Use of a proteomics approach to identify favourable conditions for production of good quality lambskin leather

Abstract

It is necessary to understand the changes that occur during the initial processing of lamb skins, because these will affect the final quality of the leather. The types of collagen, their macro and micro structures, the presence of proteins other than collagens, and the quantity and the type of proteoglycans, all have a profound effect on the quality of leather. Proteins isolated from untreated or raw sheep skin and from pickled skin (skins treated with sodium sulfide and lime followed by bating with enzymes, then preserved in sodium chloride and sulfuric acid) were significantly different when analysed by use of 2D gel electrophoresis and mass spectrometry. Agarose gel electrophoresis with a very sensitive sequential staining procedure has been used to identify the glycosaminoglycans present in raw and treated skin and their impact on quality of leather. Results showed that effective removal of proteoglycans acting as inter-fibrillar adhesives of collagen fibrils seemed to improve leather quality. Removal of these molecules not only opens up the fibre structure of the skin but may also be important in wool removal. The presence of elastin, which imparts elastic properties to skin, is of significant importance to tanners. The amino acids desmosine and isodesmosine, found exclusively in elastin, were quantitatively analysed to assess the role of elastin in leather quality.

A straightforward method to produce decellularized dermis-based matrices for tumour cell cultures

“…In particular, the processes of unhairing, liming/deliming, bating and picking have been optimized in order to remove cells, hairs, non-collagenous proteins and fats, yet they have to preserve the native fibrillar architecture of the animal skin. Proteomics studies performed on lambskin, analogous to the skin we used in this article, reported that pickled skins are almost entirely constituted by fibrillar collagen with a low percentage of elastin (~3% in weight) and traces of decorin (Choudhury et al, 2006). Washing with PBS removes inorganic salts that are normally present in pickled skin, which might be harmful for cell cultures.…”

Characterizing historical textiles and clothing with proteomics

“…Table 3 shows the main proteins identified in different collagen-based substrates. Proteomics analysis of leather indicates that de-hairing and tanning treatments not only removes the keratins from hair and the epidermis but also minor proteins such as proteoglycans and elastin [66]. In archaeological leather, mainly collagen has been detected [9].…”

Mass spectrometry and animal science: Protein identification strategies and particularities of farm animal species

“…In fact, numerous examples may be found in the literature, on that same variety of tissues and products. They include muscle [1,2], meat products and their transformation [3], liver and related products [4], milk and dairy products [5], eggs [6,7], honeybee products [8], animal fibers like wool, cashmere or mohair [9], hides [10], reproductive organs and reproduction-related fluids [11], such as sperm or blood-based fluids, namely serum or plasma [12]. The afore-mentioned complexity is further increased if farm animal proteomics, includes an increasing number of disease and parasitosis causing agents, such as bacteria, viruses and protozoa, as well as possible vectors of such diseases namely ticks, flies and mosquitoes.…”

“…In earlier studies, the bulk of proteomic work seems to rely on PMF, a strategy used for instance in horse serum [117], cattle mammary gland [118] and adipocytes [119], lambskin leather [10] and ovine liver [120]. Although gradually losing importance, PMF is still used in recent studies such as those by Sun et al [121] on the proteomic mechanisms of infection of pigs with Swine fever virus.…”