Kininogen-cytokeratin 1 interactions in endothelial cell biology.
This review brings available data together to put in perspective the binding properties of high molecular weight kininogen (HK) to cytokeratin 1 (CK1) to direct future investigations. We summarize our knowledge of the structure and function of HK and discuss the influence of HK on the biologic activities of the plasma kallikrein/kinin system. To better understand the role of HK in regulating the activation of the kallikrein/kinin system, we discuss the interaction of HK with endothelial cell CK1 and its influence on prekallikrein activation. Last, we address the question on how a cytoskeletal protein could be a membrane-binding site and its possible role in disease states.
Shariat-Madar
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Z
Division of Hematology and Oncology, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109-0649, USA.
Schmaier
A H
AH
D000595:Amino Acid Sequence; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D004347:Drug Interactions; D004730:Endothelium, Vascular / Q000378:metabolism*; D006801:Humans; D016234:Kallikrein-Kinin System / Q000502:physiology; D007633:Keratins / Q000378:metabolism*; D007704:Kininogens / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight
D007704:Kininogens; D007633:Keratins