Publication Date:
2013-05-25
Description:
Disulfide bond formation in secretory proteins occurs primarily in the endoplasmic reticulum (ER), where multiple enzyme families catalyze cysteine cross-linking. Quiescin sulfhydryl oxidase 1 (QSOX1) is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells. We examined the physiological function for extracellular catalysis of de novo disulfide bond formation by QSOX1. QSOX1 activity was required for incorporation of laminin into the extracellular matrix (ECM) synthesized by fibroblasts, and ECM produced without QSOX1 was defective in supporting cell-matrix adhesion. We developed an inhibitory monoclonal antibody against QSOX1 that could modulate ECM properties and undermine cell migration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ilani, Tal -- Alon, Assaf -- Grossman, Iris -- Horowitz, Ben -- Kartvelishvily, Elena -- Cohen, Sidney R -- Fass, Deborah -- New York, N.Y. -- Science. 2013 Jul 5;341(6141):74-6. doi: 10.1126/science.1238279. Epub 2013 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. tal.ilani@weizmann.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704371" target="_blank"〉PubMed〈/a〉
Keywords:
Antibodies, Monoclonal
;
Cell Adhesion
;
Cell Line, Tumor
;
Cell Movement
;
Cells, Cultured
;
Cysteine/metabolism
;
Disulfides/metabolism
;
Extracellular Matrix/enzymology/*physiology/ultrastructure
;
Fibroblasts/enzymology/ultrastructure
;
Humans
;
Laminin/metabolism
;
Oxidoreductases Acting on Sulfur Group Donors/antagonists &
;
inhibitors/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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