Babilas, P., Fiebig, B. S., Aslanidis, C., Hansen, J., Röcken, C., Schröder, J., Schmitz, G., Weber, B. H. F., Landthaler, M. and Vogt, T. (2009) Identification of an oncostatin M receptor mutation associated with familial primary cutaneous amyloidosis. British Journal of Dermatology, 161 (4). pp. 944-947. DOI 10.1111/j.1365-2133.2009.09237.x.

Full text not available from this repository.

Abstract

Amyloid and amyloidosis describe a heterogeneous group of diseases which are characterized by the pathological extracellular deposition of autologous proteins in an antiparallel β‐sheet conformation forming nonbranching linear fibrils of indefinite length and an approximate diameter of 10–12 nm.1 These depositions share a common tinctorial property, i.e. the presence of a characteristic green birefringence in polarized light after staining with Congo red or with thioflavin T. More than 26 different proteins and peptides have been identified that are able to form amyloid and, depending on the histoanatomical distribution and amount, amyloid may cause progressive and life‐threatening organ dysfunction.2 Dependent on the deposition pattern amyloidosis may present as a localized or as a systemic disease and can be acquired or hereditary in nature.1, 2 Hereditary amyloidoses are caused by germline mutations, which increase the propensity of the respective protein to form cross‐β aggregates and deposit as amyloid. The further classification discriminates between primary amyloidosis (in the absence of an obvious predisposing disease) and secondary amyloidosis (if caused by a certain underlying disease). The subclassification of amyloidoses is based on the main protein constituent and therefore on the chemical composition of the amyloid fibrils.2
While primary cutaneous amyloidosis (PCA) is a relatively common skin disease in South America and Southwest Asia, it is rare in caucasians. The cutaneous amyloid is believed to originate mainly from degenerated keratin of apoptotic epidermal cells (amyloid K‐component).3-5 The secondary originators of cutaneous amyloid are immunoglobulins and the normal plasma glycoprotein serum amyloid P‐component.6 The histological correlate is a focal deposition of amyloid in the papillary dermis with a fibrillar degeneration of basal keratinocytes. While PCA is not associated with other systemic forms of amyloidosis, an accidental coexistence with multiple endocrine neoplasia type 2a has been reported.7-10 Even though the exact aetiology of PCA is still unknown to date, it is believed to be multifactorial in origin, including environmental and frictional epidermal damage, and immunological and other factors.2, 3
While most cases of PCA are sporadic, familial aggregation has been reported from South America, Taiwan and Southeast Asia.7, 10-16 With only three pedigrees published to date, hereditary cases appear extremely rare in caucasians.17-19 Familial aggregation and differences in susceptibility among ethnic groups have drawn the attention of amyloidosis researchers to investigate the genetic factors. In 2006 Lee et al. performed a genome‐wide scan for familial PCA (FPCA) in Taiwanese families and found evidence for significant linkage to chromosome 5p13.1–q11.2 in a subset of FPCA pedigrees.14 Subsequently, a candidate gene analysis in the genetically linked region on chromosome 5 revealed two distinct missense mutations in affected individuals of Brazilian pedigrees and pedigrees from the U.K. and South Africa in the OSMR gene, which encodes the oncostatin M (OSM) receptor (OSMR)‐β.12
In this work we analysed a caucasian family with FPCA for mutations in the OSMR gene.

Document Type:	Article
Keywords:	amyloidosischromosome 5 genetic linkage heterozygous missense mutation osmr gene multiple endocrine neoplasia lichen amyloidosis epidermal-keratinocytes skin generations activation type-2a cells
Research affiliation:	Kiel University > Kiel Marine Science OceanRep > The Future Ocean - Cluster of Excellence Kiel University
Refereed:	Yes
Open Access Journal?:	No
Publisher:	John Wiley & Sons: Blackwell Publishing
Projects:	Future Ocean
Date Deposited:	11 Feb 2011 12:15
Last Modified:	28 Aug 2019 13:50
URI:	https://oceanrep.geomar.de/id/eprint/9278

Actions (login required)

View Item