Expression Pattern of WWP1 in Muscular Dystrophic and Normal Chickens

Abstract

The WW domain containing E ubiquitin protein ligase (WWP ) is classified into one of ubiquitin ligases which play an important role in ubiquitin-proteasome pathway. Previously, we identified the gene as a candidate gene of chicken muscular dystrophy by linkage analysis and sequence comparison. However, the mechanism causing pathological changes and underlaying gene function remains elucidated. In the present study, we analyzed the gene expression in various muscles and tissues of normal chickens, and compared with those from muscular dystrophic chickens. Two mRNA isoforms were detected in all tissues examined and revealed almost equal expression level. The expression of dystrophic chickens was decreased in almost all skeletal muscles including una ected muscles. These data indicate that there might not be a causal relationship between the alteration of expression level and the severity of muscular dystrophy.: chicken, expression analysis, fast twitch muscle fiber, muscular dystrophy, WWP Poser ; Augustine, ). The WW domain has two conserved tryptophan residues and binds prolineThe WW domain containing E ubiquitin protein ligase rich region (Sudol ). HECT domain, similar to ( ) is classified into an ubiquitin ligase (E ) which E s structurally, has a cysteine residue as an active center plays an important role in ubiquitin-proteasome pathway that transfers the activated Ub from E onto first itself, (UPP) to degrade unneeded or damaged proteins and then onto its substrates (Jackson ). (Sche ner and Staub,). E recognizes and catalyzes The muscular dystrophies are the group of inherited ubiquitin (Ub) conjugation to specific protein substrates diseases with progressive weakness and degeneration of (Liu, ). Comparative genome analysis reveals few skeletal muscle (Partridge, ). It is well known that genes encoding E , tens of E encoding genes and hunabnormalities of muscle proteins linking sarcolemma and dreds of E encoding genes (Semple ). basal lamina lead to cause muscular dystrophies (Lisi and The gene is classified into HECT (homologous Cohn, ), but there are a number of muscular to the E -AP carboxyl terminus)-type E which possesses dystrophies and related diseases of which causes are still one C domain, multiple WW domains and one HECT unknown. We identified gene as a candidate domain (Pirozzi ; Flasza ). The C responsible for the chicken muscular dystrophy by the domain binds to the cellular membranes in a linkage analysis (Matsumoto ) and the seCa -dependent manner (Plant )

Identification of the Gene Responsible for Chicken Muscular Dystrophy

“…Moreover, the expression was altered in liver and kidney, unaffected tissues. The result suggested that WWP1 expression level lowered in dystrophic phenotype is not directly related to the cause of disease in chicken muscular dystrophy, whereas mutated WWP1 does not function properly to cause the onset of chicken muscular dystrophy (Matsumoto et al, 2009).…”

Caveolin-3: A Causative Process of Chicken Muscular Dystrophy

“…Moreover, it is implicated in several diseases, such as cancers, infectious diseases, neurological diseases and aging. Northern blot analysis shows a high expression of transcripts in skeletal and cardiac muscles [ 61 ]. Full-length of chicken WWP1 shares 83% amino acid identity with human WWP1 protein [ 62 ].…”

“…The WWP1 is the most prominent among the family members tested. They are characterized by a similar domain structure with an N-terminal, membrane interacting C2 domain, 2–4 WW domains (three domains in the case of chickens) and a C-terminal HECT domain [ 61 ] (see Figure 5 a). Despite intensive studies on oncogenic characters, the role of WWP1 to muscular functions has not yet been fully understood.…”