Structure and function of tuna tail tendons

Shadwick, Robert E.; Rapoport, H Scott; Fenger, Joelle M.

doi:10.1016/s1095-6433(02)00215-5

Cited by 34 publications

(24 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…By electrophoresis, a3 was found to migrate at the same position as a1. This revealed that cobia skin collagens contain exclusively a1a2a3 heterotrimers, which were in agreement with tilapia and tuna as well as many teleosts (Kimura, 1992;Kimura, Ohno, Miyauchi, & Uchida, 1987;Shadwick, Rapoport, & Fenger, 2002;Zeng et al, 2009). Generally, the type I collagen molecule extracted from mammals is composed of three polypeptide chains: two a1 chains and one a2 chain.…”

Section: Subunit Structure Of Asc and Pscsupporting

confidence: 74%

Structure and characteristics of acid and pepsin-solubilized collagens from the skin of cobia (Rachycentron canadum)

et al. 2012

View full text Add to dashboard Cite

Section: Subunit Structure Of Asc and Pscsupporting

confidence: 74%

Structure and characteristics of acid and pepsin-solubilized collagens from the skin of cobia (Rachycentron canadum)

et al. 2012

View full text Add to dashboard Cite

“…Interestingly, these tendons, which control the protrusion and retraction mechanism of the tongue, evolved before the advent of vertebrates or endochondral bone. Cartilaginous and bony fish also have linear tendons with similar mechanical properties to mammals, but with broadly different fascicle organization [29]. The type I collagen (GPP) n motif appears to lack significant levels of 3Hyp in the tissues of bony fish (Hudson and Eyre, unpublished observation).…”

Section: Discussionmentioning

confidence: 99%

Evolutionary Origins of C-Terminal (GPP)n 3-Hydroxyproline Formation in Vertebrate Tendon Collagen

et al. 2014

View full text Add to dashboard Cite

Approximately half the proline residues in fibrillar collagen are hydroxylated. The predominant form is 4-hydroxyproline, which helps fold and stabilize the triple helix. A minor form, 3-hydroxyproline, still has no clear function. Using peptide mass spectrometry, we recently revealed several previously unknown molecular sites of 3-hydroxyproline in fibrillar collagen chains. In fibril-forming A-clade collagen chains, four new partially occupied 3-hydroxyproline sites were found (A2, A3, A4 and (GPP)n) in addition to the fully occupied A1 site at Pro986. The C-terminal (GPP)n motif has five consecutive GPP triplets in α1(I), four in α2(I) and three in α1(II), all subject to 3-hydroxylation. The evolutionary origins of this substrate sequence were investigated by surveying the pattern of its 3-hydroxyproline occupancy from early chordates through amphibians, birds and mammals. Different tissue sources of type I collagen (tendon, bone and skin) and type II collagen (cartilage and notochord) were examined by mass spectrometry. The (GPP)n domain was found to be a major substrate for 3-hydroxylation only in vertebrate fibrillar collagens. In higher vertebrates (mouse, bovine and human), up to five 3-hydroxyproline residues per (GPP)n motif were found in α1(I) and four in α2(I), with an average of two residues per chain. In vertebrate type I collagen the modification exhibited clear tissue specificity, with 3-hydroxyproline prominent only in tendon. The occupancy also showed developmental changes in Achilles tendon, with increasing 3-hydroxyproline levels with age. The biological significance is unclear but the level of 3-hydroxylation at the (GPP)n site appears to have increased as tendons evolved and shows both tendon type and developmental variations within a species.

show abstract

“…The effect of the special situation in the tuna is demonstrated by in vivo muscle 'work loops' (Fig.·7). Tunas are the only fish with large discrete tendons that have been instrumented for direct muscle force measurements during swimming (Knower et al, 1993;Shadwick et al, 2002a). The close synchrony between muscle shortening in the mid-body and force development in the caudal tendons is evident; the resulting work loop is large and positive net work is produced, like the optimized work loops of isolated muscle fibres (Figs·8, 9).…”

Section: Implications For Thunniform Swimmingmentioning

confidence: 99%

Thunniform swimming: muscle dynamics and mechanical power production of aerobic fibres in yellowfin tuna (Thunnus albacares)

Shadwick

Syme

2008

Journal of Experimental Biology

View full text Add to dashboard Cite

SUMMARYWe studied the mechanical properties of deep red aerobic muscle of yellowfin tuna (Thunnus albacares), using both in vivo and in vitro methods. In fish swimming in a water tunnel at 1-3·L·s -1 (where L is fork length), muscle length changes were recorded by sonomicrometry, and activation timing was quantified by electromyography. In some fish a tendon buckle was also implanted on the caudal tendon to measure instantaneous muscle forces transmitted to the tail. Between measurement sites at 0.45 to 0.65·L, the wave of muscle shortening progressed along the body at a relatively high velocity of 1.7·L per tail beat period, and a significant phase shift (31±4°) occurred between muscle shortening and local midline curvature, both suggesting red muscle power is directed posteriorly, rather than causing local body bending, which is a hallmark of thunniform swimming. Muscle activation at 0.53·L was initiated at about 50° of the tail beat period and ceased at about 160°, where 90°is peak muscle length and 180° is minimum length. Strain amplitude in the deep red fibres at 0.5·L was ±5.4%, double that predicted from midline curvature analysis. Work and power production were measured in isolated bundles of red fibres from 0.5·L by the work loop technique. Power was maximal at 3-4·Hz and fell to less than 50% of maximum after 6·Hz. Based on the timing of activation, muscle strain, tail beat frequencies and forces in the caudal tendon while swimming, we conclude that yellowfin tuna, like skipjack, use their red muscles under conditions that produce near-maximal power output while swimming. Interestingly, the red muscles of yellowfin tuna are slower than those of skipjack, which corresponds with the slower tail beat frequencies and cruising speeds in yellowfin.

show abstract

Structure and function of tuna tail tendons

Cited by 34 publications

References 41 publications

Structure and characteristics of acid and pepsin-solubilized collagens from the skin of cobia (Rachycentron canadum)

Structure and characteristics of acid and pepsin-solubilized collagens from the skin of cobia (Rachycentron canadum)

Evolutionary Origins of C-Terminal (GPP)n 3-Hydroxyproline Formation in Vertebrate Tendon Collagen

Thunniform swimming: muscle dynamics and mechanical power production of aerobic fibres in yellowfin tuna (Thunnus albacares)

Contact Info

Product

Resources

About