RECK, a novel matrix metalloproteinase regulator
N. Meng1, Y. Li1, H. Zhang2 and X-F Sun3
1Department of Surgery, The Forth Hospital of Hebei Medical University, Shijiazhuang, Hebei Province, China 2Division of Biomedicine, School of Life Science, University of Skövde, Skövde, Sweden and 3Department of Oncology, Institute of Clinical and Experimental Medicine, University of Linköping, Linköping, Sweden.
Offprint requests to: Prof. Xiao-Feng Sun, M.D., Ph.D., Department of Oncology, Institute of Clinical and Experimental Medicine, Linköping University, S-58185 Linköping, Sweden. e-mail: firstname.lastname@example.org
Summary. Extracellular matrix (ECM) macromolecules are important for creating the cellular environments required during development and morphogenesis of tissues. Matrix metalloproteinases (MMPs) are a family of Zn-dependent endopeptidases that collectively are capable of cleaving virtually all ECM substrates, and play an important role in some physiological and pathological processes. MMP activity can be inhibited by some natural and artificial inhibitors. A newly found membrane-anchored regulator of MMPs, the reversion-inducing-cysteine-rich protein with kazal motifs (RECK), is downregulated when the cells undergo a process of malignant transformation, and is currently the subject of considerable research activity because of its specific structure and function. In this review, we have chosen to concentrate our efforts on the structure, function, regulation, and future prospect of RECK in order to provide a new target for prevention and treatment of tumours. Histol Histopathol 23, 1003-1010 (2008)
Key words: RECK, MMPs, TIMPs