Characterization of two tropomyosin isoforms from the fast skeletal muscle of bluefin tuna Thunnus thynnusorientalis

Ochiai, Yoshihiro; Ozawa, Hideo; Huang, Ming Chih; Watabe, Shugo

doi:10.1016/j.abb.2010.07.015

Cited by 14 publications

(12 citation statements)

References 30 publications

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“…It is still an open question why the protein sequence deduced from the cDNA sequence differs at three positions from that obtained by mass spectrometry. Isoforms of tropomyosins have been described form other species, but these differ from each other at more than a few positions [35,49]. As expected the Ore m 4 sequence was very similar to those of other fish tropomyosins.…”

Section: K a L T D K L K E A E T R A E F A E R S Vsupporting

confidence: 74%

“…Tropomyosins are actin-binding proteins that regulate actin mechanics and are thus important for muscle contraction. Isoforms of tropomyosins have been described form other species, but these differ from each other at more than a few positions [35,49]. The nature of the Ore m 4 allergen was further corroborated using ELISA inhibition which showed that Ore m 4 IgE cross-reacted with tropomyosin from shrimp.…”

Section: K a L T D K L K E A E T R A E F A E R S Vmentioning

confidence: 87%

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Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen

Liu

Holck

Yang

et al. 2013

Clin Experimental Allergy

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TMs are the major allergens in allergy to crustaceans. Auto-antibodies against human TM isoform 5 have been implicated as a causative agent in inflammatory bowel disease (IBD). Intriguingly, six of the 10 tilapia allergic patients had also been diagnosed with IBD, corroborating a connection between allergy and IBD. To our knowledge, this is the first report of tropomyosin from vertebrates as an allergen.

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Section: K a L T D K L K E A E T R A E F A E R S Vsupporting

confidence: 74%

Section: K a L T D K L K E A E T R A E F A E R S Vmentioning

confidence: 87%

Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen

Liu

Holck

Yang

et al. 2013

Clin Experimental Allergy

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“…Beberapa peneliti menemukan infeksi larva nematoda pada ikan-ikan konsumsi dari perairan Indonesia, umumnya teridentifikasi sebagai Anisakis sp. Sebaran geografis larva anisakid meliputi perairan Pantai Selatan Kulon Progo-Jogjakarta (Setyobudi et al, 2011), Perairan Laut Bali (Palm et al, 2008) (WHO, 2008). Dengan ditemukannya infeksi anisakis pada ikan-ikan konsumsi maka Anisakiasis berpeluang untuk berkembang di Indonesia.…”

Section: Pendahuluan1unclassified

“…Pada otot ikan salmon TM terdapat dalam 2 isoform yaitu α-TM dan β-TM (Helley et al, 1995). Pada ikan blue fin tuna (Thunnus thynnusorientalis) juga ditemukan isoform yang sama dari TM (Ochiai et al, 2010). Blue fin tuna dan K pelamis adalah kelompok tuna dari famili Scrombidae.…”

Section: Protein Ikan Berdasarkan Berat Molekulunclassified

POTENSI ALERGI AKIBAT INFEKSI Anisakis typica PADA DAGING IKAN CAKALANG

Soewarlan

2016

jtip

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Anisakid larvae are zoonotic parasites that can cause allergy in human consuming infected raw fish. This research aims to identify the allergenic potential of skipjack flesh infected by Anisakis typica larvae stage 3 (L3). Identification was done through antigen detection in protein profile of the fillet. Samples from the white part of the skipjack flesh of both infected and non-infected flesh, as well as L3 A. typica were analysed using SDS PAGE. Futhermore, the molecular weights from the analysis were compared to the literature references of protein profile. The result showed that both samples have 8 similar bands of protein, but 4 bands were found only from the infected fish. The four bands of 212, 66, 59 and 44 kDa were antigens of L3 A. typica. The presence of antigen from L3 A. typical in the infected flesh may induce allergy when the fish is consumed.

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“…The increasing complexity of metazoa is paralleled by increasing numbers of tropomyosin genes and larger numbers of alternatelyspliced isoforms. Phylogenetic analysis of the tropomyosin genes shows that they are under a high degree of selection pressure and this is most dramatically seen in the vertebrate tropomyosins (Barua et al, 2011;Ochiai et al, 2010) (Fig. 5).…”

Section: Integration Of Tropomyosins Into Actin Filamentsmentioning

confidence: 99%

The evolution of compositionally and functionally distinct actin filaments

Gunning

Ghoshdastider

Whitaker

et al. 2015

Journal of Cell Science

255

198

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The actin filament is astonishingly well conserved across a diverse set of eukaryotic species. It has essentially remained unchanged in the billion years that separate yeast, Arabidopsis and man. In contrast, bacterial actin-like proteins have diverged to the extreme, and many of them are not readily identified from sequence-based homology searches. Here, we present phylogenetic analyses that point to an evolutionary drive to diversify actin filament composition across kingdoms. Bacteria use a one-filament-one-function system to create distinct filament systems within a single cell. In contrast, eukaryotic actin is a universal force provider in a wide range of processes. In plants, there has been an expansion of the number of closely related actin genes, whereas in fungi and metazoa diversification in tropomyosins has increased the compositional variety in actin filament systems. Both mechanisms dictate the subset of actin-binding proteins that interact with each filament type, leading to specialization in function. In this Hypothesis, we thus propose that different mechanisms were selected in bacteria, plants and metazoa, which achieved actin filament compositional variation leading to the expansion of their functional diversity.

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Characterization of two tropomyosin isoforms from the fast skeletal muscle of bluefin tuna Thunnus thynnusorientalis

Cited by 14 publications

References 30 publications

Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen

Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen

POTENSI ALERGI AKIBAT INFEKSI Anisakis typica PADA DAGING IKAN CAKALANG

The evolution of compositionally and functionally distinct actin filaments

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