ArticleCellular and molecular life sciences : CMLS2012
Chromogranin A binds to αvβ6-integrin and promotes wound healing in mice.
Article in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Blockade of αvβ6 and αvβ8 integrins with a chromogranin A-derived peptide inhibits TGFβ activation in tumors and suppresses tumor growth.Journal of experimental & clinical cancer research : CR · 2025Article
- A stapled chromogranin A-derived peptide homes in on tumors that express αvβ6 or αvβ8 integrins.International journal of biological sciences · 2023Article
- Neuropilin-1 and Integrins as Receptors for Chromogranin A-Derived Peptides.Pharmaceutics · 2022Review
- Chromogranin A and its fragments in cardiovascular, immunometabolic, and cancer regulation.Annals of the New York Academy of Sciences · 2019Review
- Circulating chromogranin A and its fragments as diagnostic and prognostic disease markers.Pflugers Archiv : European journal of physiology · 2018Review
- Article
- Chromogranin-A production and fragmentation in patients with Takayasu arteritis.Arthritis research & therapy · 2016Article
- Chromogranin A: a paradoxical player in angiogenesis and vascular biology.Cellular and molecular life sciences : CMLS · 2015Review
- Integrins in Wound Healing.Advances in wound care · 2014Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chromogranin A (CgA), a secretory protein expressed by many neuroendocrine cells, neurons, cardiomyocytes, and keratinocytes, is the precursor of various peptides that regulate the carbohydrate/lipid metabolism and the cardiovascular system. We have found that CgA, locally administered to injured mice, can accelerate keratinocyte proliferation and wound healing. This biological activity was abolished by the Asp(45)Glu mutation. CgA and its N-terminal fragments, but not the corresponding Asp(45)Glu mutants, could selectively recognize the αvβ6-integrin on keratinocytes (a cell-adhesion receptor that is up-regulated during wound healing) and regulate keratinocyte adhesion, proliferation, and migration. No binding was observed to other integrins such as αvβ3, αvβ5, αvβ8, α5β1, α1β1, α3β1, α6β4, α6β7 and α9β1. Structure-activity studies showed that the entire CgA(39-63) region is crucial for αvβ6 recognition (K(i) = 7 nM). This region contains an RGD site (residues CgA(43-45)) followed by an amphipathic α-helix (residues CgA(47-63)), both crucial for binding affinity and selectivity. These results suggest that the interaction of the RGD/α-helix motif of CgA with αvβ6 regulates keratinocyte physiology in wound healing.
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