Publikationsdatum:
1999-09-18
Beschreibung:
Antithrombin, a member of the serpin family, functions as an inhibitor of thrombin and other enzymes. Cleavage of the carboxyl-terminal loop of antithrombin induces a conformational change in the molecule. Here it is shown that the cleaved conformation of antithrombin has potent antiangiogenic and antitumor activity in mouse models. The latent form of intact antithrombin, which is similar in conformation to the cleaved molecule, also inhibited angiogenesis and tumor growth. These data provide further evidence that the clotting and fibrinolytic pathways are directly involved in the regulation of angiogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Reilly, M S -- Pirie-Shepherd, S -- Lane, W S -- Folkman, J -- P01-CA45548/CA/NCI NIH HHS/ -- R01-CA64481/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 17;285(5435):1926-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, Children's Hospital, Departments of Surgery and Cellular Biology, Harvard Microchemistry Facility, 16 Divinity Avenue, Cambridge, MA 02138, USA. oreilly@hub.tch.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10489375" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Animals
;
Antineoplastic Agents/chemistry/isolation & purification/metabolism/*pharmacology
;
Antithrombins/chemistry/isolation & purification/metabolism/*pharmacology
;
Carcinoma, Small Cell/blood supply/drug therapy
;
Cell Line
;
Culture Media, Conditioned
;
Drug Screening Assays, Antitumor
;
Humans
;
Lung Neoplasms/blood supply/drug therapy
;
Mice
;
Mice, SCID
;
Neoplasm Transplantation
;
Neovascularization, Pathologic/*drug therapy
;
Peptide Fragments/chemistry/metabolism/pharmacology
;
Protein Conformation
;
Tumor Cells, Cultured
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
