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Miyamoto et al. (2006) [ 75] showed that MAGP-1 protein can bind to the Notch1 receptor, leading to a subsequent signaling cascade.
In dermal fibroblast cultures, it was observed that MAGP-1 forms very fine and relatively short fibrils compared to fibrillin-1.
This study demonstrated that MAGP-1 colocalized with key microfibril components in the papillary dermis and dermal vasculatures, and that UV irradiation can damage this protein network.
Our results showed that MAGP-2 is upregulated in Tsk-1 skin and in cells expressing Tsk fibrillin, with the greatest increase seen in the hypodermis/superficial fascia of Tsk skin [ 18].
Gene array from young and aged donors showed that the MAGP-1 gene declined significantly (over twofold) in aged skin, along with a panel of elastic fiber-related genes (Table 1).
This showed that 618 (58%) MAGP were composed of genes belonging to the same functional category, among which 391 were MAGP maintained by operons.
This suggests that declines in MAGP-1 may contribute to the disruption in the structural integrity of follicular regions in aged skin.
An interesting observation in this study is that the dermal MAGP-1 level can significantly decline under the dermal epidermal junction at a relatively young age, when the majority of collagen and elastic fibers have been reported to still remain intact.
In summary, our studies helped to better understand the role of MAGP-1 during skin aging, and the findings indicated that the loss of MAGP-1 might contribute to or accelerate the visible signs of aging in the skin.
The mycolic acids of these glycolipids are noncovalently intercolated with the mAGP.
MAGP-2 can also interact with αvβ3 integrins via a RGD sequence that is not found in MAGP-1.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com