[The role of integrins in the physiologic and pathogenic processes].
Cell adhesion molecules (CAM) are a numerous, diverse group of cell surface proteins, which are both receptors and ligands for receptors. Their functions include adhesion, recognition, cell-cell interaction, and communication between mediate cells and extracellular matrix. The following groups of CAM can be distinguished: seletins, integrins, cadherins and other isoforms, including CD 44. Integrins are heterodimers formed from the alpha and beta chains. The a subclass is responsible for a specific bond with ligands. It defines the specificity of integrins. The 8 chain participates in the integration with cytoskeleton ptoteins. It determines the functions of the integrin receptor. The best recognized integrins include: integrin beta1, beta2 and beta3. The expression and activity of integrins have been found to be affected by a variety of factors being either activators or inhibitors. Adhesion molecules (including integrins) play a significant role in both physiological processes (embryogenesis, organogenesis, the normal growth and tissue development) and pathogenic ones. In the latter case, they are particularly involved in inflammatory, allergic and neoplastic diseases. The role of integrins is also emphasized in organ response to trauma and in skin lesion redevelopment. The knowlegde of the integrin molecular basis and that of other adhesion molecules can contribute significantly to the creation of new diagnostic and therapeutic perspectives. An adequate modification of cellular adhesion constitutes a promising way of the pathogenic processes control.
Borowska
Katarzyna
K
Wojskowy Instytut Medyczny w Warszawie, Klinika Dermatologiczna CSK MON.
Jedrych
Barbara
B
Czerny
Krystyna
K
Zabielski
Staniław
S
D000818:Animals; D002448:Cell Adhesion / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000145:classification / Q000502:physiology*; D002465:Cell Movement / Q000502:physiology; D005109:Extracellular Matrix / Q000473:pathology / Q000502:physiology; D005353:Fibronectins / Q000502:physiology; D006801:Humans; D016023:Integrins / Q000737:chemistry / Q000145:classification / Q000502:physiology*; D009369:Neoplasms / Q000473:pathology / Q000503:physiopathology*; D011485:Protein Binding; D015398:Signal Transduction / Q000502:physiology*; D013927:Thrombosis / Q000503:physiopathology
D015815:Cell Adhesion Molecules; D005353:Fibronectins; D016023:Integrins