Abstract CD147 is involved in many physiological functions, such as lymphocyte responsiveness, spermatogenesis, implantation, fertilization and neurological functions at early stages of development. Here we specifically review the role of CD147 in cancer. We focus on the following aspects: expression of CD147 in malignant versus normal tissues and its possible impact on prognosis, interaction of tumor cell-expressed CD147 with stroma cells and induction of matrix metalloproteinases, as well as the role of CD147 in tumor angiogenesis. The function of CD147 in supercomplexes with monocarboxylate transporters (MCT) and amino acid transporters such as CD98hc and large neutral amino acid transporter 1 (LAT1), as well as the functional contribution of CD147 in complexes with caveolin-1 and integrins, is discussed. Target validation experiments making use of CD147-directed RNAi and monoclonal antibodies are summarized. Finally, the relevance of CD147 as a target for therapeutic intervention in cancer patients is discussed.
• • • • • • CD147 is a member of the immunoglobulin family of receptors. Members of this family play a role in intercellular communication involved in many immune-related functions, differentiation and development. CD147 plays a role in spermatogenesis, lymphocyte activation, expression of monocarboxylate transporters (MCT) and has been identified as a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production (-). Some of these insights were obtained from the study of cd147 –/– mice.
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These animals are defective in matrix metalloproteinase (MMP) regulation, spermatogenesis, lymphocyte responsiveness and neurological functions at the early stages of development. Such female mice are infertile due to failure of implantation and fertilization (). CD147 is involved in the transport of the MCT-1 and MCT-3 to the plasma membrane since reduced accumulation of these transporters has been observed in the retina of cd147 knock-out mice. Maya on flowvella download. A functional role of CD147 in cell adhesion is supported by its involvement in the blood-brain barrier and its interactions with integrins. CD147 has been implicated in many pathological processes, such as rheumatoid arthritis, experimental lung injury, atherosclerosis, chronic liver disease induced by hepatitis C virus, ischemic myocardial injury and heart failure ().
Treatment of transplant patients with a CD147 antibody was effective due to inhibition of T-cell activation (). In the following pages, we review the expression and the functional role of CD147 in human cancer and discuss its possible role as a target for therapeutic intervention. General Features of CD147 CD147, a transmembrane protein of the immunoglobulin (Ig) superfamily was identified independently in different species and has many designations across different species such as M6, Neurothelin, 5A11, HT7, OX-47, CE9, EMMPRIN, Basigin, and gp42 (-).The most prevalent standard isoform is a single-chain type I transmembrane molecule composed of a 21 amino acid signal sequence, a 186 residues-long extracellular domain consisting of two Ig-like domains, a transmembrane domain of 21 amino acids and a cytoplasmic domain of 41 residues. The topology of CD147 and a rarely occurring splice variant as well as the corresponding amino acid sequences are shown in Figures. The transmembrane region harbors a leucine zipper and a charged residue (glutamic acid). The corresponding gene is located on chromosome 19p13.3 and encodes a 29 kDa backbone protein. Three N glycosylation sites have been identified and migration on sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) occurs between 39 and 65 kDa depending on the degree of glycosylation.
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