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Review
. 2021 May 13;43(1):116-126.
doi: 10.3390/cimb43010010.

Immunomodulatory Expression of Cathelicidins Peptides in Pulp Inflammation and Regeneration: An Update

Nireeksha  1 , Sudhir Rama Varma  2   3 , Marah Damdoum  2 , Mohammed Amjed Alsaegh  4 , Mithra N Hegde  1 , Suchetha N Kumari  5 , Srinivasan Ramamurthy  6 , Jayaraj Narayanan  7 , Eisha Imran  8 , Juzer Shabbir  9 , Zohaib Khurshid  10
Affiliations
Review

Immunomodulatory Expression of Cathelicidins Peptides in Pulp Inflammation and Regeneration: An Update

Nireeksha et al. Curr Issues Mol Biol. .

Abstract

The role of inflammatory mediators in dental pulp is unique. The local environment of pulp responds to any changes in the physiology that are highly fundamental, like odontoblast cell differentiation and other secretory activity. The aim of this review is to assess the role of cathelicidins based on their capacity to heal wounds, their immunomodulatory potential, and their ability to stimulate cytokine production and stimulate immune-inflammatory response in pulp and periapex. Accessible electronic databases were searched to find studies reporting the role of cathelicidins in pulpal inflammation and regeneration published between September 2010 and September 2020. The search was performed using the following databases: Medline, Scopus, Web of Science, SciELO and PubMed. The electronic search was performed using the combination of keywords "cathelicidins" and "dental pulp inflammation". On the basis of previous studies, it can be inferred that LL-37 plays an important role in odontoblastic cell differentiation and stimulation of antimicrobial peptides. Furthermore, based on these outcomes, it can be concluded that LL-37 plays an important role in reparative dentin formation and provides signaling for defense by activating the innate immune system.

Keywords: cathelicidins; dental caries; dental pulp; inflammation; innate immunity.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Representation of the TLR2/1–Vitamin D cathelicidins (LL-37) pathway.
Figure 2
Figure 2
Pictorial depiction of LL-37 structure. (a) N-terminal fragment of LL-37, (b) Cathelin like the domain of human cathelicidins, (c) C-terminal fragment of LL-37.
Figure 3
Figure 3
Pictorial representation of LL-37 in electrospun fiber membrane as a potential pulp capping agent.
See this image and copyright information in PMC

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