التفاصيل البيبلوغرافية
العنوان: |
The di-leucine motif in the host defense peptide LL-37 is essential for initiation of autophagy in human macrophages |
المؤلفون: |
Rokeya Sultana Rekha, Avinash Padhi, Nicolai Frengen, Julia Hauenstein, Ákos Végvári, Birgitta Agerberth, Robert Månsson, Guðmundur H. Guðmundsson, Peter Bergman |
المصدر: |
Cell Reports, Vol 44, Iss 1, Pp 115031- (2025) |
بيانات النشر: |
Elsevier, 2025. |
سنة النشر: |
2025 |
المجموعة: |
LCC:Biology (General) |
مصطلحات موضوعية: |
CP: Immunology, Biology (General), QH301-705.5 |
الوصف: |
Summary: The human cathelicidin peptide LL-37 induces autophagy in human macrophages. Different post-translational modifications (PTMs) such as citrullination, acetylation, and formylation impact LL-37, yet their effect on autophagy remains unknown. Thus, we set out to study how the cellular source could impact PTM of LL-37 and subsequent effects on autophagy initiation. Neutrophil-released LL-37 failed to induce autophagy, unlike macrophage-released LL-37. Mass spectrometry analysis revealed modifications on neutrophil-derived LL-37, especially at the N terminus, while macrophage-derived LL-37 remained mostly native. Native LL-37 initiated autophagy, while formylated and acetylated versions did not. Truncated peptides lacking the N-terminal di-leucine motif or substituted with di-alanine did not initiate autophagy. Native LL-37 failed to initiate autophagy in macrophages with genetic inactivation of dipeptidyl peptidase-1. An intact N-terminal di-leucine motif in LL-37 was crucial for autophagy initiation, and modifications abrogated the effects. This pathway presents a novel way to regulate the effects of LL-37 in infection or inflammation. |
نوع الوثيقة: |
article |
وصف الملف: |
electronic resource |
اللغة: |
English |
تدمد: |
2211-1247 |
Relation: |
http://www.sciencedirect.com/science/article/pii/S2211124724013822; https://doaj.org/toc/2211-1247 |
DOI: |
10.1016/j.celrep.2024.115031 |
URL الوصول: |
https://doaj.org/article/4d9decee0cd94bef8f0724da29e4b9cd |
رقم الانضمام: |
edsdoj.4d9decee0cd94bef8f0724da29e4b9cd |
قاعدة البيانات: |
Directory of Open Access Journals |