br />

CD62<br />

Short consensus repeat<br />

Selectins.<br />

L-selectin (CD62L) expressed on leukocytes; P-selectin<br />

(CD62P) expressed on platelets and activated endothelium;<br />

and E-selectin (CD62E) expressed on activated endothelium.<br />

Under shear forces, the characteristic structural motif<br />

is comprised of an N terminal lectin domain, a domain with<br />

homology to epidermal growth factor (EGF), and various<br />

complement regulatory protein repeat sequences. Refer also<br />

to E-selectin, L-selectin, P-selectin, and CD62.<br />

selective IgA and IgG deficiency<br />

This disease that affects both sexes is either X-linked,<br />

autosomal-recessive, or acquired later in life. A genetic<br />

defect in the switch mechanism may cause immunoglobulin-producing<br />

cells to change from immunoglobulin M<br />

(IgM) to IgG or IgA synthesis. Respiratory infections with<br />

pyogenic microorganisms or autoimmune states that include<br />

hemolytic anemia, thrombocytopenia, and neutropenia may<br />

occur. Numerous IgM-synthesizing plasma cells are demonstrable<br />

in lymph nodes and spleens of affected individuals.<br />

selective IgA and IgM deficiency<br />

A concomitant reduction in both immunoglobulin A (IgA)<br />

and IgM concentrations with normal IgG levels. The IgG<br />

produced in many individuals may not be protective and<br />

recurrent infections may result. The response to many<br />

immunogens is inadequate in this disease, which occurs in<br />

four males for every female affected.<br />

selective IgA deficiency<br />

The most frequent immunodeficiency disorder affecting<br />

approximately 1 in 600 individuals. It is characterized by nearly<br />

absent serum and secretory immunoglobulin A (IgA). The IgA<br />

level is less than 5 mg/dL, whereas the remaining immunoglobulin<br />

class levels are normal or elevated. The disorder is familial<br />

or may be acquired in association with measles, other types of<br />

virus infection, or toxoplasmosis. Patients may appear normal

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