The Hemopexin-like Domain (C Domain) of Human Gelatinase A (Matrix Metalloproteinase-2) Requires Ca2+ for Fibronectin and Heparin Binding

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The Hemopexin-like Domain (C Domain) of Human Gelatinase A (Matrix Metalloproteinase-2) Requires Ca for Fibronectin and Heparin Binding BINDING PROPERTIES OF RECOMBINANT GELATINASE A C DOMAIN TO EXTRACELLULAR MATRIX AND BASEMENT MEMBRANE COMPONENTS*

The binding properties of the COOH-terminal hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2, 72-kDa gelatinase) were investigated to determine whether the C domain has binding affinity for extracellular matrix and basement membrane components. Recombinant C domain (rC domain) (Gly-Cys) was expressed in Escherichia coli, and the purified protein, identified usi...

متن کامل

Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin.

The complete amino acid sequence of a DNA- and heparin-binding domain isolated by limited thermolysin digestion of human plasma fibronectin has been obtained. The domain contains 90 amino acids with a calculated molecular weight of 10,225. The apparent molecular mass of this domain is 14 kDa when analyzed by sodium dodecyl sulfate-gel electrophoresis. The anomalously high molecular size estimat...

متن کامل

The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR.

Matrix metalloproteinases (MMPs) including membrane type 1 MMP (MT1-MMP) can degrade extracellular matrix and cell surface receptor molecules and have an essential function in malignancy. Recently, we established a functional link between MT1-MMP and the receptor of complement component 1q (gC1qR). The gC1qR is known as a compartment-specific regulator of diverse cellular and viral proteins. On...

متن کامل

Small Molecule Anti-Cancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9 (MMP-9)

Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Acknowledgements: We thank the members of the Sampson, Zucker and Cao labs for their insightful discussions and suggestions on the manuscript, and Kevin Zarrabi for his help with editing and Dr. Francis Johnson for his critical reading. We are also grateful to J. Shipman and T. Balius for their...

متن کامل

Small-molecule anticancer compounds selectively target the hemopexin domain of matrix metalloproteinase-9.

Lack of target specificity by existing matrix metalloproteinase (MMP) inhibitors has hindered antimetastatic cancer drug discovery. Inhibitors that bind to noncatalytic sites of MMPs and disrupt protease signaling function have the potential to be more specific and selective. In this work, compounds that target the hemopexin (PEX) domain of MMP-9 were identified using an in silico docking appro...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1997

ISSN: 0021-9258

DOI: 10.1074/jbc.272.11.7473