Developmental expression of high molecular weight tropomyosin isoforms in Mesocestoides corti

• Published in: Molecular and biochemical parasitology Vol. 175; no. 2; pp. 181 - 191
• Main Authors: Koziol, Uriel, Costábile, Alicia, Domínguez, María Fernanda, Iriarte, Andrés, Alvite, Gabriela, Kun, Alejandra, Castillo, Estela
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-02-2011; Amsterdam: Elsevier
• Subjects: Alternative splicing; Animals; Conserved Sequence; Development; DNA, Helminth - chemistry; DNA, Helminth - genetics; Echinococcus granulosus - genetics; Echinococcus multilocularis - genetics; EST; Evolution, Molecular; expressed sequence tag; Gene Duplication; high molecular weight; HMW; LMW; low molecular weight; MALDI-TOF; matrix-assisted laser desorption/ionization-time-of-flight; Mesocestoides; Mesocestoides - genetics; Mesocestoides - growth & development; Mice; Molecular Sequence Data; Muscle; Muscles - chemistry; PAGE; PBS; phosphate buffered saline; Phylogeny; polyacrilamide gel electrophoresis; Protein Isoforms - biosynthesis; Protein Isoforms - genetics; Schistosoma mansoni - genetics; SDS; Sequence Analysis, DNA; Sequence Homology; sodium dodecyl-sulfate; TPM; Tropomyosin; Tropomyosin - biosynthesis; Tropomyosin - genetics; Turbellaria - genetics; PBS; Alternative splicing; SDS; MALDI-TOF; Tropomyosin; EST; PAGE; Mesocestoides; TPM; HMW; LMW; Development; Muscle
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/j.molbiopara.2010.11.009

High molecular weight tropomyosin isoforms of Mesocestoides corti are expressed in muscle fibers, being markers for the final differentiation of the genital primordium. [Display omitted]
▶ Two tropomyosin genes isolated from Mesocestoides corti are conserved in neodermatans. ▶ Divergent tropomyosin isoforms are generated from each gene by alternative splicing. ▶ High molecular weight tropomyosin isoforms are expressed in muscle layers. ▶ These isoforms are markers for the development of primordia into genital ducts.
Tropomyosins are a family of actin-binding proteins with diverse roles in actin filament function. One of the best characterized roles is the regulation of muscle contraction. Tropomyosin isoforms can be generated from different genes, and from alternative promoters and alternative splicing from the same gene. In this work, we have isolated sequences for tropomyosin isoforms from the cestode Mesocestoides corti, and searched for tropomyosin genes and isoforms in other flatworms. Two genes are conserved in the cestodes M. corti and Echinococcus multilocularis, and in the trematode Schistosoma mansoni. Both genes have the same structure, and each gene gives rise to at least two different isoforms, a high molecular weight (HMW) and a low molecular weight (LMW) one. Because most exons are duplicated and spliced in a mutually exclusive fashion, isoforms from one gene only share one exon and are highly divergent. The gene duplication preceded the divergence of neodermatans and the planarian Schmidtea mediterranea. Further duplications occurred in Schmidtea, coupled to the selective loss of duplicated exons, resulting in genes that only code for HMW or LMW isoforms. A polyclonal antibody raised against a HMW tropomyosin from Echinococcus granulosus was demonstrated to specifically recognize HMW tropomyosin isoforms of M. corti, and used to study their expression during segmentation. HMW tropomyosins are expressed in muscle layers, with very low or absent levels in other tissues. No expression of HMW tropomyosins is present in early or late genital primordia, and expression only begins once muscle fibers develop in the genital ducts. Therefore, HMW tropomyosins are markers for the development of muscles during the final differentiation of genital primordia.