Actin Expression
Published by Anonymous on 2007/9/28 (2725 reads)
1: J Pathol. 2004 Nov;204(4):386-95.
Pathological situations characterized by altered actin isoform expression.
Chaponnier C, Gabbiani G.
Department of Pathology and Immunology, CMU, University of Geneva, Geneva, Switzerland. Christine.Chaponnier@medecine.unige.ch
Modulation of actin isoform expression is a well-established feature of developmental phenomena. As one might expect, it is also characteristic of several pathological situations that are the subject of the present review. alpha-Smooth muscle actin has proven to be a reliable marker for identifying (a) vascular smooth muscle cells during vascular development and vascular diseases, and (b) myofibroblasts during wound healing, fibrocontractive diseases, and stromal reaction to epithelial tumours. The hallmark of a differentiated myofibroblast relies on the acquisition of an organized contractile apparatus characterized by alpha-smooth muscle actin-expressing stress fibres. More and more data suggest that alpha-smooth muscle actin plays a direct role in myofibroblast contractile activity through its N-terminal domain AcEEED. Newly developed antibodies against alpha-skeletal and alpha-cardiac actins have allowed the detection of subpopulations of alpha-skeletal positive cardiomyocytes in adult, hypertrophic, and failing heart. These antibodies have also permitted us to identify the differentiation degree of malignant cells in tumours such as rhabdomyosarcoma. Whether the differential expression of actin isoforms in human diseases is functionally relevant is not yet fully established, although studies on human actin mutations, actin null mice, and the N-terminal end of alpha-smooth muscle actin support this possibility. Copyright (c) 2004 Pathological Society of Great Britain and Ireland.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15495226 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: J Urol. 2004 Oct;172(4 Pt 2):1667-72.
Decreased expression of smooth muscle alpha-actin results in decreased contractile function of the mouse bladder.
Zimmerman RA, Tomasek JJ, McRae J, Haaksma CJ, Schwartz RJ, Lin HK, Cowan RL, Jones AN, Kropp BP.
Department of Urology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
PURPOSE: Smooth muscle alpha-actin (SMalphaA) is an important actin isoform for functional contractility in the mouse bladder. Alterations in the expression of SMalphaA have been associated with a variety of bladder pathological conditions. Recently, a SMalphaA-null mouse was generated and differences in vascular tone and contractility were observed between wild-type and SMalphaA-null mice suggesting alterations in function of vascular smooth muscle. We used SMalphaA-null mice to explore the hypothesis that SMalphaA is necessary for normal bladder function. MATERIALS AND METHODS: Reverse transcriptase polymerase chain reaction, Western blotting and immunohistochemical staining were used to confirm the absence of SMalphaA transcript and protein in the bladder of SMalphaA-null mice. In vitro bladder contractility compared between bladder rings harvested from wild-type and SMalphaA-null mice was determined by force measurement following electrical field stimulation (EFS), and exposure to chemical agonists and antagonists including KCl, carbachol, atropine and tetrodotoxin. Resulting force generation profiles for each tissue and agent were analyzed. RESULTS: There was no detectable SMalphaA transcript and protein expression in the bladder of SMalphaA-null mice. Nine wild-type and 9 SMalphaA-null mice were used in the contractility study. Bladders from SMalphaA-null mice generated significantly less force than wild-type mice in response to EFS after KCl. Similarly, bladders from SMalphaA-null mice generated less force than wild-type mice in response to pretreatment EFS, and EFS after carbachol and atropine, although the difference was not significant. Surprisingly, the bladders in SMalphaA-null mice appeared to function normally and showed no gross or histological abnormalities. CONCLUSIONS: SMalphaA appears to be necessary for the bladder to be able to generate normal levels of contractile force. No functional deficits were observed in the bladders of these animals but no stress was placed on these bladders. To our knowledge this study represents the first report to demonstrate the importance of expression of SMalphaA in force generation in the bladder.
Publication Types:
Review
PMID: 15371786 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Chest. 2003 Mar;123(3 Suppl):392S-8S.
Actin dynamics: a potential integrator of smooth muscle (Dys-)function and contractile apparatus gene expression in asthma. Parker B. Francis lecture.
Solway J, Bellam S, Dowell M, Camoretti-Mercado B, Dulin N, Fernandes D, Halayko A, Kocieniewski P, Kogut P, Lakser O, Liu HW, McCauley J, McConville J, Mitchell R.
Section of Pulmonary and Critical Care Medicine, Department of Medicine, University of Chicago, Chicago, IL 60637, USA. jsolway@medicine.bsd.unichicago.edu
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12629000 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Wound Repair Regen. 2001 Jan-Feb;9(1):11-8.
Musculoskeletal connective tissue cells with muscle: expression of muscle actin in and contraction of fibroblasts, chondrocytes, and osteoblasts.
Spector M.
Department of Orthopaedic Surgery, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. mspector@rics.bwh.harvard.edu
The expression of the gene for a muscle actin in certain nonmuscle cells and the contraction of these connective tissue cells has been associated with several important physiological and pathological processes; the contraction of healing skin wounds and the contracture in Dupuytren's disease being two notable examples. Studies in recent years have shown that a much wider variety of connective tissue cells than previously considered, including cells in many of the musculoskeletal tissues, e.g., chondrocytes and osteoblasts, can express the gene for alpha-smooth muscle actin and can display contractile behavior. These findings suggest that muscle actin-enabled cell contraction may also be playing important roles in the other connective tissues comprising the musculoskeletal system, namely, tendon, ligament, meniscus, intervertebral disc, articular cartilage, and bone.
Publication Types:
Review
PMID: 11350635 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Zoolog Sci. 1997 Oct;14(5):707-18.
Ascidian actin genes: developmental regulation of gene expression and molecular evolution.
Kusakabe T.
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Actin is a ubiquitous protein in eukaryotic cells and plays an important role in cell structure, cell motility, and the generation of contractile force in both muscle and nonmuscle cells. Multiple genes encoding muscle or nonmuscle actins have been isolated from several species of ascidians and their expression patterns have been investigated. Sequence and expression analyses of muscle actin genes have shown that ascidians have at least two distinct isoforms of muscle actin, the larval muscle and body-wall isoforms. In the ascidian Halocynthia roretzi, two clusters of actin genes are expressed in the larval muscle cells. The HrMA2/4 cluster contains at least five actin genes and the HrMA1 cluster contains a pair of actin genes whose expression is regulated by a single bidirectional promoter. cis-Regulatory elements essential for muscle-specific expression of a larval muscle actin gene HrMA4a have been identified. The adult body-wall muscle actin is clearly distinguished from the larval muscle actin by diagnostic amino acids. The adult muscle actin genes may be useful tools to investigate the mechanisms of muscle development in ascidian adults. The evolution of chordate actin genes has been inferred by comparing the organization and sequences of actin genes and performing molecular phylogenetic analysis. The results suggest a close relationship between ascidian and vertebrate actins. The chordate ancestor seems to have evolved the "chordate-type" cytoplasmic and muscle actins before its divergence into vertebrates and urochordates. The phylogenetic analysis also suggests that the vertebrate muscle actin isoforms evolved after the separation of the vertebrates and urochordates. Muscle actin genes have been used to investigate the mechanism of muscle cell regression during the evolution of anural development. The results suggest that the regression of muscle cell differentiation is mediated by changes in the structure of muscle actin genes rather than in the trans-acting regulatory factors required for their expression. Actin genes have provided a unique system to study developmental and evolutionary mechanisms in chordates.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9450384 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Biochimie. 1996;78(11-12):1075-80.
A role for Rev in the association of HIV-1 gag mRNA with cytoskeletal beta-actin and viral protein expression.
Kimura T, Hashimoto I, Nishikawa M, Fujisawa JI.
Department of Microbiology, Kansai Medical University, Osaka, Japan.
Human immunodeficiency virus type-1 (HIV-1) Rev acts by inducing the specific nucleocytoplasmic transport of a class of incompletely spliced RNAs that encodes the viral structural proteins. The transfection of HeLa cells with a rev-defective HIV-1 expression plasmid, however, resulted in the export of overexpressed, intron-containing species of viral RNAs, possibly through a default process of nuclear retention. Thus, this system enabled us to directly compare Rev+ and Rev+ cells as to the usage of RRE-containing mRNAs by the cellular translational machinery. Biochemical examination of the transfected cells revealed that although significant levels of gag and env mRNAs were detected in both the presence and absence of Rev, efficient production of viral proteins was strictly dependent on the presence of Rev. A fluorescence in situ hybridisation assay confirmed these findings and provided further evidence that even in the presence of Rev, not all of the viral mRNA was equally translated. At the early phase of RNA export in Rev+ cells, gag mRNA was observed throughout both the cytoplasm and nucleoplasm as uniform fine stippling. In addition, the mRNA formed clusters mainly in the perinuclear region, which were not observed in Rev+ cells. In the presence of Rev, expression of the gag protein was limited to these perinuclear sites where the mRNA accumulated. Subsequent staining of the cytoskeletal proteins demonstrated that in Rev+ cells gag mRNA is colocalized with beta-actin in the sites where the RNA formed clusters. In the absence of Rev, in contrast, the gag mRNA failed to associate with the cytoskeletal proteins. These results suggest that in addition to promoting the emergence of intron-containing RNA from the nucleus, Rev plays an important role in the compartmentation of translation by directing RRE-containing mRNAs to the beta-actin to form the perinuclear clusters at which the synthesis of viral structural proteins begins.
Publication Types:
Review
PMID: 9150887 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Adv Exp Med Biol. 1994;358:215-30.
Control of p52(PAI-1) gene expression in normal and transformed rat kidney cells: relationship between p52(PAI-1) induction and actin cytoarchitecture.
Ryan MP, Higgins PJ.
Department of Microbiology, Immunology and Molecular Genetics, Albany Medical College, New York 12208.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 7801807 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Tanpakushitsu Kakusan Koso. 1993 Mar;38(4):721-30.
[Structure and expression of actin genes]
[Article in Japanese]
Kusakabe T, Satoh N.
Department of Zoology, Faculty of Science, Kyoto University, Japan.
Publication Types:
English Abstract
Review
PMID: 8475328 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Int Rev Cytol. 1991;125:139-63.
Divergence and differential expression of actin gene families in higher plants.
Meagher RB.
Department of Genetics, University of Georgia, Athens 30602.
Publication Types:
Comparative Study
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2032783 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Biotechnology. 1991;16:103-24.
Expression of a human multidrug-resistance cDNA (MDR1) under the control of a beta-actin promoter in transgenic mice.
Galski H, Merlino GT, Gottesman MM, Pastan I.
Publication Types:
Review
PMID: 2007187 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Med Hypotheses. 1990 May;32(1):39-43.
Are changes in expression of actin genes involved in estrogen-induced cholestasis?
Reyes-Romero MA.
Facultad de Medicina, Universidad Juárez del Estado de Durango, Department of Biochemistry, México.
It is postulated that cholestasis associated with high estrogen levels found in women in various conditions, is due to alterations in structure and/or function of the system of actin microfilaments by estrogen-induced changes on expression of actin genes and/or some regulatory actin-binding protein genes. Because bile secretion by hepatocytes is apparently mediated by the microfilamentous system of actin, the proposed hormonally induced dysfunction of this system could be translated to cholestasis.
Publication Types:
Review
PMID: 2190068 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Prog Clin Biol Res. 1990;327:583-9.
Cellular and molecular control of vascular smooth muscle alpha-actin gene expression during BC3H1 myogenic cell differentiation.
Strauch AR, Min B, Reeser JC, Berman MD, Miller HR, Foster DN.
Department of Anatomy, Ohio State University, Columbus 43210.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 2181477 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: Dev Biol (N Y 1985). 1988;5:189-208.
Regulation of actin gene expression during sea urchin development.
Crain WR Jr.
Cell Biology Group, Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
The progress that has been made in the last several years toward an understanding of the expression of the actin genes of the sea urchin is impressive. It serves as an excellent example of how the application of modern molecular biological techniques to a classic experimental system (the sea urchin embryo) can begin to give us insight into the processes of embryological development. There is reason to hope that general principles will emerge from studies such as these, but many questions are unanswered. With specific regard to the actin genes and proteins, there are some obvious questions. Are the actins encoded by the different genes functionally distinct, and what roles do they play in differentiation and development? How is the expression of each of these genes regulated; i.e., what molecules participate, how do they work, where are they located in the embryo, and when do they appear? The more general question is: How are these (and other) genes and proteins affected by, or how do they contribute to, determination and induction in early development? We hope that answers to the specific questions posed will provide important steps toward answers to the general question.
Publication Types:
Review
PMID: 3077974 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Essays Biochem. 1985;20:77-109.
Actin and myosin multigene families: their expression during the formation of skeletal muscle.
Buckingham ME.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 3896780 [PubMed - indexed for MEDLINE]
Pathological situations characterized by altered actin isoform expression.
Chaponnier C, Gabbiani G.
Department of Pathology and Immunology, CMU, University of Geneva, Geneva, Switzerland. Christine.Chaponnier@medecine.unige.ch
Modulation of actin isoform expression is a well-established feature of developmental phenomena. As one might expect, it is also characteristic of several pathological situations that are the subject of the present review. alpha-Smooth muscle actin has proven to be a reliable marker for identifying (a) vascular smooth muscle cells during vascular development and vascular diseases, and (b) myofibroblasts during wound healing, fibrocontractive diseases, and stromal reaction to epithelial tumours. The hallmark of a differentiated myofibroblast relies on the acquisition of an organized contractile apparatus characterized by alpha-smooth muscle actin-expressing stress fibres. More and more data suggest that alpha-smooth muscle actin plays a direct role in myofibroblast contractile activity through its N-terminal domain AcEEED. Newly developed antibodies against alpha-skeletal and alpha-cardiac actins have allowed the detection of subpopulations of alpha-skeletal positive cardiomyocytes in adult, hypertrophic, and failing heart. These antibodies have also permitted us to identify the differentiation degree of malignant cells in tumours such as rhabdomyosarcoma. Whether the differential expression of actin isoforms in human diseases is functionally relevant is not yet fully established, although studies on human actin mutations, actin null mice, and the N-terminal end of alpha-smooth muscle actin support this possibility. Copyright (c) 2004 Pathological Society of Great Britain and Ireland.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15495226 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: J Urol. 2004 Oct;172(4 Pt 2):1667-72.
Decreased expression of smooth muscle alpha-actin results in decreased contractile function of the mouse bladder.
Zimmerman RA, Tomasek JJ, McRae J, Haaksma CJ, Schwartz RJ, Lin HK, Cowan RL, Jones AN, Kropp BP.
Department of Urology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
PURPOSE: Smooth muscle alpha-actin (SMalphaA) is an important actin isoform for functional contractility in the mouse bladder. Alterations in the expression of SMalphaA have been associated with a variety of bladder pathological conditions. Recently, a SMalphaA-null mouse was generated and differences in vascular tone and contractility were observed between wild-type and SMalphaA-null mice suggesting alterations in function of vascular smooth muscle. We used SMalphaA-null mice to explore the hypothesis that SMalphaA is necessary for normal bladder function. MATERIALS AND METHODS: Reverse transcriptase polymerase chain reaction, Western blotting and immunohistochemical staining were used to confirm the absence of SMalphaA transcript and protein in the bladder of SMalphaA-null mice. In vitro bladder contractility compared between bladder rings harvested from wild-type and SMalphaA-null mice was determined by force measurement following electrical field stimulation (EFS), and exposure to chemical agonists and antagonists including KCl, carbachol, atropine and tetrodotoxin. Resulting force generation profiles for each tissue and agent were analyzed. RESULTS: There was no detectable SMalphaA transcript and protein expression in the bladder of SMalphaA-null mice. Nine wild-type and 9 SMalphaA-null mice were used in the contractility study. Bladders from SMalphaA-null mice generated significantly less force than wild-type mice in response to EFS after KCl. Similarly, bladders from SMalphaA-null mice generated less force than wild-type mice in response to pretreatment EFS, and EFS after carbachol and atropine, although the difference was not significant. Surprisingly, the bladders in SMalphaA-null mice appeared to function normally and showed no gross or histological abnormalities. CONCLUSIONS: SMalphaA appears to be necessary for the bladder to be able to generate normal levels of contractile force. No functional deficits were observed in the bladders of these animals but no stress was placed on these bladders. To our knowledge this study represents the first report to demonstrate the importance of expression of SMalphaA in force generation in the bladder.
Publication Types:
Review
PMID: 15371786 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Chest. 2003 Mar;123(3 Suppl):392S-8S.
Actin dynamics: a potential integrator of smooth muscle (Dys-)function and contractile apparatus gene expression in asthma. Parker B. Francis lecture.
Solway J, Bellam S, Dowell M, Camoretti-Mercado B, Dulin N, Fernandes D, Halayko A, Kocieniewski P, Kogut P, Lakser O, Liu HW, McCauley J, McConville J, Mitchell R.
Section of Pulmonary and Critical Care Medicine, Department of Medicine, University of Chicago, Chicago, IL 60637, USA. jsolway@medicine.bsd.unichicago.edu
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12629000 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Wound Repair Regen. 2001 Jan-Feb;9(1):11-8.
Musculoskeletal connective tissue cells with muscle: expression of muscle actin in and contraction of fibroblasts, chondrocytes, and osteoblasts.
Spector M.
Department of Orthopaedic Surgery, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. mspector@rics.bwh.harvard.edu
The expression of the gene for a muscle actin in certain nonmuscle cells and the contraction of these connective tissue cells has been associated with several important physiological and pathological processes; the contraction of healing skin wounds and the contracture in Dupuytren's disease being two notable examples. Studies in recent years have shown that a much wider variety of connective tissue cells than previously considered, including cells in many of the musculoskeletal tissues, e.g., chondrocytes and osteoblasts, can express the gene for alpha-smooth muscle actin and can display contractile behavior. These findings suggest that muscle actin-enabled cell contraction may also be playing important roles in the other connective tissues comprising the musculoskeletal system, namely, tendon, ligament, meniscus, intervertebral disc, articular cartilage, and bone.
Publication Types:
Review
PMID: 11350635 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Zoolog Sci. 1997 Oct;14(5):707-18.
Ascidian actin genes: developmental regulation of gene expression and molecular evolution.
Kusakabe T.
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Actin is a ubiquitous protein in eukaryotic cells and plays an important role in cell structure, cell motility, and the generation of contractile force in both muscle and nonmuscle cells. Multiple genes encoding muscle or nonmuscle actins have been isolated from several species of ascidians and their expression patterns have been investigated. Sequence and expression analyses of muscle actin genes have shown that ascidians have at least two distinct isoforms of muscle actin, the larval muscle and body-wall isoforms. In the ascidian Halocynthia roretzi, two clusters of actin genes are expressed in the larval muscle cells. The HrMA2/4 cluster contains at least five actin genes and the HrMA1 cluster contains a pair of actin genes whose expression is regulated by a single bidirectional promoter. cis-Regulatory elements essential for muscle-specific expression of a larval muscle actin gene HrMA4a have been identified. The adult body-wall muscle actin is clearly distinguished from the larval muscle actin by diagnostic amino acids. The adult muscle actin genes may be useful tools to investigate the mechanisms of muscle development in ascidian adults. The evolution of chordate actin genes has been inferred by comparing the organization and sequences of actin genes and performing molecular phylogenetic analysis. The results suggest a close relationship between ascidian and vertebrate actins. The chordate ancestor seems to have evolved the "chordate-type" cytoplasmic and muscle actins before its divergence into vertebrates and urochordates. The phylogenetic analysis also suggests that the vertebrate muscle actin isoforms evolved after the separation of the vertebrates and urochordates. Muscle actin genes have been used to investigate the mechanism of muscle cell regression during the evolution of anural development. The results suggest that the regression of muscle cell differentiation is mediated by changes in the structure of muscle actin genes rather than in the trans-acting regulatory factors required for their expression. Actin genes have provided a unique system to study developmental and evolutionary mechanisms in chordates.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9450384 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Biochimie. 1996;78(11-12):1075-80.
A role for Rev in the association of HIV-1 gag mRNA with cytoskeletal beta-actin and viral protein expression.
Kimura T, Hashimoto I, Nishikawa M, Fujisawa JI.
Department of Microbiology, Kansai Medical University, Osaka, Japan.
Human immunodeficiency virus type-1 (HIV-1) Rev acts by inducing the specific nucleocytoplasmic transport of a class of incompletely spliced RNAs that encodes the viral structural proteins. The transfection of HeLa cells with a rev-defective HIV-1 expression plasmid, however, resulted in the export of overexpressed, intron-containing species of viral RNAs, possibly through a default process of nuclear retention. Thus, this system enabled us to directly compare Rev+ and Rev+ cells as to the usage of RRE-containing mRNAs by the cellular translational machinery. Biochemical examination of the transfected cells revealed that although significant levels of gag and env mRNAs were detected in both the presence and absence of Rev, efficient production of viral proteins was strictly dependent on the presence of Rev. A fluorescence in situ hybridisation assay confirmed these findings and provided further evidence that even in the presence of Rev, not all of the viral mRNA was equally translated. At the early phase of RNA export in Rev+ cells, gag mRNA was observed throughout both the cytoplasm and nucleoplasm as uniform fine stippling. In addition, the mRNA formed clusters mainly in the perinuclear region, which were not observed in Rev+ cells. In the presence of Rev, expression of the gag protein was limited to these perinuclear sites where the mRNA accumulated. Subsequent staining of the cytoskeletal proteins demonstrated that in Rev+ cells gag mRNA is colocalized with beta-actin in the sites where the RNA formed clusters. In the absence of Rev, in contrast, the gag mRNA failed to associate with the cytoskeletal proteins. These results suggest that in addition to promoting the emergence of intron-containing RNA from the nucleus, Rev plays an important role in the compartmentation of translation by directing RRE-containing mRNAs to the beta-actin to form the perinuclear clusters at which the synthesis of viral structural proteins begins.
Publication Types:
Review
PMID: 9150887 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Adv Exp Med Biol. 1994;358:215-30.
Control of p52(PAI-1) gene expression in normal and transformed rat kidney cells: relationship between p52(PAI-1) induction and actin cytoarchitecture.
Ryan MP, Higgins PJ.
Department of Microbiology, Immunology and Molecular Genetics, Albany Medical College, New York 12208.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 7801807 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Tanpakushitsu Kakusan Koso. 1993 Mar;38(4):721-30.
[Structure and expression of actin genes]
[Article in Japanese]
Kusakabe T, Satoh N.
Department of Zoology, Faculty of Science, Kyoto University, Japan.
Publication Types:
English Abstract
Review
PMID: 8475328 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Int Rev Cytol. 1991;125:139-63.
Divergence and differential expression of actin gene families in higher plants.
Meagher RB.
Department of Genetics, University of Georgia, Athens 30602.
Publication Types:
Comparative Study
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2032783 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Biotechnology. 1991;16:103-24.
Expression of a human multidrug-resistance cDNA (MDR1) under the control of a beta-actin promoter in transgenic mice.
Galski H, Merlino GT, Gottesman MM, Pastan I.
Publication Types:
Review
PMID: 2007187 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Med Hypotheses. 1990 May;32(1):39-43.
Are changes in expression of actin genes involved in estrogen-induced cholestasis?
Reyes-Romero MA.
Facultad de Medicina, Universidad Juárez del Estado de Durango, Department of Biochemistry, México.
It is postulated that cholestasis associated with high estrogen levels found in women in various conditions, is due to alterations in structure and/or function of the system of actin microfilaments by estrogen-induced changes on expression of actin genes and/or some regulatory actin-binding protein genes. Because bile secretion by hepatocytes is apparently mediated by the microfilamentous system of actin, the proposed hormonally induced dysfunction of this system could be translated to cholestasis.
Publication Types:
Review
PMID: 2190068 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Prog Clin Biol Res. 1990;327:583-9.
Cellular and molecular control of vascular smooth muscle alpha-actin gene expression during BC3H1 myogenic cell differentiation.
Strauch AR, Min B, Reeser JC, Berman MD, Miller HR, Foster DN.
Department of Anatomy, Ohio State University, Columbus 43210.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 2181477 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: Dev Biol (N Y 1985). 1988;5:189-208.
Regulation of actin gene expression during sea urchin development.
Crain WR Jr.
Cell Biology Group, Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
The progress that has been made in the last several years toward an understanding of the expression of the actin genes of the sea urchin is impressive. It serves as an excellent example of how the application of modern molecular biological techniques to a classic experimental system (the sea urchin embryo) can begin to give us insight into the processes of embryological development. There is reason to hope that general principles will emerge from studies such as these, but many questions are unanswered. With specific regard to the actin genes and proteins, there are some obvious questions. Are the actins encoded by the different genes functionally distinct, and what roles do they play in differentiation and development? How is the expression of each of these genes regulated; i.e., what molecules participate, how do they work, where are they located in the embryo, and when do they appear? The more general question is: How are these (and other) genes and proteins affected by, or how do they contribute to, determination and induction in early development? We hope that answers to the specific questions posed will provide important steps toward answers to the general question.
Publication Types:
Review
PMID: 3077974 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Essays Biochem. 1985;20:77-109.
Actin and myosin multigene families: their expression during the formation of skeletal muscle.
Buckingham ME.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 3896780 [PubMed - indexed for MEDLINE]
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