Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes.

Tranter, M P; Sugrue, Stephen P.; Schwartz, Michael A.

doi:10.1083/jcb.109.6.2833

Cited by 14 publications

(21 citation statements)

References 36 publications

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“…It was postulated by these investigators that such direct interactions between actin and cell membranes occur in vivo. Similar observations have also been made by several other groups (Gert de Couet et al, 1984;Tranter et al, 1989;Gillard et al, 1992). Therefore, in light of the above data, it is conceivable that actin is also present on many cell surfaces despite the absence of an actin signal peptide or a transmembrane domain.…”

Section: Discussionsupporting

confidence: 90%

ENDOTHELIAL CELL SURFACE ACTIN SERVES AS A BINDING SITE FOR PLASMINOGEN, TISSUE PLASMINOGEN ACTIVATOR AND LIPOPROTEIN(a)

Dudani

Ganz

1996

Br J Haematol

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One of the mechanisms by which endothelial cells (ECs) regulate fibrinolysis is through the regulated assembly of proteins such as plasminogen, tissue plasminogen activator (tPA) and urokinase (uPA) on their membrane surface. Receptors for many of these fibrinolytic factors have been isolated and characterized. A unique 45 kD plasminogen receptor present on ECs derived from vein vasculature has been identified and resolved into two plasminogen binding components. One component consists of the unique 45 kD plasminogen receptor (pI = 6.3) whereas the other component (pI = 5.1) is identified as the cytoskeletal protein, actin. Immunofluorescent studies of isolated ECs confirm the presence of actin on their extracellular surface. This observation is consistent with a number of other recent reports of actin externally localized on other cell types. In vitro studies using purified actin confirm that plasminogen binds to actin both saturably and with relatively high affinity. Competition studies with lysine indicated that the binding was largely kringle-dependent, and when binding of tPA to actin was assessed, it also bound to actin with 70-80% of binding inhibited by lysine. Lipoprotein (a), which shows homology with plasminogen, also interacted with actin. Addition of plasminogen and low-density lipoproteins inhibited Lp(a) binding to actin in a dose-dependent fashion. Moreover, in competition with tPA, partial inhibition of plasminogen binding to actin was also observed. In experiments using anti-actin antibodies added in excess to cultured ECs, binding of plasminogen was inhibited by 45%, tPA binding was inhibited by 46% and Lp(a) binding was reduced by 56%, confirming actin as a binding site for these various ligands whilst attesting to the presence of other EC receptors for these proteins. Collectively, the data presented are consistent with actin playing a major role in localizing binding not only of plasminogen, but also of tissue plasminogen activator and Lp(a) to the surface of human endothelial cells.

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Section: Discussionsupporting

confidence: 90%

ENDOTHELIAL CELL SURFACE ACTIN SERVES AS A BINDING SITE FOR PLASMINOGEN, TISSUE PLASMINOGEN ACTIVATOR AND LIPOPROTEIN(a)

Dudani

Ganz

1996

Br J Haematol

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“…We recently reported that direct interactions between actin and integral membrane proteins also occur in the mammalian liver (Tranter et al, 1989). Using the sedimentationbinding assay mentioned above, we found that t2~I-actin binds specifically and saturably to liver cell membranes and that integral membrane proteins appear to be responsible.…”

mentioning

confidence: 85%

“…While electron micrographs show occasional filamentous structures attached to unstfipped liver cell membranes (Tranter et al, 1989), these filaments do not appear to be present in sufficient abundance to account for the level of endogenous membrane-bound actin (,o5 % of the total membrane protein). In addition, endogenous actin is very resistant to extraction by a variety of agents known to depolymerize actin filaments (Tranter et al, 1989;Hubbard and Ma, 1983). Interestingly, Hubbard and Ma (1983) have reported that actin bound to liver cell membranes does not bind myosin S-1.…”

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confidence: 91%

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Binding of actin to liver cell membranes: the state of membrane-bound actin.

Tranter

Sugrue

Schwartz

1991

The Journal of Cell Biology

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“…In addition to being a major protein of the contractile apparatus in muscle cells, actin is an important constituent of a diverse range of cellular processes including maintenance of the cytoskeleton, cytokinesis, and whole cell motility [Schwartz and Stone, 19831. Recent studies have indicated that actin may also play a role in gene transcription 0 1993 Wiley-Liss, Inc. and chromosome morphology [Ankenbauer et al, 19891, selective mRNA translation [Cheng and Bjerknes, 1989;Sundell and Singer, 19901, cellular localization and modulation of certain enzymes [Morita et al, 1989;Hunt et al, 1990;Farwell et al, 19901, and cytoskeletal interactions with the cell membrane [Tranter et al, 1989;St-Onge and Gicquaud, 19901. The classic studies of Vandekerckhove and coworkers [ Vandekerckhove and Weber, 1978,;1979a;1979b;Gabbiani et al, 19811 first established the presence of multiple distinct actin isotypes in vertebrates.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and expression of the chicken smooth muscle γ‐actin mRNA

Kovacs

Zimmer

1993

Cell Motil. Cytoskeleton

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We have investigated the expression of chicken smooth muscle gamma-actin mRNA by isolation and characterization of cDNAs representing this actin isoform and utilizing the cDNA to probe RNA from adult and developing cells. Nucleotide sequence elucidated from an apparent full length smooth muscle gamma-actin cDNA revealed that it contained 94 bp of 5' non-translated sequence, an open reading frame of 1131 bp, and 97 bp of 3' non-translated sequence. Within the 376 amino acid sequence deduced from the chicken cDNA were diagnostic amino acids at the NH2- and COOH-terminal regions which provided unequivocal identification of the gamma-enteric smooth muscle actin isoform. In addition, the chicken gamma-enteric actin deduced from our cDNA clones was found to differ from the sequence reported in earlier protein studies [J. Vandekerckhove and K. Weber, FEBS Lett. 102:219, 1979] by containing a proline rather than a glutamine at position 359 of the protein, indicating that the avian gamma-enteric actin isoform is identical to its mammalian counterpart. Comparison of the 5' and 3' non-translated sequence determined from the chicken cDNA to that elucidated for rat, mouse, and human showed that there is not a high degree of cross-species sequence conservation outside of the coding regions among these mRNAs. Northern hybridization analyses demonstrated that the gamma-enteric actin mRNA is expressed in adult aorta and oviduct tissues but not in adult skeletal muscle, cardiac muscle, liver, brain, and spleen tissues. The gamma-enteric actin mRNA was first observed in measurable quantities in gizzard tissue from 4-5 day embryos and increased in content in developing smooth muscle cells through 16-17 embryonic days. Following this initial increase during embryonic development, the gamma-enteric actin mRNA exhibits a decline in content until approximately 7 days posthatching, after which there is an increase in content to maximal levels found in adult gizzard tissue. In general, the developmental appearance of the gamma-enteric mRNA parallels that observed for this protein in previous studies indicating that the developmental expression of smooth muscle gamma-actin is regulated, in part, by an increased content of mRNA in chicken visceral smooth muscle cells during myogenesis.

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Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes.

Cited by 14 publications

References 36 publications

ENDOTHELIAL CELL SURFACE ACTIN SERVES AS A BINDING SITE FOR PLASMINOGEN, TISSUE PLASMINOGEN ACTIVATOR AND LIPOPROTEIN(a)

ENDOTHELIAL CELL SURFACE ACTIN SERVES AS A BINDING SITE FOR PLASMINOGEN, TISSUE PLASMINOGEN ACTIVATOR AND LIPOPROTEIN(a)

Binding of actin to liver cell membranes: the state of membrane-bound actin.

Molecular cloning and expression of the chicken smooth muscle γ‐actin mRNA

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