secreted protein acidic and rich in cysteine is a matrix scavenger chaperone分泌蛋白的酸性和富含半胱氨酸清道夫伴侣是一个矩阵.pdfVIP

secreted protein acidic and rich in cysteine is a matrix scavenger chaperone分泌蛋白的酸性和富含半胱氨酸清道夫伴侣是一个矩阵.pdf

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secreted protein acidic and rich in cysteine is a matrix scavenger chaperone分泌蛋白的酸性和富含半胱氨酸清道夫伴侣是一个矩阵

Secreted Protein Acidic and Rich in Cysteine Is a Matrix Scavenger Chaperone 1 1 1 1¤a 1¤b Alexandre Chlenski *, Lisa J. Guerrero , Helen R. Salwen , Qiwei Yang , Yufeng Tian , Andres 1 2 3 1 4¤c 1 Morales La Madrid , Salida Mirzoeva , Patrice G. Bouyer , David Xu , Matthew Walker , Susan L. Cohn 1 Department of Pediatrics, University of Chicago, Chicago, Illinois, United States of America, 2 Department of Pathology, Northwestern University, Chicago, Illinois, United States of America, 3 Department of Surgery, University of Chicago, Chicago, Illinois, United States of America, 4 Committee on Cancer Biology, University of Chicago, Chicago, Illinois, United States of America Abstract Secreted Protein Acidic and Rich in Cysteine (SPARC) is one of the major non-structural proteins of the extracellular matrix (ECM) in remodeling tissues. The functional significance of SPARC is emphasized by its origin in the first multicellular organisms and its high degree of evolutionary conservation. Although SPARC has been shown to act as a critical modulator of ECM remodeling with profound effects on tissue physiology and architecture, no plausible molecular mechanism of its action has been proposed. In the present study, we demonstrate that SPARC mediates the disassembly and degradation of ECM networks by functioning as a matricellular chaperone. While it has low affinity to its targets inside the cells where the Ca2+ concentrations are low, high extracellular concentrations of Ca2+ activate binding to multiple ECM prote

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