{'fraction_non_alphanumeric': 0.022834360275462123, 'fraction_numerical': 0.0032620514679231605, 'mean_word_length': 5.188340807174888, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
A de novo heterozygous point mutation in the p63 gene causing the syndrome of ectrodactyly, ectodermal dysplasia and facial clefting

with weak expression of fibronectin also in the lower dermis. In contrast, vitronectin and undulin were not expressed in basement membranes but instead only in interstitial dermal connective tissue, with weaker expression of undulin in the lower dermis (see also Fig. 1a). Expression of collagen IV and laminin was restricted to basement membranes. In most cases and with most ECM proteins studied, there was a striking modulation of expression in the three inflammatory skin diseases which was, however, not consistent in all specimens (Table 2). In psoriasis, most ECM proteins were downregulated, except for an upregulation of tenascin in about 70% of the specimens and of undulin subepidermally (Fig. 1b). In lichen planus and morphoea, fibronectin and tenascin were upregulated in the dermis, whereas vitronectin and undulin were unchanged. As in psoriasis, laminin and collagen IV were decreased and ⁄ or fragmented in almost all cases at the dermoepidermal junction, whereas expression at basement membranes around vessels and appendages was unaltered in comparison with normal skin (Fig. 2). A close apposition to ECM molecules was seen only for laminin and collagen IV at both the dermoepidermal junction and around vessels (not shown). The present findings are novel in that, for the first time, a close apposition of mature mast cells to the major basement components collagen IV and laminin, particularly around vascular basement membranes, is demonstrated in normal and diseased skin. Furthermore, our findings fit previous in vitro studies where collagen IV and laminin have been shown to interact with immature murine and leukaemic human mast cells (HMC-1 cell line). The lack of contacts with fibronectin and vitronectin, as described before, may be due to differences in cultured immature vs. normal tissue mast cells studied here. The present data are in agreement with previous studies regarding the distribution and expression of ECM proteins in normal and diseased skin (for example, see Schalkwijk et al.). The findings regarding tenascin in cutaneous lichen planus, vitronectin in morphoea, and undulin in lichen planus and morphoea are, however, new. The functional significance of the present findings most probably relates to the interaction of mast cells with basement membranes and the effect of these cells on keratinocytes, endothelial cells and fibroblasts, by the possible induction of production of a number of growth factors for these cells. This should allow for the maintenance of the functional integrity of vessels and epithelia via the stimulation of laminin and collagen IV production.