作者: Alberto Passi , Daniela Negrini , Riccardo Albertini , Giuseppe Miserocchi , Giancarlo De Luca
DOI: 10.1016/S0014-5793(99)00929-1
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摘要: Large chondroitinsulphate-containing proteoglycan (versican) isolated from rabbit lung was cleaved by purified gelatinase A (MMP-2) and B (MMP-9), as well crude enzyme extract with hydraulic edema. Gelatine zymography, performed after purification of gelatinases affinity chromatography, demonstrated that the contained two main gelatinolytic bands at about 92 kDa 72 kDa, identified specific antisera latent proMMP-9 proMMP-2, respectively. Moreover, edematous showed an increased amount proteolytically activated forms both respect to normal controls. These results suggest MMP-2 MMP-9 are involved in breakdown versican occurring during development