Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 397661
Title Angiopoietin-Like 4 Interacts with Integrins ß1 and ß5 to Modulate Keratinocyte Migration
Author(s) Goh, Y.Y.; Pal, M.; Chong, H.C.; Zhu, P.; Tan, M.J.; Punugu, L.; Lam, C.R.I.; Yau, Y.H.; Tan, C.K.; Huang, R.L.; Tan, S.; Yang Tang, M.B.; Ling Ding, J.; Kersten, A.H.; Tan, N.S.
Source American Journal of Pathology 177 (2010)6. - ISSN 0002-9440 - p. 2791 - 2803.
DOI https://doi.org/10.2353/ajpath.2010.100129
Department(s) Nutrition, Metabolism and Genomics
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) induced adipose factor - cell-migration - alpha-6-beta-4 integrin - in-vivo - protein - kinase - expression - repair - metastasis - inhibition
Abstract Adipose tissue secretes adipocytokines for energy homeostasis, but recent evidence indicates that some adipocytokines also have a profound local impact on wound healing. Upon skin injury, keratinocytes use various signaling molecules to promote reepithelialization for efficient wound closure. In this study, we identify a novel function of adipocytokine angiopoietin-like 4 (ANGPTL4) in keratinocytes during wound healing through the control of both integrin-mediated signaling and internalization. Using two different in vivo models based on topical immuno-neutralization of ANGPTL4 as well as ablation of the ANGPTL4 gene, we show that ANGPTL4-deficient mice exhibit delayed wound reepithelialization with impaired keratinocyte migration. Human keratinocytes in which endogenous ANGPTL4 expression was suppressed by either siRNA or a neutralizing antibody show impaired migration associated with diminished integrin-mediated signaling. Importantly, we identify integrins ß1 and ß5, but not ß3, as novel binding partners of ANGPTL4. ANGPTL4-bound integrin ß1 activated the FAK-Src-PAK1 signaling pathway, which is important for cell migration. The findings presented herein reveal an unpredicted role of ANGPTL4 during wound healing and demonstrate how ANGPTL4 stimulates intracellular signaling mechanisms to coordinate cellular behavior. Our findings provide insight into a novel cell migration control mechanism and underscore the physiological importance of the modulation of integrin activity in cancer metastasis
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