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Identification of novel peptide motifs in the serpin maspin that affect vascular smooth muscle cell function
S E Jenkinson1, L J Brown2, J Ombor2
1Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, UK; Institute of Cardiovascular Sciences, Institute for Biomedical Research, The Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Abstract:
Maspin is a non-inhibitory member of the serpin family that affects cell behaviours related to migration and survival. We have previously shown that peptides of the isolated G α-helix (G-helix) domain of maspin show bioactivity. Migration, invasion, adhesion and proliferation of vascular smooth muscle cells (VSMC) are important processes that contribute to the build-up of atherosclerotic plaques. Here we report the use of functional assays of these behaviours to investigate whether other maspin-derived peptides impact directly on VSMC; focusing on potential anti-atherogenic properties. We designed 18 new peptides from the structural moieties of maspin above ten amino acid residues in length and considered them beside the existing G-helix peptides. Of the novel peptides screened those with the sequences of maspin strand 4 and 5 of beta sheet B (S4B and S5B) reduced VSMC migration, invasion and proliferation, as well as increasing cell adhesion. A longer peptide combining these consecutive sequences showed a potentiation of responses, and a 7-mer contained all essential elements for functionality. This is the first time that these parts of maspin have been highlighted as having key roles affecting cell function. We present evidence for a mechanism whereby S4B and S5B act through ERK1/2 and AMP-activated protein kinase (AMPK) to influence VSMC responses.
Insights
New maspin peptides, specifically S4B and S5B, effectively reduce vascular smooth muscle cell (VSMC) migration, invasion, and proliferation, while enhancing adhesion, suggesting anti-atherogenic potential.
Area of Science:
- Biochemistry
- Molecular Biology
- Cardiovascular Research
Background:
- Maspin, a serpin family member, influences cell migration and survival.
- Previous studies identified bioactivity in maspin's G-helix domain peptides.
- Vascular smooth muscle cell (VSMC) behaviors are critical in atherosclerotic plaque development.
Purpose of the Study:
- To investigate the anti-atherogenic properties of novel maspin-derived peptides on VSMCs.
- To identify specific maspin structural moieties that impact VSMC functions.
- To explore the mechanistic pathways involved in maspin peptide activity.
Main Methods:
- Design and synthesis of 18 new maspin-derived peptides (>10 amino acids).
- Functional assays assessing VSMC migration, invasion, adhesion, and proliferation.
- Screening of novel peptides alongside existing G-helix peptides.
- Mechanistic studies involving ERK1/2 and AMPK signaling pathways.
Main Results:
- Maspin strand 4 and 5 of beta sheet B (S4B and S5B) peptides significantly reduced VSMC migration, invasion, and proliferation.
- These S4B and S5B peptides also increased VSMC adhesion.
- A combined peptide potentiated these effects, and a 7-mer peptide contained essential functional elements.
- Evidence suggests S4B and S5B act via ERK1/2 and AMPK pathways.
Conclusions:
- Maspin strand 4 and 5 of beta sheet B (S4B and S5B) are key functional domains with anti-atherogenic potential.
- These maspin peptides directly modulate VSMC behavior, impacting key processes in atherosclerosis.
- The findings reveal a novel mechanism involving ERK1/2 and AMPK signaling for maspin peptide activity in VSMCs.
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