Carbonic anhydrases IX (CA IX), also known as membrane antigen MN or CA9, is a member of the carbonic anhydrase (CA) family and may be involved in cell proliferation and cellular transformation. CAs are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide (H2O + CO2 = H+ + HCO3–) and thus participate in a variety of biological and physical processes. CA IX protein is expressed primarily in carcinoma cells lines, and the expression is cell density dependent and has been shown to be strongly induced by hypoxia, accordingly facilitates adaptation of tumor cells to hypoxic conditions. It is involved in tumorigenesis through many pathways, such as pH regulation and cell adhesion control. CA IX is used as a marker of tumor hypoxia and as a new therapeutic target for many human carcinomas and cancers.
Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA IX is a transmembrane protein and is one of only two tumor-associated carbonic anhydrase isoenzymes known. It is expressed in all clear-cell renal cell carcinoma, but is not detected in normal kidney or most other normal tissues. It may be involved in cell proliferation and transformation. This gene was mapped to 17q21.2 by fluorescence in situ hybridization, however, radiation hybrid mapping localized it to 9p13-p12.
Cadherin-11; also known as OSF-4; Osteoblast cadherin and CDH11; is a type II classical cadherin from the cadherin superfamily; integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherins interact with themselves in a homophilic manner in connecting cells; may thus contribute to the sorting of heterogeneous cell types. Cadherin-11 contains five cadherin domains and is mainly expressed in brain. Mature cadherin proteins consists of a large N-terminal extracellular domain; a single membrane-spanning domain; and a small; highly conserved C-terminal cytoplasmic domain. It is shown that cadherin-11 is a viable molecular target for therapeutic intervention in Glioblastoma multiforme.
Cadherin-11 is a type II classical cadherin member of the cadherin superfamily of integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherins interact with themselves in a homophilic manner in connecting cells; and thus contribute to the sorting of heterogeneous cell types. Cadherin-11 contains five cadherin domains and is mainly expressed in the brain. Mature cadherin proteins consists of a large N-terminal extracellular domain; a single membrane-spanning domain; and a small highly conserved C-terminal cytoplasmic domain. It is shown that Cadherin-11 is a viable molecular target for therapeutic intervention in Glioblastoma multiforme.
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