Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes
Mycosporine-like amino acids (MAAs) are secondary metabolites found in diverse marine, freshwater, and terrestrial organisms. Evidence suggests that MAAs have several beneficial effects on skin homeostasis such as protection against UV radiation and reactive oxygen species (ROS). In addition, MAAs a...
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doaj-739fe00d89f9407d8a5fd964c4822e022020-11-24T22:52:01ZengMDPI AGMarine Drugs1660-33972015-11-0113127055706610.3390/md13127056md13127056Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in KeratinocytesYun-Hee Choi0Dong Joo Yang1Atul Kulkarni2Sang Hyun Moh3Ki Woo Kim4Anti-aging Research Institute of BIO-FD & C Co. Ltd., Incheon 406-840, KoreaDepartments of Pharmacology and Global Medical Science, Wonju College of Medicine, Yonsei University, Wonju 220-701, KoreaAnti-aging Research Institute of BIO-FD & C Co. Ltd., Incheon 406-840, KoreaAnti-aging Research Institute of BIO-FD & C Co. Ltd., Incheon 406-840, KoreaDepartments of Pharmacology and Global Medical Science, Wonju College of Medicine, Yonsei University, Wonju 220-701, KoreaMycosporine-like amino acids (MAAs) are secondary metabolites found in diverse marine, freshwater, and terrestrial organisms. Evidence suggests that MAAs have several beneficial effects on skin homeostasis such as protection against UV radiation and reactive oxygen species (ROS). In addition, MAAs are also involved in the modulation of skin fibroblasts proliferation. However, the regulatory function of MAAs on wound repair in human skin is not yet clearly elucidated. To investigate the roles of MAAs on the wound healing process in human keratinocytes, three MAAs, Shinorine (SH), Mycosporine-glycine (M-Gly), and Porphyra (P334) were purified from Chlamydomonas hedlyei and Porphyra yezoensis. We found that SH, M-Gly, and P334 have significant effects on the wound healing process in human keratinocytes and these effects were mediated by activation of focal adhesion kinases (FAK), extracellular signal-regulated kinases (ERK), and c-Jun N-terminal kinases (JNK). These results suggest that MAAs accelerate wound repair by activating the FAK-MAPK signaling pathways. This study also indicates that MAAs can act as a new wound healing agent and further suggests that MAAs might be a novel biomaterial for wound healing therapies.http://www.mdpi.com/1660-3397/13/12/7056Mycosporine-like amino acids (MAAs)wound healingmitogen-activated protein (MAP) kinasesextracellular signal-regulated kinases (ERK)c-Jun N-terminal kinases (JNK) |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yun-Hee Choi Dong Joo Yang Atul Kulkarni Sang Hyun Moh Ki Woo Kim |
spellingShingle |
Yun-Hee Choi Dong Joo Yang Atul Kulkarni Sang Hyun Moh Ki Woo Kim Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes Marine Drugs Mycosporine-like amino acids (MAAs) wound healing mitogen-activated protein (MAP) kinases extracellular signal-regulated kinases (ERK) c-Jun N-terminal kinases (JNK) |
author_facet |
Yun-Hee Choi Dong Joo Yang Atul Kulkarni Sang Hyun Moh Ki Woo Kim |
author_sort |
Yun-Hee Choi |
title |
Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes |
title_short |
Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes |
title_full |
Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes |
title_fullStr |
Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes |
title_full_unstemmed |
Mycosporine-Like Amino Acids Promote Wound Healing through Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinases (MAP Kinases) Signaling Pathway in Keratinocytes |
title_sort |
mycosporine-like amino acids promote wound healing through focal adhesion kinase (fak) and mitogen-activated protein kinases (map kinases) signaling pathway in keratinocytes |
publisher |
MDPI AG |
series |
Marine Drugs |
issn |
1660-3397 |
publishDate |
2015-11-01 |
description |
Mycosporine-like amino acids (MAAs) are secondary metabolites found in diverse marine, freshwater, and terrestrial organisms. Evidence suggests that MAAs have several beneficial effects on skin homeostasis such as protection against UV radiation and reactive oxygen species (ROS). In addition, MAAs are also involved in the modulation of skin fibroblasts proliferation. However, the regulatory function of MAAs on wound repair in human skin is not yet clearly elucidated. To investigate the roles of MAAs on the wound healing process in human keratinocytes, three MAAs, Shinorine (SH), Mycosporine-glycine (M-Gly), and Porphyra (P334) were purified from Chlamydomonas hedlyei and Porphyra yezoensis. We found that SH, M-Gly, and P334 have significant effects on the wound healing process in human keratinocytes and these effects were mediated by activation of focal adhesion kinases (FAK), extracellular signal-regulated kinases (ERK), and c-Jun N-terminal kinases (JNK). These results suggest that MAAs accelerate wound repair by activating the FAK-MAPK signaling pathways. This study also indicates that MAAs can act as a new wound healing agent and further suggests that MAAs might be a novel biomaterial for wound healing therapies. |
topic |
Mycosporine-like amino acids (MAAs) wound healing mitogen-activated protein (MAP) kinases extracellular signal-regulated kinases (ERK) c-Jun N-terminal kinases (JNK) |
url |
http://www.mdpi.com/1660-3397/13/12/7056 |
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