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Untitled - D Ank Unlimited

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medulla 486 membrane attack complex (MAC)<br />

medulla<br />

The innermost or central region of an organ. The central<br />

area of a thymic lobe is the thymic medulla, which is rich in<br />

antigen-presenting cells derived from the bone marrow and<br />

medullary epithelial cells. Macrophages and plasma cells<br />

are rich in the lymph node medulla through which lymph<br />

passes en route to the efferent lymphatics.<br />

medullary cord<br />

A region of the lymph node medulla composed of macrophages<br />

and plasma cells that lies between the lymphatic<br />

sinusoids.<br />

medullary sinus<br />

Potential cavities in the lymph node medulla that receive<br />

lymph prior to its entering efferent lymphatics.<br />

medullary thymic epithelial cells (mTECs)<br />

Refer to thymic epithelial cells.<br />

Megakaryocyte.<br />

megakaryocyte<br />

Relatively large bone marrow giant cells of myeloid lineage<br />

that are multinucleate and from which blood platelets are<br />

derived by the breaking up of membrane-bound cytoplasm<br />

to produce thrombocytes.<br />

MEL-14<br />

A selectin on the surfaces of lymphocytes significant in<br />

lymphocyte interaction with endothelial cells of peripheral<br />

lymph nodes. Selectins are important for adhesion despite<br />

shear forces associated with circulating blood. MEL-14 is<br />

lost from the surfaces of both granulocytes and T lymphocytes<br />

following their activation. It combines with phosphorylated<br />

oligosaccharides.<br />

MEL-14 antibody<br />

A gp90 receptor that permits lymphocyte binding to<br />

peripheral lymph node high endothelial venules. Immature<br />

double-negative thymocytes comprise cells that vary from<br />

high to low in MEL-14 content. The gp90 MEL-14 epitope<br />

is a glycoprotein on murine lymph node lymphocyte<br />

surfaces. MEL-14 antibody prevents these lymphocytes<br />

from binding to postcapillary venules. The gp90 MEL-14<br />

is apparently a lymphocyte homing receptor that directs<br />

these cells to lymph nodes in preference to lymphoid tissue<br />

associated with the gut.<br />

melanization reaction<br />

Refer to ProPO system.<br />

melanocyte<br />

A melanin pigment-producing cell of the skin.<br />

melanoma<br />

Malignant tumors of melanocytes in the skin.<br />

melanoma antigen-1 gene<br />

See MAGE-1.<br />

melanoma-associated antigens (MAAs)<br />

Antigens associated with the aggressive, malignant, and<br />

metastatic tumors arising from melanocytes or melanocyte-associated<br />

nevus cells. Monoclonal antibodies have<br />

identified more than 40 MAAs. They are classified as major<br />

histocompatibility complex (MHC) molecules, cation binding<br />

proteins, growth factor receptors, gangliosides, high<br />

molecular weight extracellular matrix-binding molecules,<br />

and nevomelanocyte differentiation antigens. Some of the<br />

antigens are expressed on normal cells; others are expressed<br />

on tumor cells. Melanoma patient blood sera often contain<br />

anti-MAA antibodies that are regrettably not protective.<br />

Monoclonal antibodies against MAAs aid studies on the<br />

biology of tumor progression, immunodiagnosis, and<br />

immunotherapy trials.<br />

melanoma growth stimulatory activity<br />

See MGSA.<br />

melanosome<br />

A melanocyte organelle linked to the endocytic pathway<br />

that is charged with synthesis of pigment proteins.<br />

HOOC<br />

CH<br />

NH 2<br />

CH 2<br />

CH 2 CH 2 Cl<br />

CH 2 CH 2 Cl<br />

Structure of melphalan (l-phenylalanine mustard).<br />

melphalan (l-phenylalanine mustard)<br />

Nitrogen mustard used to treat multiple myeloma patients.<br />

Membrane perforations resulting from membrane attack complex<br />

(MAC) action.<br />

membrane attack complex (MAC)<br />

Five terminal proteins (C5, C6, C7, C8, and C9) associate<br />

into a membrane attack complex (MAC) on a target cell<br />

membrane to mediate injury. Initiation of MAC assembly<br />

begins with C5 cleavage into C5a and C5b fragments.<br />

A (C5b678) 1(C9) n complex then forms either on natural<br />

membranes or, in their absence, in combination with<br />

such plasma inhibitors as lipoproteins, antithrombin III,<br />

and S protein. C9 and C8 α proteins resemble each other<br />

structurally and also in sequence homologies. Both bind<br />

N

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