CAMP

CAMP Full Name

cathelicidin antimicrobial peptide

CAMP Introduction

Cathelicidin antimicrobial peptide (CAMP) is an antimicrobial peptide encoded by the CAMP gene in the human body. Cathelicidins play a crucial role in the innate immune defense of mammals against invasive bacterial infections. The peptides of the protease family are classified as antimicrobial peptides (AMPs). The AMP family also includes defense factors. Although defense factors share common structural features, protease related peptides exhibit high heterogeneity. Members of the antimicrobial peptide cathelicidin family are characterized by highly conserved regions (cathelin domains) and highly variable cathelicidin peptide domains. Cathelicidin peptides have been isolated from many different species of mammals, including marsupials. Cathelicidins mainly exist in neutrophils, monocytes, mast cells, dendritic cells, and macrophages. After being activated by bacteria, viruses, fungi, parasites, or hormones 1,25-D, 1,25-D is the hormone active form of vitamin D. They also exist in other cells, including epithelial cells and human keratinocytes. Some viruses have evolved immune regulatory mechanisms by downregulating cellular vitamin D receptors to avoid exposure to cathelicidin.

Figure.The CAMP signaling pathway is involved in cancer cell proliferation, migration, and tumor progression.(Source: Kuroda, Kengo, et al, 2015)

Cathelicidin antimicrobial peptides (CAMPs) are an important class of endogenous antimicrobial peptides in living organisms and are core effector molecules of the innate immune system. Its name comes from its unique dual domain structure: a highly conserved N-terminal "cathelin" - like domain and a C-terminal variable active peptide segment with broad-spectrum antibacterial activity. In humans, CAMP usually refers to LL-37, which is an active peptide composed of 37 amino acids released from its 18 kDa precursor protein (hCAP18) after proteolytic cleavage. It is named after its first two amino acids being "LL". As the first line of defense for the host, CAMP not only plays a crucial role in directly killing pathogens, but also extensively participates in complex biological processes such as immune regulation, wound healing, cell chemotaxis, and inflammatory response. It is an important bridge connecting innate immunity and acquired immunity.

Application
The research on the AMP family, especially its mechanism of action, has been ongoing for nearly 20 years. Despite ongoing interest, treatment methods derived from or utilizing AMP have not been widely used in clinical practice for various reasons. Firstly, the bioavailability window of AMP candidate drugs is narrow because peptides are quickly broken down by proteases. Secondly, the production of peptide drugs is more expensive than small molecule drugs, which is problematic because peptide drugs must be administered in large doses to counteract rapid enzymatic degradation. These characteristics also limit the route of administration, typically through injection, infusion, or sustained-release therapy.

Alternate Names for CAMP

CAMP; cathelicidin antimicrobial peptide; LL37; CAP18; CRAMP; HSD26; CAP-18; FALL39; FALL-39; 18 kDa cationic antimicrobial protein;

• 1.Kuroda, Kengo, et al. The human cathelicidin antimicrobial peptide LL-37 and mimics are potential anticancer drugs. Frontiers in oncology, 2015, 5: 144.