Interactions of basement membrane components |
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| Authors: | David T Woodley CN Rao John R Hassell Lance A Liotta George R Martin Hynda K Kleinman |
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| Institution: | 1. Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research Bethesda, MD 20205, U.S.A.;2. Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20205, U.S.A. |
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| Abstract: | The binding of laminin, type IV collagen, and heparan sulfate proteoglycan to each other was assessed. Laminin binds preferentially to native type IV (basement membrane) collagen over other collagens. A fragment of laminin (Mr 600 000) containing the three short chains (Mr 200 000) but lacking the long chain Mr 400 000) showed the same affinity for type IV collagen as the intact protein. The heparan sulfate proteoglycan binds well to laminin and to type IV collagen. These studies show that laminin, type IV collagen and heparan sulfate proteoglycan interact with each other. Such interactions in situ may determine the structure of basement membranes. |
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| Keywords: | Laminin Collagen Heparan sulfate Protein-protein interaction Carbohydrate-protein interaction (Basement membrane) |
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