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PubMed1993

Immunoblotting of contractile and cytoskeletal proteins of canine basilar artery in vasospasm.

Vasospasm was produced in the canine basilar arteries by a two-hemorrhage method, and voltage- and receptor-dependent contractions of the normal canine basilar arteries were induced by local applications of potassium chloride (KCI) and serotonin, respectively, after transclival exposure. Actin, myosin, desmin, filamin, talin, vinculin, and alpha-actinin in the basilar artery were studied by immunoblotting. The immunoblots showed a decrease or loss in immunoreactivity of some native proteins and generation of protein fragments, smaller in size than native proteins, in spastic, KCI, and serotonin groups, indicating a proteolytic degradation. In the spastic group on Day 2, actin, desmin, and filamin were usually degraded slightly; myosin moderately; and talin and alpha-actinin substantially. Vinculin and metavinculin remained intact. In the spastic group on Day 7, actin and desmin were usually decomposed slightly; myosin, filamin, and vinculin substantially; and talin, metavinculin, and alpha-actinin markedly. In the KCI and serotonin groups, slight degradation was usually observed in filamin, often in alpha-actinin, and occasionally in actin, whereas desmin, vinculin, and metavinculin were not degraded. In addition, myosin was usually degraded moderately in the KCI group and slightly in the serotonin group, and talin was generally decomposed slightly in the KCI group and moderately in the serotonin group. The degraded fragments, although variable in number and immunoreactivity, were similar in size in the three groups. We suggest that the intracellular devices responsible for contraction of the basilar arteries are degraded more severely in the spastic group than in the KCI or serotonin group, probably by similar proteolytic mechanism and progressively with the passage of time after subarachnoid hemorrhage in vasospasm.

Animals↗
PubMed1983

Redistribution of microfilament-associated proteins during the formation of focal contacts and adhesions in chick fibroblasts.

The roles of the microfilament-associated proteins vinculin, alpha-actinin, myosin and filamin have been studied by immunofluorescence and double fluorescence in conjunction with interference reflection microscopy (IRM), during the development of focal contacts and focal adhesions in a chick fibroblast system which initially has no such adhesion specializations but then develops them sequentially over a 48 h period. Without exception, all focal contacts and focal adhesions contain both vinculin and alpha-actinin at every stage that we can detect by IRM or by double staining to reveal the associated microfilament bundles. Indeed the appearance of small bodies containing alpha-actinin and vinculin is shown to precede focal contact formation in our model system and such structures (not visible by IRM) are proposed to be the precursors of focal contacts and adhesions. Myosin and filamin are distributed generally with some reticular patterning in the early motile cells which lack the focal specializations, but as focal contacts and adhesions form these proteins become progressively recruited into the associated microfilament bundles. Only then do we see the marked depletion that has been reported earlier of diffusely distributed myosin and filamin in the leading lamella. Although this is not initially associated with any change in the motile status of the cells, the recruitment of these microfilament-associated proteins into stress fibres is proposed to occur in preparation for anchorage and bracing of cells to the substratum when they later become stationary.

Actinin↗
PubMed1994

Correlation between inhibition of cytoskeleton proteolysis and anti-vesiculation effect of calpeptin during A23187-induced activation of human platelets: are vesicles shed by filopod fragmentation?

Platelets were incubated in the presence of calpeptin to inhibit calpain-mediated cytoskeleton proteolysis during further activation by Ca2+ ionophore A23187. The appearance of filamin and myosin subfragments (93 kDa and 135 kDa, respectively) was inhibited by low calpeptin doses (1 microgram/ml). Higher doses (10-20 micrograms/ml) were required to completely inhibit talin and filamin degradation. Vesiculation strongly depended on cytoskeleton proteolysis and was reduced by 60% when platelets were preincubated with 10 micrograms/ml calpeptin. Activated platelets bore longer and more filopods when pretreated with calpeptin. Filopods were straight and regular when high calpeptin doses were used, whereas they were shorter and broader with bloated surfaces when calpeptin was omitted. Some bloated areas were also found in straight filopods. These results suggest that the cytoskeleton proteolysis, and more specifically filamin proteolysis, induced bloating of filopod surfaces, thus facilitating fragmentation of filopod into vesicles.

Blood Platelets↗
PubMed2005

The ABP-120 C-end region from Entamoeba histolytica interacts with sulfatide, a new lipid target.

EhABP-120 is the first filamin identified in the parasitic protozoan Entamoeba histolytica. Filamins are a family of cross-linking actin-binding proteins that promote a dynamic orthogonal web. They have been reported to interact directly with more than 30 cellular proteins and some phosphoinositides. The biochemical consequences of these interactions may have either positive or negative effects on the cross-linking function and also form a link between the cytoskeleton and plasma membrane. In this study, the EhABP-120 carboxy-terminal domain (END) was biochemically characterized. This domain was able to associate to 3-sulfate galactosyl ceramide, a new lipid target for a member of the filamin family. Also, the END domain was able to dimerize "in vitro." Molecular modeling analysis showed that the dimeric region is stabilized by a disulfide bond. Electrostatic and docking studies suggest that an electropositive concave pocket at the dimeric END domain interacts simultaneously with several sulfogalactose moieties of the sulfatide.

Amino Acid Sequence↗
PubMed1982

Cultured megakaryocytes: changes in the cytoskeleton after ADP-induced spreading.

Megakaryocytes from guinea pig bone marrow were isolated and maintained in liquid culture and were treated with ADP, thrombin, arachidonic acid, or collagen. Megakaryocytes spread with an active ruffled membrane in response to ADP (1-100 microM), thrombin (1.0 U/ml), and arachidonic acid (50 microM) but responded to collagen surfaces only if fibronectin was added to the cultures. Spreading could be blocked completely by dibutyryl cyclic AMP (dibutyryl cAMP) or isobutylmethylxanthine at 1 mM, as well as by cytochalasin D (2 microgram/ml), but not by colchicine up to 1 mg/ml. The distribution of contractile proteins was examined by immunofluorescence. In untreated, spherical cells, staining with antimyosin, antifilamin, anti-alpha-actinin, or with fluorescein-labeled subfragment 1 (FITC-S1) was diffuse and unpatterned. With antitubulin antibody, however, microtubules were seen in a dense array throughout the unspread cells. In actively ruffling spreading cells, myosin, filamin, and actin were visualized in the region of the ruffled membrane while alpha-actinin was seen most prominently in a band located proximal to the inner part of the ruffle. In fully spread cells, actin, myosin, filamin, and alpha-actinin were seen in filaments that filled the cytoplasm. Antimyosin and anti-alpha-actinin staining of the filaments was periodic with approximately 1 micrometer center-to-center spacing. Actin, filamin, and alpha-actinin were also identified in punctate spots throughout the spread cytoplasm. Microtubules were absent from the ruffle but filled the cytoplasm of fully spread cells. Rings, 1.5-2.5 micrometer in diameter, were seen with antitubulin in 13% of the spread cells. Our results show that megakaryocytes respond to platelet agonists, but typically by spreading, rather than extending, filopodia. From the changes in localization of contractile proteins and from time-lapse cinematography, we propose a model for cell spreading.

Actinin↗
PubMed1993

Localization of two myosin-subfragment-1 binding contacts in the 96-132 region of actin subdomain-1.

Many direct observations and indirect experimental approaches have pin-pointed two segments (sequences 1-28 and 360-372) in actin subdomain-1 which bind to myosin subfragment-1. In a previous investigation [Labbé, J. P., Méjean, C., Benyamin, Y. & Roustan, C. (1990) Biochem. J. 271, 407-413], we have observed competition between myosin subfragment-1 and anti-actin antibodies specific to epitopes including Thr103. A multisite interface model has also been proposed to take into account myosin-head binding to the N-terminal and C-terminal regions and to more central 40-113 sequence of actin. In the present study, two limited actin segments encompassing residues 96-103 and 112-125 were identified as myosin-head-binding sites. Myosin subfragment-1 competed for monomeric actin with the antibodies directed against sequences 96-105 and 114-120 and its binding to the tryptic 96-113 and synthetic 112-125 actin peptides was prevented by magnesium pyrophosphate but not by calcium pyrophosphate. In the presence of ATP-Mg2+, myosin subfragment-1 was dissociated by filamin from its complex with monomeric actin or with peptide 105-120. Contact points of filamin on actin were previously located in the 105-120 and 360-372 actin sequences [Méjean, C., Lebart, M. C., Boyer, M., Roustan, C. & Benyamin, Y. (1992) Eur. J. Biochem. 209, 555-562]. The in vitro inhibitory effect of filamin on actin-activated Mg2+-ATPase would thus be explained by this competition. Furthermore, the (27-kDa-50-kDa-20-kDa) trypsin-split myosin subfragment-1 which could no longer be activated by actin, did not bind at all to the two sites located in the 96-125 region, but it still interacted with the 360-372 segment. Our results regarding the position of the myosin head on actin monomers in rigor conditions provide evidence on the presence of two topologically independent contact points in the myosin-head/actin interface. One group exposed residues in the 1-7, 21-29, 77-95 and 96-103 actin segment, another, on the opposite side of subdomain-1, included residues from 112-125 and 360-372 sequences.

Actins↗
PubMed1999

Actin filament organization is required for proper cAMP-dependent activation of CFTR.

Previous studies have indicated a role of the actin cytoskeleton in the regulation of the cystic fibrosis transmembrane conductance regulator (CFTR) ion channel. However, the exact molecular nature of this regulation is still largely unknown. In this report human epithelial CFTR was expressed in human melanoma cells genetically devoid of the filamin homologue actin-cross-linking protein ABP-280 [ABP(-)]. cAMP stimulation of ABP(-) cells or cells genetically rescued with ABP-280 cDNA [ABP(+)] was without effect on whole cell Cl(-) currents. In ABP(-) cells expressing CFTR, cAMP was also without effect on Cl(-) conductance. In contrast, cAMP induced a 10-fold increase in the diphenylamine-2-carboxylate (DPC)-sensitive whole cell Cl(-) currents of ABP(+)/CFTR(+) cells. Further, in cells expressing both CFTR and a truncated form of ABP-280 unable to cross-link actin filaments, cAMP was also without effect on CFTR activation. Dialysis of ABP-280 or filamin through the patch pipette, however, resulted in a DPC-inhibitable increase in the whole cell currents of ABP(-)/CFTR(+) cells. At the single-channel level, protein kinase A plus ATP activated single Cl(-) channels only in excised patches from ABP(+)/CFTR(+) cells. Furthermore, filamin alone also induced Cl(-) channel activity in excised patches of ABP(-)/CFTR(+) cells. The present data indicate that an organized actin cytoskeleton is required for cAMP-dependent activation of CFTR.

Actins↗
PubMed2006

HIV infection changes glomerular podocyte cytoskeletal composition and results in distinct cellular mechanical properties.

In addition to forming the selective filtration barrier for the renal glomerulus, podocytes maintain glomerular capillary architecture by opposing distending hemodynamic forces. To understand the relationship of cytoskeletal properties and the mechanical characteristics of podocytes, we studied filamin expression and distribution and measured cell membrane deformability in conditionally immortalized wild-type (WT) mouse podocytes, and in podocytes derived from a mouse model of HIV-associated nephropathy (HIVAN). In the WT cells, filamin and F-actin were localized at the periphery and in prominent stress fibers. In the HIVAN cells, filamin expression was reduced, and stress fibers were sparse. In a microaspiration assay, HIVAN cells ruptured under minimal negative pressure. Atomic force microscopy demonstrated that the WT cells had a stiffness of 17 kPa, whereas the value for the HIVAN cells was 4 kPa. These results demonstrate that the mechanical properties of WT and HIVAN podocytes are markedly different in a manner that is consistent with differences in the composition and arrangement of their cytoskeletons. The mechanical properties of the WT podocytes suggest that these cells can better maintain capillary integrity than the HIVAN podocytes and implicate pathological assembly of the cytoskeleton as a mechanism of HIVAN.

Actinin↗
PubMed2004

Yeast two-hybrid screening for proteins that interact with alpha1-adrenergic receptors.

AIM: To find novel proteins that may bind to alpha1A-adrenergic receptor (alpha1A-AR) and investigate their interactions with the other two alpha1-AR subtypes (alpha1B-AR and alpha1D-AR) with an expectation to provide new leads for the function study of the receptors. METHODS: Yeast two-hybrid assay was performed to screen a human brain cDNA library using the C terminus of alpha1A-AR (alpha1A-AR-CT) as bait. X-Gal assay and o-nitrophenyl-beta-D-galactopyranoside (ONPG) assay were subsequently conducted to further qualitatively or quantitatively confirm the interactions between receptors and the three identified proteins. RESULTS: (1) Selection medium screening identified segments of bone morphogenetic protein-1 (BMP-1), active Bcr-related protein (Abr), and filamin-C as binding partners of alpha1A-AR-CT in yeast cells respectively. Besides, protein segments of BMP-1 and Abr could only specifically interact with alpha1A-AR-CT while filamin-C segment interacted with all three alpha1-AR subtypes. (2) In X-Gal assay, the co-transformants of alpha1A-AR-CT and BMP-1 segments turned strong blue at about 30 min while other positive transformants only developed weak blue at about 5-6 h. (3) In ONPG assay, interaction (shown in beta-galactosidase activity) between alpha1A-AR-CT and BMP-1 segments was about 30 times stronger than that of control (P<0.01), while other positive interactions were only about 2-5 times as strong as those of controls (P<0.05). CONCLUSION: In yeast cells BMP-1, Abr and/or filamin-C could interact with three alpha1-AR subtypes, among which, interaction between BMP-1 and alpha1A-AR was the strongest while other interactions between proteins and receptors were relatively weak.

Bone Morphogenetic Protein 1↗
PubMed1987

Phosphorylation of actin-binding proteins by casein kinases 1 and 2.

Filamin and vinculin from chicken gizzards were significantly phosphorylated in vitro by casein kinases 1 and 2, but not by alpha-actinin. Antisera raised against these actin-binding proteins immunoprecipitated the phosphorylated proteins corresponding to filamin and vinculin, but no phosphoprotein corresponding to alpha-actinin was detected. These results suggest that filamin and vinculin are phosphorylated in vivo but alpha-actinin is not.

Actinin↗
PubMed1987

Structural and biochemical analysis of skinned smooth muscle preparations.

This paper describes a biochemical and immunocytochemical analysis of smooth muscle strips that were chemically skinned and subjected to contraction and relaxation cycles according to procedures commonly employed in current skinned smooth muscle work. The fate of four major proteins, myosin, filamin, caldesmon and actin, was followed with respect to the proportionate loss of these proteins to the bathing medium as well as to their structural redistribution within the cells in the muscle strips. Large losses (of the order of 50%) of both myosin and filamin occurred at the skinning step, using either Triton X-100 or Saponin as the detergent; losses of actin were up to 30% with Triton X-100 and around 15% with Saponin. Losses of caldesmon were difficult to assess due to the rapid degradation of this protein in the bathing medium. Subsequent cycles of contraction and relaxation resulted in accumulated loss, notably of myosin and filamin, so that after the third contraction as little as 20% and 40% respectively of the original complement of these proteins remained in the muscle strips. These changes in protein composition were accompanied by a drastic redistribution of the proteins in the muscle cells. Most marked were the changes seen with myosin, significant amounts of this protein being already found in the connective tissue space after the first relaxation. These findings point to the need for a careful reappraisal of the conditions currently used in skinned smooth muscle research.

Animals↗
PubMed2006

Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity.

We report that caveolin-1, one of the major structural protein of caveolae, interacts with TCP-1, a hetero-oligomeric chaperone complex present in all eukaryotic cells that contributes mainly to the folding of actin and tubulin. The caveolin-TCP-1 interaction entails the first 32 amino acids of the N-terminal segment of caveolin. Our data show that caveolin-1 expression is needed for the induction of TCP-1 actin folding function in response to insulin stimulation. Caveolin-1 phosphorylation at tyrosine residue 14 induces the dissociation of caveolin-1 from TCP-1 and activates actin folding. We show that the mechanism by which caveolin-1 modulates TCP-1 activity is indirect and involves the cytoskeleton linker filamin. Filamin is known to bind caveolin-1 and to function as a negative regulator of insulin-mediated signaling. Our data support the notion that the caveolin-filamin interaction contributes to restore insulin-mediated phosphorylation of caveolin, thus allowing the release of active TCP-1.

Amino Acid Sequence↗
PubMed1997

Localization of smoothelin in avian smooth muscle and identification of a vascular-specific isoform.

Smoothelin is a smooth muscle-specific protein of minor abundance first identified via a monoclonal antibody obtained using an avian gizzard extract as antigen. Dual labelling of ultrathin sections with antibodies to smoothelin together with antibodies to other smooth muscle proteins showed that smoothelin was co-distributed with filamin and desmin in the cytoskeleton domain of the smooth muscle cell. From the finding that smoothelin, unlike desmin, was readily extracted by Triton X-100 as well as under conditions that solubilized myosin, beta-actin and filamin, we conclude that smoothelin is most likely associated with the actin cytoskeleton. Western blot analysis of gizzard smooth muscle tissue revealed an immunoreactive protein band with an apparent molecular weight of 59 kDa that separated into 3-4 isolated variants, while avian vascular muscle showed a polypeptide band of 95 kDa. These results point to the presence of specific isoforms in visceral and vascular smooth muscles. The 59 kDa isoform was shown to be distinct from the 60 kDa filamin-binding protein, described by Maekawa and Sakai (FEBS Lett. 221, 68-72, 1987). As compared to other smooth muscle markers, such as calponin and SM22, smoothelin appeared very late during differentiation in the chick gizzard, on about the 18th embryonic day.

Animals↗
PubMed1983

Purification of a HeLa cell high molecular weight action binding protein and its identification in HeLa cell plasma membrane ghosts and intact HeLa cells.

The high molecular weight protein (HMWP) which was previously observed to be a major component of the actin based gels formed by incubating cytoplasmic extracts of HeLa cells at 25 degrees C [Weihing, R. R. (1977) J. Cell Biol. 75, 95-103] has now been purified by gel filtration of 0.6 M KCl extracts of precipitated gels. A few hundred micrograms of HMWP, which is about 90% pure, can be isolated from 4 X 10(9) cells. HMWP can gel muscle actin and cross-link it into filament bundles. Its subunit molecular weight is 250 0000, its Stokes radius is 125 A, and its sedimentation coefficient is 9 S. A native molecular weight of 480 000 was calculated by using the latter two parameters, and therefore the native molecule is a dimer. Its amino acid analysis is nearly indistinguishable from that of macrophage actin binding protein and of mammalian and avian filamins. All of these findings indicate that HMWP is homologous to the latter proteins. However, HeLa cell HMWP and avian filamin must differ in their primary sequences because their partial peptide maps are distinct and because an antiserum against HMWP reacts only weakly with filamin. For studies on the intracellular location of HMWP, a goat antiserum against purified HMWP was prepared and characterized and then used to localize HMWP in suspension grown cells. The technique of immunoblotting revealed that the antiserum reacted virtually exclusively with the high molecular weight polypeptide that comigrates with HMWP in cell lysates and in ZnCl2-stabilized plasma membrane ghosts prepared from HeLa cells [Gruenstein, E., Rich, A., & Weihing, R. R. (1975) J. Cell Biol. 64, 223-234] and that it did not react with rabbit myosin heavy chain, microtubule proteins (MAPS and tubulin) from HeLa cells and calf brain, or the proteins of human erythrocyte ghosts including spectrin. Suspension-grown cells which were stained with the antiserum by the technique of indirect immunofluorescence showed bright fluorescence at the rim of the cells and less intense generalized fluorescence. If preimmune serum or immune serum treated with HMWP was substituted for the immune serum, then staining at the rim was not observed, but the generalized fluorescence was only slightly reduced; unpermeabilized cells were not stained. These results indicate that HMWP is a component of the cortical cytoplasm of HeLa cells. Possible functions of cortical HMWP are discussed briefly.

Actins↗
PubMed1990

The cytoskeletal and contractile apparatus of smooth muscle: contraction bands and segmentation of the contractile elements.

Confocal laser scanning microscopy of isolated and antibody-labeled avian gizzard smooth muscle cells has revealed the global organization of the contractile and cytoskeletal elements. The cytoskeleton, marked by antibodies to desmin and filamin is composed of a mainly longitudinal, meandering and branched system of fibrils that contrasts with the plait-like, interdigitating arrangement of linear fibrils of the contractile apparatus, labeled with antibodies to myosin and tropomyosin. Although desmin and filamin were colocalized in the body of the cell, filamin antibodies labeled additionally the vinculin-containing surface plaques. In confocal optical sections the contractile fibrils showed a continuous label for myosin for at least 5 microns along their length: there was no obvious or regular interruption of label as might be expected for registered myosin filaments. The cytoplasmic dense bodies, labeled with antibodies to alpha-actinin exhibited a regular, diagonal arrangement in both extended cells and in cells shortened in solution to one-fifth of their extended length: after the same shortening, the fibrils of the cytoskeleton that showed colocalization with the dense bodies in extended cells became crumpled and disordered. It is concluded that the dense bodies serve as coupling elements between the cytoskeletal and contractile systems. After extraction with Triton X-100, isolated cells bound so firmly to a glass substrate that they were unable to shorten as a whole when exposed to exogenous Mg ATP. Instead, they contracted internally, producing integral of 10 regularly spaced contraction nodes along their length. On the basis of differences of actin distribution two types of nodes could be distinguished: actin-positive nodes, in which actin straddled the node, and actin-negative nodes, characterized by an actin-free center flanked by actin fringes of 4.5 microns minimum length on either side. Myosin was concentrated in the center of the node in both cases. The differences in node morphology could be correlated with different degrees of coupling of the contractile with the cytoskeletal elements, effected by a preparation-dependent variability of proteolysis of the cells. The nodes were shown to be closely related to the supercontracted cell fragments shown in the accompanying paper (Small et al., 1990) and furnished further evidence for long actin filaments in smooth muscle. Further, the segmentation of the contractile elements pointed to a hierarchial organization of the myofilaments governed by as yet undetected elements.

Actinin↗
PubMed1987

A 250K-molecular-weight actin-binding protein from actin-based gels formed in sea urchin egg cytoplasmic extract.

The actin-based gel formed at 35 degrees C in the cytoplasmic extract from eggs of a sea urchin, Tripneustes gratilla, contains several high-molecular-weight proteins. Among them, the 250K-molecular-weight protein was isolated and characterized. This protein migrated slightly more slowly than filamin from chicken gizzard upon polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. It reacted only very weakly with antibodies against chicken gizzard filamin or against a high-molecular-weight actin-binding protein from Physarum plasmodia. It did not react with antibodies against chicken erythrocyte alpha-spectrin nor against the 220K protein from the same egg. A chemical crosslinking experiment revealed the presence of dimers in the purified 250K protein preparation. A rotary shadowed specimen of such a preparation showed wavy single-stranded molecules 120-170 nm long, having five to six globular domains, which may represent dimers. The appearance was different from that of spectrin or actin-binding protein from macrophage or chicken gizzard filamin. This protein increased the viscosity of F-actin solution. It bound to F-actin preferably at low KCl concentrations such as 20 mM. The binding ability was not influenced by pH between 6.0 and 7.5, although it was somewhat reduced above pH 8.0. The binding was insensitive to low Ca ion concentrations. Electron microscopy using the negative staining technique supported the idea that this protein crosslinks actin filaments. In addition, a second protein from egg gels, with a reported molecular weight of about 220K (Kane, R.E., J. Cell Biol. 66, 305-315 (1975)), comigrated with human erythrocyte alpha-spectrin on an SDS-gel and reacted with antibodies against chicken erythrocyte alpha-spectrin. This suggests that this protein is a sea urchin egg spectrin. The role of these proteins in the cytoskeleton formation in the sea urchin egg is discussed.

Animals↗
PubMed1987

Structural analysis of the cytoskeleton of Tritrichomonas foetus.

The cytoskeleton of Tritrichomonas foetus was studied by immunofluorescence microscopy, using anti-actin, anti-filamin, anti-myosin and anti-tubulin monospecific antibodies, and by high voltage electron microscopy of Triton X-100 extracted cells. Actin, filamin and myosin were distributed throughout the cytoplasm of T. foetus. Filamin, however, is more concentrated at the cell periphery. The peltar-axostylar system could be seen in interphasic and dividing cells using anti-tubulin antibodies. High voltage electron micrographs showed the spatial distribution of the microtubules and their association with the hydrogenosomes, and the association of the costa with the recurrent flagellum.

Animals↗
PubMed1979

Identification of a high molecular weight actin-binding protein in skeletal muscle.

A large polypeptide having a molecular weight of 240,000 as determined by electrophoresis in the presence of sodium dodecyl sulfate has been identified in whole cell homogenates from chick skeletal muscle myoblasts and the rat myoblast L6 cell line. A similar polypeptide was identified in both thigh and breast chicken skeletal muscle, but the latter contained less of this protein per g of tissue. Antibodies made to gizzard filamin (an actin-binding protein having a molecular weight of 240,000) cross-reacted with the partially purified Mr = 240,000 protein from chicken skeletal muscle. With use of the indirect immunofluorescence technique, the filamin antibody localized in the Z-line region of chicken skeletal muscle myofibrils. These results indicate that skeletal muscle contains a filamin-like protein that may form an integral part of the myofibril structure.

Actins↗