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M Tollin

Publications and source records attributed to M Tollin.

2 recordsLinked to original sources

Vernix caseosa as a multi-component defence system based on polypeptides, lipids and their interactions.

Vernix caseosa is a white cream-like substance that covers the skin of the foetus and the newborn baby. Recently, we discovered antimicrobial peptides/proteins such as LL-37 in vernix, suggesting host defence functions of vernix. In a proteomic approach, we have continued to characterize proteins in vernix and have identified 20 proteins, plus additional variant forms. The novel proteins identified, considered to be involved in host defence, are cystatin A, UGRP-1, and calgranulin A, B and C. These proteins add protective functions to vernix such as antifungal activity, opsonizing capacity, protease inhibition and parasite inactivation. The composition of the lipids in vernix has also been characterized and among these compounds the free fatty acids were found to exhibit antimicrobial activity. Interestingly, the vernix lipids enhance the antimicrobial activity of LL-37 in vitro, indicating interactions between lipids and antimicrobial peptides in vernix. In conclusion, vernix is a balanced cream of compounds involved in host defence, protecting the foetus and newborn against infection.

Amino Acid Sequence↗

Phylogeny, processing and expression of the rat cathelicidin rCRAMP: a model for innate antimicrobial peptides.

A database search identified a rat cDNA clone which phylogenetic analysis revealed to encode a cathelicidin most similar to mouse cathelicidin CRAMP. The analysis also showed that the evolutionary pattern of the cathelicidin family is lineage specific. The rat cathelicidin is called rCRAMP. Its peptide was isolated from granulocytes, and determined to be 43 amino acids long by mass spectrometry and N-terminal sequencing. Synthetic rCRAMP had antimicrobial activity. The expression of rCRAMP was investigated by reverse-transcriptase polymerase chain reaction followed by Southern hybridization and by Western blot analysis. rCRAMP was identified in granulocytes, thymus, testis, lung, mouth mucosa, tongue, oesophagus, colon, caecum and small intestine, a distribution similar to cathelicidins of mouse and human. The rat is a small laboratory animal with additional disease models available compared to the mouse. Our results open up the possibility to use the rat as a model system to study responses connected to cathelicidin expression in health and disease.

Amino Acid Sequence↗