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1.
Br J Dermatol ; 156(6): 1251-7, 2007 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-17535223

RESUMEN

BACKGROUND: Curettage and dermabrasion are effective in treating giant congenital melanocytic naevi (GCMN). We report two patients with rapid, severe postoperative repigmentation. To the best of our knowledge this is the first report on the histological features of such patients. OBJECTIVES: We wish to call attention to histological features that may cause rapid, severe repigmentation after curettage and dermabrasion of medium to giant CMN. PATIENTS/METHODS: From 1998 to 2002, we treated 23 patients with medium to giant CMN with curettage and dermabrasion. Patients being treated ranged in age from 1 month to 19 years. Histological samples were taken from the centre of naevi in all patients during surgery. Histological types were 12 intradermal and 11 compound. Follow-up after curettage lasted at least 3 years. RESULTS: Among our 23 patients only two showed repigmentation soon after surgery. Histological sections from these two patients indicated naevoid cells in the deep dermis along hair follicles or sebaceous glands. However, no such pigmented naevoid cells along hair follicles were observed in samples from patients successfully treated with curettage and dermabrasion with less repigmentation. CONCLUSIONS: Although we saw only two cases of repigmentation soon after curettage and dermabrasion, we suspect a correlation between pigmented naevoid cells around hair follicles and repigmentation. If histological sections of skin biopsies show pigmented cells along hair follicles in the deep dermis, other treatments such as total skin resection followed by skin grafting or tissue expansion may be better choices than curettage or dermabrasion.


Asunto(s)
Legrado/métodos , Dermabrasión/métodos , Nevo Pigmentado/patología , Trastornos de la Pigmentación/etiología , Femenino , Humanos , Lactante , Recién Nacido , Masculino , Nevo Pigmentado/congénito , Nevo Pigmentado/cirugía , Recurrencia
2.
Biochem Biophys Res Commun ; 266(1): 216-21, 1999 Dec 09.
Artículo en Inglés | MEDLINE | ID: mdl-10581192

RESUMEN

Dishevelled (Dsh) is involved in both Wingless (Wg) and Frizzled (Fz) signaling pathways. To further determine the function of Dsh, we have performed yeast two-hybrid screening and isolated several genes encoding the molecules associated with the PDZ domain of Dvl1, one of the murine Dsh homologs. During the screening, we found that EPS8, which is a substrate for activated EGF receptor (EGFR), specifically interacted with Dvl1. This interaction was also confirmed in vitro. Through transfection studies, we observed the mutual action between Dvl1 and EPS8. Dvl1 was hyperphosphorylated in the presence of EPS8, whereas the tyrosine phosphorylation of EPS8 by activated EGFR was inhibited in the presence of Dvl1. Immunohistochemistry showed that Dvl1 and EPS8 expression overlap in particular tissues during organogenesis. These results indicate that interaction between Dvl1 and receptor tyrosine kinase signal plays certain roles in developmental events.


Asunto(s)
Fosfoproteínas/metabolismo , Proteínas/metabolismo , Fosfatasa Ácida/metabolismo , Proteínas Adaptadoras Transductoras de Señales , Animales , Línea Celular , Sistema Nervioso Central/embriología , Sistema Nervioso Central/metabolismo , Proteínas del Citoesqueleto , Proteínas Dishevelled , Desarrollo Embrionario y Fetal , Factor de Crecimiento Epidérmico/antagonistas & inhibidores , Factor de Crecimiento Epidérmico/farmacología , Receptores ErbB/antagonistas & inhibidores , Receptores ErbB/metabolismo , Expresión Génica , Inmunohistoquímica , Ratones , Especificidad de Órganos , Fosfoproteínas/química , Fosfoproteínas/genética , Fosforilación/efectos de los fármacos , Fosfotirosina/metabolismo , Pruebas de Precipitina , Unión Proteica , Proteínas/química , Proteínas/genética , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/metabolismo , Transfección , Técnicas del Sistema de Dos Híbridos
3.
Mol Pathol ; 56(2): 127-8, 2003 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-12665631

RESUMEN

A proposal is put forth to unify the nomenclature of the CCN family of secreted, cysteine rich regulatory proteins. In the order of their description in the literature, CCN1 (CYR61), CCN2 (CTGF), CCN3 (NOV), CCN4 (WISP-1), CCN5 (WISP-2), and CCN6 (WISP-3) constitute a family of matricellular proteins that regulate cell adhesion, migration, proliferation, survival, and differentiation, at least in part through integrin mediated mechanisms. This proposal is endorsed by the International CCN Society and will serve to eliminate confusion from the multiple names that have been given to these molecules.


Asunto(s)
Proteínas Inmediatas-Precoces , Péptidos y Proteínas de Señalización Intercelular , Terminología como Asunto , Factor de Crecimiento del Tejido Conjuntivo , Proteína 61 Rica en Cisteína , Humanos , Proteína Hiperexpresada del Nefroblastoma , Sociedades Científicas
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