Reactome | PRTN3 cleaves CAMP(31-170) to generate CAMP(134-170)

PRTN3 cleaves CAMP(31-170) to generate CAMP(134-170)

Stable Identifier

R-HSA-6801687

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

extracellular region

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

PRTN3 cleaves CAMP(31-170) to generate CAMP(134-170)

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Cathelicidin (CAMP, LL-37 and hCAP), is a major protein in specific granules of neutrophils (Sorensen O et al. 1997). CAMP is also present in subpopulations of lymphocytes and monocytes, squamous epithelial cells and keratinocytes (Agerberth B et al. 2000; Frohm M et al. 1997; Frohm Nilsson M et al. 1999). CAMP is synthesized as preproprotein (Zanetti M et al. 1995). After removal of the signal peptide, CAMP(31-170) is stored in granules as an inactive proform (Sorensen OE et al. 2001). CAMP (31-170) was shown to be processed extracellularly to the active antimicrobial peptide LL-37 (CAMP(134-170)) by proteinase 3 (PRTN3) (Sorensen OE et al. 2001).

Literature References

PubMed ID	Title	Journal	Year
11389039	Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3 Sørensen, OE, Follin, P, Johnsen, AH, Calafat, J, Tjabringa, GS, Hiemstra, PS, Borregaard, N	Blood	2001