Identification of High Molecular Weight Proteins in Squid Muscle by Western Blotting Analysis and Postmortem Rheological Changes

Kasamatsu, Chinatsu; Kimura, Sumiko; Kagawa, Mieko; Hatae, Keiko

doi:10.1271/bbb.68.1119

Cited by 7 publications

(3 citation statements)

References 29 publications

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“…Titin (also known as connectin) is a giant protein that works as a molecular spring for the passive elasticity of tissues. The degradation of this protein is one of the major reasons for quality changes in fresh raw squid tissues [51]. Potential tryptic (DGSWQNLVTVLGCLKPQFVNLQR, GYPPPIISWYR) bioactive titin peptides determined in this study may be used as potential biomarkers of quality changes or processing time in squid products ( Table 5).…”

Section: Putative Bioactive Peptidesmentioning

confidence: 94%

Characterization of the Jumbo Squid (Dosidicus gigas) Skin By-Product by Shotgun Proteomics and Protein-Based Bioinformatics

2019

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Jumbo squid (Dosidicus gigas) is one of the largest cephalopods, and represents an important economic fishery in several regions of the Pacific Ocean, from southern California in the United States to southern Chile. Large and considerable discards of this species, such as skin, have been reported to constitute an important source of potential by-products. In this paper, a shotgun proteomics approach was applied for the first time to the characterization of the jumbo squid (Dosidicus gigas) skin proteome. A total of 1004 different peptides belonging to 219 different proteins were identified. The final proteome compilation was investigated by integrated in-silico studies, including gene ontology (GO) term enrichment, pathways, and networks studies. Potential new valuable bioactive peptides such as antimicrobial, bioactive collagen peptides, antihypertensive and antitumoral peptides were predicted to be present in the jumbo squid skin proteome. The integration of the global proteomics results and the bioinformatics analysis of the jumbo squid skin proteome show a comprehensive knowledge of this fishery discard and provide potential bioactive peptides of this marine by-product.

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Section: Putative Bioactive Peptidesmentioning

confidence: 94%

Characterization of the Jumbo Squid (Dosidicus gigas) Skin By-Product by Shotgun Proteomics and Protein-Based Bioinformatics

2019

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“…Calpains may be responsible for the degradation during the early postmortem stage, while cathepsins may act in proteolysis during the later stage (Delbarre-Ladrat et al, 2006;Ahmed et al, 2015). Mitsuhashi et al (2002) reported that approximately 80% of titin in jack mackerel was reduced after storage for 24 h, indicating that titin was sensitively degraded during the early stage of storage (Kasamatsu et al, 2004). Desmin was partially degraded due to the calpains occurring at special sites, and it may be subjected to further degradation during the later stage due to the presence of cathepsins (Lomiwes et al, 2014).…”

Section: Desminmentioning

confidence: 99%

“…Therefore, the structural proteins, which are responsible for regulating the contraction of sarcomeres and maintaining the integrity of muscle tissues, are correlated to the variation of the myofibrillar structure. Some published reports have indicated that post‐mortem proteolysis could influence the degradation of large structural proteins such as titin and nebulin, which are abundant in the myofibrils and contribute to meat quality (Kasamatsu et al , ; Huff Lonergan et al , ; Wu et al , ). Titin accounts for approximately 30% of the total elasticity of myofibrils, and one end with nebulin is attached to the Z‐disc and parallel to the titin filament (Ahmed et al , ).…”

Section: Introductionmentioning

confidence: 99%

Degradation of structural proteins and their relationship with the quality of Mandarin fish (Siniperca chuatsi) during post‐mortem storage and cooking

Tang

Dai

et al. 2019

Int J of Food Sci Tech

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This study was carried out to investigate the changes in the microstructure and structural proteins (titin, nebulin, desmin and tropomyosin (TPM)) of mandarin fish muscle as well as the relationship between the structural proteins and the quality characteristics of fish muscle during post‐mortem storage and after cooking. During post‐mortem storage, titin was degraded initially, accompanied with an increase of the I‐band length. Subsequently, the degradation of desmin induced a gradual breakage of the myofibrils. The following degradation of nebulin accelerated the destruction of N2‐lines, which occurred with a slightly fuzzy Z‐disc. Finally, TPM began to degrade, and the remaining desmin was also degraded further. Principal component analysis (PCA) and correlation analysis indicated that the changes in the quality characteristics of fish muscle were intimately related to the degradation of structural proteins. Hence, these structural proteins could be the biomarkers to monitor the quality characteristics of fish muscle.

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Partial sequence of connectin-like 1200K-protein in obliquely striated muscle of a polychaete (Annelida): Evidence for structural diversity from vertebrate and invertebrate connectins

Izawa

Fukuzawa

Kanzawa

et al. 2006

J Muscle Res Cell Motil

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Vertebrate striated muscle contains the giant elastic protein connectin that maintains the position of the A-band at the center of the sarcomere during repeated muscular contraction and relaxation. Connectin-like molecules may perform conserved functions in vertebrate and invertebrate striated and oblique muscles, although less is known about the structure of invertebrate connectins at present. The protein that maintains such a structure is present not only in vertebrate striated muscle, but also in invertebrate striated and oblique muscle. In the present study, we analyzed the partial primary structure of a 1200K-protein, which is a connectin-like protein that is expressed in Neanthes sp. body wall muscle that is in turn composed of oblique muscle. Antibody screening of a cDNA library of Neanthes sp. body wall muscle identified two different clones. Both clones coded for a sequence predominantly comprised of the four amino acids proline (P), glutamate (E), valine (V) and lysine (K). One clone included a PEVK-like repeat sequence flanked by an Ig domain, while the other clone comprised a distinct 14 amino acid repeat rich in PEVK residues, flanked by a non-repetitive unique sequence. The PEVK region is found in vertebrate connectin and is thought to generate elasticity and be responsible for passive tension of the muscle. The antibodies produced against a portion of each clone both reacted with bands corresponding to 1200 kDa present in Neanthes sp. body wall muscle. Therefore, our results demonstrate that this 1200K-protein is a connectin-like elastic protein and includes specific PEVK-like fragment. We suggest that this 1200K-protein plays a major role in maintaining the structure of oblique muscle in invertebrates.

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Identification of High Molecular Weight Proteins in Squid Muscle by Western Blotting Analysis and Postmortem Rheological Changes

Cited by 7 publications

References 29 publications

Characterization of the Jumbo Squid (Dosidicus gigas) Skin By-Product by Shotgun Proteomics and Protein-Based Bioinformatics

Characterization of the Jumbo Squid (Dosidicus gigas) Skin By-Product by Shotgun Proteomics and Protein-Based Bioinformatics

Degradation of structural proteins and their relationship with the quality of Mandarin fish (Siniperca chuatsi) during post‐mortem storage and cooking

Partial sequence of connectin-like 1200K-protein in obliquely striated muscle of a polychaete (Annelida): Evidence for structural diversity from vertebrate and invertebrate connectins

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