title: Hsp40 is involved in cilia regeneration in sea urchin embryos.
abstract: In a previous paper we demonstrated that, in Paracentrotus lividus embryos, deciliation represents a specific kind of stress that induces an increase in the levels of an acidic protein of about 40 kD (p40). Here we report that deciliation also induces an increase in Hsp40 chaperone levels and enhancement of its ectodermal localization. We suggest that Hsp40 might play a chaperoning role in cilia regeneration.
authors: Dipartimento di Biologia Cellulare e dello Sviluppo Alberto Monroy, Palermo, Italy. cascate@unipa.it
authors: Caterina
authors: C
authors: Casano
authors: Fabrizio
authors: F
authors: Gianguzza
authors: Maria C
authors: MC
authors: Roccheri
authors: Rossana
authors: R
authors: Di Giorgi
authors: Luigia
authors: L
authors: Maenza
authors: Maria A
authors: MA
authors: Ragusa
mesh_terms: D000818:Animals; D018385:Centrosome / Q000378:metabolism; D002923:Cilia / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D046508:Culture Techniques; D004475:Ectoderm / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004625:Embryo, Nonmammalian / Q000378:metabolism; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D018832:Molecular Chaperones / Q000096:biosynthesis*; D012038:Regeneration; D012617:Sea Urchins; D013312:Stress, Physiological / Q000378:metabolism*
chemical_list: D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones