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《Chinese Journal of Cancer Prevention and Treatment》 2006-18
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Relationship between matrix metalloproteinases and lung cancer

ZHONG Xiao-jun, YANG Rui-sen, WEI Shu-zhenDepartment of Thoracic Surgery, Shandong Tumor Hospital, Jinan 250117, P.R.China  
The matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases. MMPs are essential enzymes which are involved in the degradation of basilar membrane and the extracellular matrix, and play an important role in the tumor invasion and metastasis. Currently, at least 26 members of this family are known to exist. Based on substrate specificity and domain organization, the MMPs can be loosely divided into four main groups: the interstitial collagenases, gelatinases, stromelysins and membrane-type MMPs. Most members of the MMP family are organized into three domains based on structural considerations: an amino-terminal propeptide; a catalytic domain; and a hemopexin-like domain at the carboxy-terminal. The process of activation involves sequential cleavage of the propeptide, and proteolytic activity is inhibited by tissue inhibitors known as tissue inhibitors of metalloproteinase (TIMPs). the TIMP family, which presently includes four proteins: TIMP-1, TIMP-2, TIMP-3, and TIMP-4, inhibits protease activity by forming high-affinity 1:1 complexes with the MMPs. Recent data from model systems suggest that MMPs/TIMPs are involved in lung cancer initiation, invasion and metastasis. Consistent with their role in lung cancer progression, high levels of several MMPs have been found to correlate with poor prognosis in patients with lung cancer. Because MMPs are apparently involved in lung cancer initiation and dissemination, inhibition of these proteinases may be of value both in preventing lung cancer and in blocking metastasis of established tumours.
【CateGory Index】: R734.2
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