Serpinin in the Skin.

Cristina Fraquelli,Zenon Pidsudko,Vinay Kumar Sharma,Josef Troger,Georgios Blatsios,Maria Nolano,Jasmine Hauzinger,Christian Humpel,Peng Loh,Vincenzo Provitera

doi:10.3390/biomedicines10010183

Abstract

The serpinins are relatively novel peptides generated by proteolytic processing of chromogranin A and they are comprised of free serpinin, serpinin-RRG and pGlu-serpinin. In this study, the presence and source of these peptides were studied in the skin. By Western blot analysis, a 40 kDa and a 50 kDa protein containing the sequence of serpinin were detected in the trigeminal ganglion and dorsal root ganglia in rats but none in the skin. RP-HPLC followed by EIA revealed that the three serpinins are present in similar, moderate amounts in rat dorsal root ganglia, whereas in the rat skin, free serpinin represents the predominant molecular form. There were abundant serpinin-positive cells in rat dorsal root ganglia and colocalization with substance P was evident. However, much more widespread distribution of the serpinins was found in dorsal root ganglia when compared with substance P. In the skin, serpinin immunoreactivity was found in sensory nerves and showed colocalization with substance P; as well, some was present in autonomic nerves. Thus, although not exclusively, there is evidence that serpinin is a constituent of the sensory innervation of the skin. The serpinins are biologically highly active and might therefore be of functional significance in the skin.

Highlights

Introduction published maps and institutional affilThe serpinins are relatively novel neuropeptides that are generated by proteolytic processing of chromogranin (Cg) A [1,2]
The most important finding of this study is that serpinin is a constituent of the sensory innervation of the skin as are the CgB-derived peptides PE-11 and secretolytin [16]
Certain granin-derived peptides have been demonstrated to be a constituent of the sensory innervation of the eye, in particular the SgII-derived neuropeptide secretoneurin [17], the CgB-derived peptide PE-11 [18] and the CgA-derived peptides GE-25 [19], catestatin [14] and serpinin [12]

Summary

Introduction

Introduction published maps and institutional affilThe serpinins are relatively novel neuropeptides that are generated by proteolytic processing of chromogranin (Cg) A [1,2]. CgA belongs to the family of granins, which are the acidic proteins of secretory granules in a variety of endocrine and neuroendocrine cells as well as cells of the central and peripheral nervous system, where they are stored in large dense core vesicles. They comprise CgB and secretogranin (Sg) II [3,4]. Several fragments are generated by proteolytic processing of the granins, such as catestatin, pancreastatin, vasostatin, serpinin or GE-25 by proteolytic processing of CgA, secretolytin or PE-11 by proteolytic processing of CgB and secretoneurin by proteolytic processing of SgII (review, see [6]).

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Methods

Conclusion