Nebulin and titin expression in Duchenne muscular dystrophy appears normal

Fürst, Dieter O.; Nave, R.; Osborn, Mary; Weber, Klaus; Bardosi, A.; Archidiacono, Nicoletta; Ferro, Mariangela; Romano, Valentino; Romeo, Giovanni

doi:10.1016/0014-5793(87)80420-9

Cited by 21 publications

(7 citation statements)

References 10 publications

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“…By analogy with titin in vertebrate striated muscle (Trinick et al, 1984;Furst et al, 1988) individual molecules of p800 in flight muscle may extend from Z-disc to A-band, stretching as C-filaments lengthen. The use of monoclonal antibodies allows us to localize epitopes on the proteins but Ni if the epitopes are repeated.…”

Section: Discussionmentioning

confidence: 99%

“…If there is one epitope per molecule, the broad area of A-band labelled would suggest that the molecules are not in lateral register across the A-band. Titin ( 3000 kd) is 1-1.3 Am long (Furst et al, 1988), therefore molecules of p800 with the configuration of isolated titin could span the distance occupied by connecting protein in Lethocerus flight muscle. In vertebrate striated muscle the longer titin molecule spans the I-band and nearly half the A-band (Trinick et al, 1984;Furst et al, 1988) and may have more than one function.…”

Section: Tit I I D S T S S F Ts Lv L D N Vmentioning

confidence: 99%

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Identification and localization of high molecular weight proteins in insect flight and leg muscle.

Lakey¹,

Ferguson²,

Labeit³

et al. 1990

The EMBO Journal

114

112

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Thick and thin filaments in asynchronous flight muscle overlap nearly completely and thick filaments are attached to the Z‐disc by connecting filaments. We have raised antibodies against a fraction of Lethocerus flight muscle myofibrils containing Z‐discs and associated filaments and also against a low ionic strength extract of myofibrils. Monoclonal antibodies were obtained to proteins of 800 kd (p800), 700 kd (p700), 400 kd (p400) and alpha‐actinin. The positions of the proteins in Lethocerus flight and leg myofibrils were determined by immunofluorescence and electron microscopy. p800 is in connecting filaments of flight myofibrils and in A‐bands of leg myofibrils. p700 is in Z‐discs of flight myofibrils and an immunologically related protein, p500, is in leg muscle Z‐discs. p400 is in M‐lines of both flight and leg myofibrils. Preliminary DNA sequencing shows that p800 is related to vertebrate titin and nematode twitchin. Molecules of p800 could extend from the Z‐disc a short way along thick filaments, forming a mechanical link between the two structures. All three high molecular weight proteins probably stabilize the structure of the myofibril.

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Section: Discussionmentioning

confidence: 99%

Section: Tit I I D S T S S F Ts Lv L D N Vmentioning

confidence: 99%

Identification and localization of high molecular weight proteins in insect flight and leg muscle.

Lakey¹,

Ferguson²,

Labeit³

et al. 1990

The EMBO Journal

114

112

View full text Add to dashboard Cite

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“…Myofibrillogenesis involves the ordered assembly of hundreds of protein subunits in a temporally and spatially defined manner. Titin [1], described also as connectin [2], acts as a molecular ruler for the assembly of the sarcomere by providing spatially defined binding sites for other sarcomeric proteins [3]over the distance of an entire half‐sarcomere [4]. Titin is expressed as one of the earliest sarcomeric proteins and is localised to primordial sites of sarcomeric assembly on stress‐fibre‐like structures together with α‐actinin [5].…”

Section: Introductionmentioning

confidence: 99%

Two immunoglobulin‐like domains of the Z‐disc portion of titin interact in a conformation‐dependent way with telethonin

et al. 1998

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The giant muscle protein titin/connectin plays a crucial role in myofibrillogenesis as a molecular ruler for sarcomeric protein sorting. We describe here that the N-terminal titin immunoglobulin domains Z1 and Z2 interact specifically with telethonin in yeast two-hybrid analysis and protein binding assays. Immunofluorescence with antibodies against the Nterminal region of titin and telethonin detects both proteins at the Z-disc of human myotubes. Longer titin fragments, comprising a serine-proline-rich phosphorylation site and the next domain, do not interact. The interaction of telethonin with titin is therefore conformation-dependent, reflecting a possible phosphorylation regulation during myofibrillogenesis.z 1998 Federation of European Biochemical Societies.

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“…1B) while by immunofluorescence it gave a single stripe signal around the N1‐line (data not shown). Moreover, this titin 150‐kDa fragment was found to react with the T12 anti‐titin monoclonal antibody, defined to label each half sarcomere approximately at 100 nm from the Z‐line [29].…”

Section: Resultsmentioning

confidence: 99%

Binding of a native titin fragment to actin is regulated by PIP2

et al. 1998

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Titin is a giant protein which extends from Z-line to M-line in striated muscles. We report here the purification of a 150-kDa titin fragment, obtained after V8 protease treatment of myofibrils. This polypeptide was located at the N1-line level, in a titin part known to exhibit stiff properties correlated to an association with actin. By solid or liquid phase binding assays and cosedimentation, we have clearly demonstrated a direct, saturable and relative high affinity binding of the native titin fragment to F-actin. The 150-kDa titin fragment was also shown to accelerate actin polymerization. Furthermore, the actin-titin interaction was found to be inhibited by phosphoinositides.z 1998 Federation of European Biochemical Societies.

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Nebulin and titin expression in Duchenne muscular dystrophy appears normal

Cited by 21 publications

References 10 publications

Identification and localization of high molecular weight proteins in insect flight and leg muscle.

Identification and localization of high molecular weight proteins in insect flight and leg muscle.

Two immunoglobulin‐like domains of the Z‐disc portion of titin interact in a conformation‐dependent way with telethonin

Binding of a native titin fragment to actin is regulated by PIP2

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