کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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3980719 | 1257454 | 2007 | 10 صفحه PDF | دانلود رایگان |
SummaryWhile the death rate from cancer has substantially decreased over the past decade, the search for effective and tolerable therapies is a great challenge as yet. The evidence that malignant cells cannot grow to a clinically detectable tumor mass and spread in the absence of an adequate vascular support, has opened a new area of research towards the selective inhibition or even destruction of tumor vessels. Angiostatin and angiostatin-related proteins are a family of specific angiogenesis inhibitors produced by tumors from a family of naturally occurring proteins, which also includes plasminogen and lipoprotein[a]. The anti-angiogenic activity of these proteins resides in cryptic and highly-repetitive molecular domains hidden within the protein moiety, called kringles. Lipoprotein[a] is an intriguing molecule consisting of a low-density lipoprotein core in addition to the covalently bound apolipoprotein[a]. Apolipoprotein[a] is characterized by an inactive protease domain, a single copy of the plasminogen kringle V and multiple repeats of domains homologous to the plasminogen kringle IV. Reliable studies on animal models indicate that the proteolytic break-down products of apolipoprotein[a] would posses anti-angiogenic and anti-tumoral properties both in vitro and in vivo, a premise to develop novel therapeutic modalities which may efficiently suppress tumor growth and metastasis. This review is focused on the biochemical structure, metabolism and the anti-angiogenic activity of this unique and elusive kringle-containing lipoprotein.
Journal: Cancer Treatment Reviews - Volume 33, Issue 5, August 2007, Pages 427–436