MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1

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• 作者：Kazuhiro Yamamoto^a ; ^{kazuhiro.yamamoto@kennedy.ox.ac.uk} ; Hiroshi Okano^a ; ^b ; ¹ ; Wakako Miyagawa^a ; ^b ; ¹ ; Robert Visse^a ; Yasuyuki Shitomi^a ; Salvatore Santamaria^a ; ² ; Jayesh Dudhia^c ; Linda Troeberg^a ; Dudley K. Strickland^d ; Satoshi Hirohata^b ; Hideaki Nagase^a
• 关键词：ADAMTS ; adamalysin-like metalloproteinase with thrombospondin motifs ; DMEM ; Dulbecco's modified Eagle's medium ; EEA1 ; early endosome antigen 1 ; ECM ; extracellular matrix ; FBS ; foetal bovine serum ; Hpx ; hemopexin domain ; LDL ; low-density lipoprotein ; LRP ; LDL receptor-related protein ; MMP ; matrix metalloproteinase ; OA ; osteoarthritis ; RAP ; receptor-associated protein ; RPLP0 ; the 60S acidic ribosomal protein P0 ; TIMP ; tissue inhibitor of metalloproteinases
• 刊名：Matrix Biology
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：56
• 期：Complete
• 页码：57-73
• 全文大小：1854 K
• 卷排序：56

文摘

ProMMP-13 is constitutively produced and endocytosed by chondrocytes. LRP1 is a key modulator of extracellular levels of proMMP-13 and MMP-13. ProMMP-13 and MMP-13 directly bind to LRP1 via the hemopexin domain. Unique sites on LRP1 for MMP-13 binding have been mapped. Co-endocytosis of proMMP-13 with ADAMTS-4, -5 and TIMP-3.