Fibronectin Expression
Published by Anonymous on 2007/9/29 (2027 reads)
1: Fa Yi Xue Za Zhi. 2003;19(3):190-2, inside backcover.
[The research progress of fibronectin EDA's expression and functions]
[Article in Chinese]
Xue AM, Zhao ZQ.
Department of Forensic Medicine, Shanghai Medical School, Fudan uiversity, Shanghai 200032, China
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15116753 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Fa Yi Xue Za Zhi. 2001 Nov;17(4):245-8.
[The alternative splicing & expression of fibronectin IIIcs segment and its relationship with wound healing]
[Article in Chinese]
Ji Y, Zhao ZQ.
Department of Forensic Medicine, Medical Center of Fudan University, Shanghai 200032. jigi0412@yahoo.com
Fibronectin is an important large adhesive glycoprotein of the extracellular matrix, which is alternatively spliced in three regions, designated EIIIA, EIIIB and IIIcs respectively. IIIcs contains two binding domains for a variety of cell surface and extracellular ligands. Through this multiplicity of adhesive activities, IIIcs can fulfill key roles in a broad spectrum of physiological processes, such as cell spreading and migration, differentiation and embryogenesis, wound healing, malignant transformation and metastasis, etc. Here, we will discuss the structure, biological property, and function of IIIcs splicing variants and its forensic applications.
Publication Types:
English Abstract
Review
PMID: 12533877 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Kidney Int Suppl. 2000 Sep;77:S88-92.
Effect of lovastatin on small GTP binding proteins and on TGF-beta1 and fibronectin expression.
Kim SI, Kim HJ, Han DC, Lee HB.
Hyonam Kidney Laboratory, Soon Chun Hyang University, Seoul, Korea.
We have shown that lovastatin, an inhibitor of 3 hydroxy-3-methylglutary coenzyme A (HMG CoA) reductase, delays development and progression of diabetic nephropathy in streptozotocine-induced diabetic rats through suppression of glomerular transforming growth factor (TGF)-beta1 mRNA expression. We have also shown that lovastatin suppresses both control and high glucose (HG)-induced TGF-beta1 and fibronectin mRNA expression and protein synthesis by rat mesangial cell (RMC) and that this down-regulation by lovastatin is reversed by mevalonate. It was postulated that this down-regulation may be linked to signaling of small guanine triphosphate (GTP)-binding proteins and mediated by the limitation of isoprenoids such as farnesylpyrophosphate (FPP) and geranylgeranylpyrophosphate (GGPP) in RMC. To determine the isoprenoid and small GTP-binding proteins involved in TGF-beta1 and fibronectin expression. FPP or GGPP was added alone or in combination to RMC treated with lovastatin cultured under normal or high glucose condition. Suppression of TGF-beta1 and fibronectin expression by lovastatin was reversed effectively when GGPP was added alone. Partial reversal of lovastatin effect on fibronectin and TGF-beta1 expression was found when FPP was added alone. Adding both GGPP and FPP resulted in complete reversal of lovastatin effect on fibronectin but not TGF-beta1 suggesting that fibronectin and TGF-beta1 are regulated differently. Furthermore, luciferase activity of RMC cotransfected with fibronectin promoter reporter system and plasmid-expressing C3 exoenzyme (a specific inactivator of Rho family GTP binding proteins, pEFC3) was completely suppressed when compared with RMC cotransfected with empty vector, pEF. Because geranylgeranylation is usually involved in post-translational modification and membrane targeting of Rho family small GTP binding proteins, these data indicate that Rho family small GTP-binding proteins rather than Ras family small GTP binding proteins may play a key role in the TGF-beta1 and fibronectin expression in RMC.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 10997696 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Exp Gerontol. 1997 Jan-Apr;32(1-2):95-103.
Expression of endothelin, fibronectin, and mortalin as aging and mortality markers.
Kumazaki T, Wadhwa R, Kaul SC, Mitsui Y.
Department of Biochemistry and Biophysics, Hiroshima University, Japan.
Studies on fibronectin, endothelin-1, and mortalin from our laboratory are reviewed here. Fibronectin expression has been analyzed as upregulated during in vitro serial passaging of human fetal lung and neonatal foreskin fibroblasts as well as umbilical vein endothelial cells. In vivo aging of skin fibroblasts, as well as aortic endothelial cells, are also accompanied by upregulation of fibronectin expression. Fibronectin promoter binding proteins from young and old cell nuclear extracts were further explored by gel retardation assay. Preliminary analyses have detected age-related differential binding activities with respect to AP-1, CRES, TFIID, CTF, and AP-2 regions, whereas Sp1 binding proteins remain unaltered. Endothelin-1 expression is also seen as upregulated during in vitro and in vivo aging of endothelial cells. This can contribute to the hypertension commonly observed in elderly patients. Mortalin, a novel member of hsp 70 family of proteins, was initially identified by virtue of its association with a cellular mortal phenotype. Subsequently, normal cells and the ones with an immortal phenotype have been found to have differential subcellular localization of this protein. Antiproliferative activity of this protein in normal cells and the deregulation of expression in transformed cells is observed which suggests the association of mortalin in pathways that determine cellular divisional phenotype.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9088906 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Herz. 1995 Apr;20(2):118-26.
Fibronectin expression in the cardiovascular system.
Sabri A, Farhadian F, Contard F, Samuel JL, Rappaport L.
Unité 127 INSERM, IFR Circulation, Université D Diderot, Hôpital Lariboisiére, Paris, France.
Fibronectin (FN) is a dimeric glycoprotein found in the extracellular matrix (ECM) of most tissues and serves as a bridge between cells and the interstitial collagen meshwork. It also influences diverse processes including cell growth, adhesion, migration, and wound repair. Multiple FN forms arise by the alternative splicing of a primary transcript originating from a single gene. The spatial and temporal alterations in FN expression in the cardiovascular system have been studied in vitro in cell culture and in vivo during fetal development, hypertrophy, infarction, arterial injury and aging. This review describes characteristics of FN expression in cardiovascular system: 1. the FN phenotype is regulated during development. A high FN mRNA level is related to an early cardiac organogenesis and a progressive decrease that begins at the fetal stage and continues through senescence. During cardiac ontogeny, there is a linear correlation between total FN mRNA accumulation and the relative amounts of FN-EIIIA and EIIIB RNA. This correlation is absent during cardiac growth in the adult. 2. A differential reexpression of the FN isoforms is observed in both myocardium and aorta in different models of hypertension or infarction but with different threshold and time course. Changes in total FN mRNA levels in hypertensive models vary depending on the authors. Nevertheless the differences in the expression of the fetal forms of FN mRNA observed among the various models of hypertension-induced hypertrophy indicate that the process of FN pre-mRNA splicing in the adult myocardium is specifically regulated and depends on the pathological situations and the type of cell.(ABSTRACT TRUNCATED AT 250 WORDS)
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 7774863 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: J Mol Cell Cardiol. 1995 Apr;27(4):981-90.
Fibronectin expression during physiological and pathological cardiac growth.
Farhadian F, Contard F, Corbier A, Barrieux A, Rappaport L, Samuel JL.
Unité 127 INSERM, IFR Circulation, Université D Diderot Hopital Lariboisiére, Paris, France.
Fibronectin (FN) is a dimeric glycoprotein found in the extracellular matrix of most tissues that serves as a bridge between cells and the interstitial collagen meshwork and influences diverse processes including cell growth, adhesion, migration, and wound repair. Multiple FN forms arise by the alternative splicing of a primary transcript originating from a single gene. The spatial and temporal alterations in FN expression in the myocardium has been studied in models of cardiac growth in vivo such as fetal development, and hypertrophy secondary to pressure overload. This review focuses on the differential expression of FN isoforms that are observed in different models of cardiac growth. Using a combination of qualitative and quantitative analyses it is shown that in the rat myocardium: (1) the FN phenotype is developmentally regulated, (2) the re-expression of the fetal FN isoforms is observed in different models of cardiac hypertrophy secondary to a sudden or progressive hypertension and (3) the changes in cardiac FN expression affect mostly the coronary artery smooth muscle cells.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 7563110 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Am Rev Respir Dis. 1991 Sep;144(3 Pt 2):S25-8.
Glycoprotein synthesis and secretion. Expression of fibronectin and its cell surface receptors.
Dean DC, Birkenmeier TM, Rosen GD, Weintraub SJ.
Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
Fibronectin (FN) is an extracellular matrix protein that acts as a substrate for cell migration and adhesion during development. Cells adhere to FN through integral membrane proteins that are members of the integrin family of adhesion molecules. The interaction between cells and FN is important in a number of biologic processes, including gastrulation, hematopoietic differentiation, neural crest cell migration, cardiac development, branching morphogenesis in lung, wound healing, tumorigenesis, and metastasis. Expression of FN and its receptors is controlled by a number of hormones and growth factors as well as by tissue-specific factors. Here, the molecular aspects of how expression of these genes is controlled are reviewed, with particular emphasis on promoter regulator elements that modulate expression.
Publication Types:
Review
PMID: 1832529 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Cell Differ Dev. 1990 Dec 2;32(3):401-8.
Expression of tenascin and of the ED-B containing oncofetal fibronectin isoform in human cancer.
Nicolò G, Salvi S, Oliveri G, Borsi L, Castellani P, Zardi L.
Laboratory of Anatomic Pathology, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.
Tenascin (TN) and the oncofetal ED-B containing fibronectin isoform (B-FN) have been reported to be stromal markers of a number of malignancies. Here we report on studies of the distribution of TN and B-FN in normal adult tissues and in benign and malignant tumors, as well as on the levels of the B-FN mRNA in cultured fetal and non-fetal human fibroblasts originating from different tissues. B-FN has an extremely restricted distribution in normal adult tissues, is not expressed in benign tumors, but is greatly expressed in a high percentage of malignant tumors. On the contrary, human TN in normal adult tissues is less restricted than what has previously been reported and it is largely expressed in a number of both benign and malignant tumors. Moreover, we observed a great variability in the relative amount of B-FN mRNA among the 17 normal human fibroblast cell lines tested. We found very low levels in non-fetal skin fibroblasts and higher levels in fetal lung fibroblasts. We also found differences in the relative amounts of B-FN mRNA between fibroblast cell lines originating from the skin and the lung of the same subject.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Review
PMID: 1711919 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: J Invest Dermatol. 1990 Jun;94(6 Suppl):128S-134S.
Fibronectin matrix deposition and fibronectin receptor expression in healing and normal skin.
Clark RA.
Department of Dermatology and Medicine, University of Colorado School of Medicine, Denver.
During cutaneous tissue organization, numerous critical interactions occur between cells and the extracellular matrix (ECM). Cell-matrix interactions depend on the presence of ECM receptors. Many ECM receptors, known as integrins, are heterodimeric glycoproteins consisting of one alpha and one beta chain. Integrins containing beta 1 or beta 3 chains are ECM receptors, whereas those containing beta 2 chains are leukocyte cell-cell receptors. We have used porcine cutaneous wounds as a paradigm for tissue organization and probed healing wounds and adjacent normal skin with polyclonal antibodies to fibronectin and fibronectin (alpha 5 beta 1) receptor. During re-epithelialization, the epidermis transits over a provisional matrix containing fibronectin. Migrating epidermal cells expressed fibronectin receptors in a bright linear peripheral pattern. At 10 days, when reepithelialization was complete and the basement membrane was re-established, the fibronectin matrix was markedly reduced and fibronectin-receptor expression was limited to the basolateral aspect of basal cells, as observed in normal epidermis. Beneath the migrating epidermis in 5-d wounds, granulation tissue had filled 80% of the wound space. Day-5 wound fibroblasts did not express fibronectin nor other beta 1 integrin receptors, were randomly oriented, and contained no actin bundles. Fibronectin fibrils were assembled on the surfaces of day-5 wound fibroblasts but formed few linkages between cells. Day-7 wound fibroblasts expressed fibronectin receptors, contained peripheral cytoplasmic actin bundles consistent with a contractile fibroblast phenotype, and were coaligned across the wound in parallel array with interconnecting fibronectin fibrils. The wounds contracted between 7 and 10 days. Thus the migrating epidermis consistently expressed fibronectin receptors. Fibronectin receptors were expressed by fibroblasts just prior to wound contraction.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2161886 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Am J Respir Cell Mol Biol. 1989 Jul;1(1):5-10.
Expression of the fibronectin gene.
Dean DC.
Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.
Fibronectin (FN) is an extracellular matrix protein that acts as a substrate for cell migration and adhesion during development. FN adheres to cells through a dimeric membrane protein, the FN receptor. Antibodies to FN and synthetic peptides that inhibit FN-receptor interaction inhibit gastrulation, block neural crest cell migration, arrest cardiac development, and block the fusion of myoblasts to form myotubes. FN and its receptor also appear to be important for lung development, where their expression coincides with the onset of branching morphogenesis, but drops to barely detectable levels in adult lung, indicating developmental specificity. FN expression is generally low in most adult tissues. However, synthesis is drastically increased during injury and wound healing, a process that in many ways mimics development. FN synthesis is also drastically increased in fibroproliferative lung lesions associated with major architectural changes in the lung. Expression of FN is regulated by a variety of growth factors and hormones. Several of these inducers (cAMP, transforming growth factor-beta, epidermal growth factor, platelet-derived growth factor, glucocorticoids, and vitamin D3) have themselves been implicated in developmental processes, and both cAMP and transforming growth factor-beta are known to stimulate expression of other matrix genes. One role of these hormones and growth factors in development may be to control expression of matrix genes, thereby controlling cell migration and adhesion. In the following report, the effect of hormones and growth factors on expression of the FN gene is reviewed.
Publication Types:
Review
PMID: 2696510 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Nutr Rev. 1988 Apr;46(4):168-70.
Vitamin A controls fibronectin gene expression.
[No authors listed]
Publication Types:
Review
PMID: 3285252 [PubMed - indexed for MEDLINE]
[The research progress of fibronectin EDA's expression and functions]
[Article in Chinese]
Xue AM, Zhao ZQ.
Department of Forensic Medicine, Shanghai Medical School, Fudan uiversity, Shanghai 200032, China
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15116753 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Fa Yi Xue Za Zhi. 2001 Nov;17(4):245-8.
[The alternative splicing & expression of fibronectin IIIcs segment and its relationship with wound healing]
[Article in Chinese]
Ji Y, Zhao ZQ.
Department of Forensic Medicine, Medical Center of Fudan University, Shanghai 200032. jigi0412@yahoo.com
Fibronectin is an important large adhesive glycoprotein of the extracellular matrix, which is alternatively spliced in three regions, designated EIIIA, EIIIB and IIIcs respectively. IIIcs contains two binding domains for a variety of cell surface and extracellular ligands. Through this multiplicity of adhesive activities, IIIcs can fulfill key roles in a broad spectrum of physiological processes, such as cell spreading and migration, differentiation and embryogenesis, wound healing, malignant transformation and metastasis, etc. Here, we will discuss the structure, biological property, and function of IIIcs splicing variants and its forensic applications.
Publication Types:
English Abstract
Review
PMID: 12533877 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Kidney Int Suppl. 2000 Sep;77:S88-92.
Effect of lovastatin on small GTP binding proteins and on TGF-beta1 and fibronectin expression.
Kim SI, Kim HJ, Han DC, Lee HB.
Hyonam Kidney Laboratory, Soon Chun Hyang University, Seoul, Korea.
We have shown that lovastatin, an inhibitor of 3 hydroxy-3-methylglutary coenzyme A (HMG CoA) reductase, delays development and progression of diabetic nephropathy in streptozotocine-induced diabetic rats through suppression of glomerular transforming growth factor (TGF)-beta1 mRNA expression. We have also shown that lovastatin suppresses both control and high glucose (HG)-induced TGF-beta1 and fibronectin mRNA expression and protein synthesis by rat mesangial cell (RMC) and that this down-regulation by lovastatin is reversed by mevalonate. It was postulated that this down-regulation may be linked to signaling of small guanine triphosphate (GTP)-binding proteins and mediated by the limitation of isoprenoids such as farnesylpyrophosphate (FPP) and geranylgeranylpyrophosphate (GGPP) in RMC. To determine the isoprenoid and small GTP-binding proteins involved in TGF-beta1 and fibronectin expression. FPP or GGPP was added alone or in combination to RMC treated with lovastatin cultured under normal or high glucose condition. Suppression of TGF-beta1 and fibronectin expression by lovastatin was reversed effectively when GGPP was added alone. Partial reversal of lovastatin effect on fibronectin and TGF-beta1 expression was found when FPP was added alone. Adding both GGPP and FPP resulted in complete reversal of lovastatin effect on fibronectin but not TGF-beta1 suggesting that fibronectin and TGF-beta1 are regulated differently. Furthermore, luciferase activity of RMC cotransfected with fibronectin promoter reporter system and plasmid-expressing C3 exoenzyme (a specific inactivator of Rho family GTP binding proteins, pEFC3) was completely suppressed when compared with RMC cotransfected with empty vector, pEF. Because geranylgeranylation is usually involved in post-translational modification and membrane targeting of Rho family small GTP binding proteins, these data indicate that Rho family small GTP-binding proteins rather than Ras family small GTP binding proteins may play a key role in the TGF-beta1 and fibronectin expression in RMC.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 10997696 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Exp Gerontol. 1997 Jan-Apr;32(1-2):95-103.
Expression of endothelin, fibronectin, and mortalin as aging and mortality markers.
Kumazaki T, Wadhwa R, Kaul SC, Mitsui Y.
Department of Biochemistry and Biophysics, Hiroshima University, Japan.
Studies on fibronectin, endothelin-1, and mortalin from our laboratory are reviewed here. Fibronectin expression has been analyzed as upregulated during in vitro serial passaging of human fetal lung and neonatal foreskin fibroblasts as well as umbilical vein endothelial cells. In vivo aging of skin fibroblasts, as well as aortic endothelial cells, are also accompanied by upregulation of fibronectin expression. Fibronectin promoter binding proteins from young and old cell nuclear extracts were further explored by gel retardation assay. Preliminary analyses have detected age-related differential binding activities with respect to AP-1, CRES, TFIID, CTF, and AP-2 regions, whereas Sp1 binding proteins remain unaltered. Endothelin-1 expression is also seen as upregulated during in vitro and in vivo aging of endothelial cells. This can contribute to the hypertension commonly observed in elderly patients. Mortalin, a novel member of hsp 70 family of proteins, was initially identified by virtue of its association with a cellular mortal phenotype. Subsequently, normal cells and the ones with an immortal phenotype have been found to have differential subcellular localization of this protein. Antiproliferative activity of this protein in normal cells and the deregulation of expression in transformed cells is observed which suggests the association of mortalin in pathways that determine cellular divisional phenotype.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9088906 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Herz. 1995 Apr;20(2):118-26.
Fibronectin expression in the cardiovascular system.
Sabri A, Farhadian F, Contard F, Samuel JL, Rappaport L.
Unité 127 INSERM, IFR Circulation, Université D Diderot, Hôpital Lariboisiére, Paris, France.
Fibronectin (FN) is a dimeric glycoprotein found in the extracellular matrix (ECM) of most tissues and serves as a bridge between cells and the interstitial collagen meshwork. It also influences diverse processes including cell growth, adhesion, migration, and wound repair. Multiple FN forms arise by the alternative splicing of a primary transcript originating from a single gene. The spatial and temporal alterations in FN expression in the cardiovascular system have been studied in vitro in cell culture and in vivo during fetal development, hypertrophy, infarction, arterial injury and aging. This review describes characteristics of FN expression in cardiovascular system: 1. the FN phenotype is regulated during development. A high FN mRNA level is related to an early cardiac organogenesis and a progressive decrease that begins at the fetal stage and continues through senescence. During cardiac ontogeny, there is a linear correlation between total FN mRNA accumulation and the relative amounts of FN-EIIIA and EIIIB RNA. This correlation is absent during cardiac growth in the adult. 2. A differential reexpression of the FN isoforms is observed in both myocardium and aorta in different models of hypertension or infarction but with different threshold and time course. Changes in total FN mRNA levels in hypertensive models vary depending on the authors. Nevertheless the differences in the expression of the fetal forms of FN mRNA observed among the various models of hypertension-induced hypertrophy indicate that the process of FN pre-mRNA splicing in the adult myocardium is specifically regulated and depends on the pathological situations and the type of cell.(ABSTRACT TRUNCATED AT 250 WORDS)
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 7774863 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: J Mol Cell Cardiol. 1995 Apr;27(4):981-90.
Fibronectin expression during physiological and pathological cardiac growth.
Farhadian F, Contard F, Corbier A, Barrieux A, Rappaport L, Samuel JL.
Unité 127 INSERM, IFR Circulation, Université D Diderot Hopital Lariboisiére, Paris, France.
Fibronectin (FN) is a dimeric glycoprotein found in the extracellular matrix of most tissues that serves as a bridge between cells and the interstitial collagen meshwork and influences diverse processes including cell growth, adhesion, migration, and wound repair. Multiple FN forms arise by the alternative splicing of a primary transcript originating from a single gene. The spatial and temporal alterations in FN expression in the myocardium has been studied in models of cardiac growth in vivo such as fetal development, and hypertrophy secondary to pressure overload. This review focuses on the differential expression of FN isoforms that are observed in different models of cardiac growth. Using a combination of qualitative and quantitative analyses it is shown that in the rat myocardium: (1) the FN phenotype is developmentally regulated, (2) the re-expression of the fetal FN isoforms is observed in different models of cardiac hypertrophy secondary to a sudden or progressive hypertension and (3) the changes in cardiac FN expression affect mostly the coronary artery smooth muscle cells.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 7563110 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Am Rev Respir Dis. 1991 Sep;144(3 Pt 2):S25-8.
Glycoprotein synthesis and secretion. Expression of fibronectin and its cell surface receptors.
Dean DC, Birkenmeier TM, Rosen GD, Weintraub SJ.
Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
Fibronectin (FN) is an extracellular matrix protein that acts as a substrate for cell migration and adhesion during development. Cells adhere to FN through integral membrane proteins that are members of the integrin family of adhesion molecules. The interaction between cells and FN is important in a number of biologic processes, including gastrulation, hematopoietic differentiation, neural crest cell migration, cardiac development, branching morphogenesis in lung, wound healing, tumorigenesis, and metastasis. Expression of FN and its receptors is controlled by a number of hormones and growth factors as well as by tissue-specific factors. Here, the molecular aspects of how expression of these genes is controlled are reviewed, with particular emphasis on promoter regulator elements that modulate expression.
Publication Types:
Review
PMID: 1832529 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Cell Differ Dev. 1990 Dec 2;32(3):401-8.
Expression of tenascin and of the ED-B containing oncofetal fibronectin isoform in human cancer.
Nicolò G, Salvi S, Oliveri G, Borsi L, Castellani P, Zardi L.
Laboratory of Anatomic Pathology, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.
Tenascin (TN) and the oncofetal ED-B containing fibronectin isoform (B-FN) have been reported to be stromal markers of a number of malignancies. Here we report on studies of the distribution of TN and B-FN in normal adult tissues and in benign and malignant tumors, as well as on the levels of the B-FN mRNA in cultured fetal and non-fetal human fibroblasts originating from different tissues. B-FN has an extremely restricted distribution in normal adult tissues, is not expressed in benign tumors, but is greatly expressed in a high percentage of malignant tumors. On the contrary, human TN in normal adult tissues is less restricted than what has previously been reported and it is largely expressed in a number of both benign and malignant tumors. Moreover, we observed a great variability in the relative amount of B-FN mRNA among the 17 normal human fibroblast cell lines tested. We found very low levels in non-fetal skin fibroblasts and higher levels in fetal lung fibroblasts. We also found differences in the relative amounts of B-FN mRNA between fibroblast cell lines originating from the skin and the lung of the same subject.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Review
PMID: 1711919 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: J Invest Dermatol. 1990 Jun;94(6 Suppl):128S-134S.
Fibronectin matrix deposition and fibronectin receptor expression in healing and normal skin.
Clark RA.
Department of Dermatology and Medicine, University of Colorado School of Medicine, Denver.
During cutaneous tissue organization, numerous critical interactions occur between cells and the extracellular matrix (ECM). Cell-matrix interactions depend on the presence of ECM receptors. Many ECM receptors, known as integrins, are heterodimeric glycoproteins consisting of one alpha and one beta chain. Integrins containing beta 1 or beta 3 chains are ECM receptors, whereas those containing beta 2 chains are leukocyte cell-cell receptors. We have used porcine cutaneous wounds as a paradigm for tissue organization and probed healing wounds and adjacent normal skin with polyclonal antibodies to fibronectin and fibronectin (alpha 5 beta 1) receptor. During re-epithelialization, the epidermis transits over a provisional matrix containing fibronectin. Migrating epidermal cells expressed fibronectin receptors in a bright linear peripheral pattern. At 10 days, when reepithelialization was complete and the basement membrane was re-established, the fibronectin matrix was markedly reduced and fibronectin-receptor expression was limited to the basolateral aspect of basal cells, as observed in normal epidermis. Beneath the migrating epidermis in 5-d wounds, granulation tissue had filled 80% of the wound space. Day-5 wound fibroblasts did not express fibronectin nor other beta 1 integrin receptors, were randomly oriented, and contained no actin bundles. Fibronectin fibrils were assembled on the surfaces of day-5 wound fibroblasts but formed few linkages between cells. Day-7 wound fibroblasts expressed fibronectin receptors, contained peripheral cytoplasmic actin bundles consistent with a contractile fibroblast phenotype, and were coaligned across the wound in parallel array with interconnecting fibronectin fibrils. The wounds contracted between 7 and 10 days. Thus the migrating epidermis consistently expressed fibronectin receptors. Fibronectin receptors were expressed by fibroblasts just prior to wound contraction.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2161886 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Am J Respir Cell Mol Biol. 1989 Jul;1(1):5-10.
Expression of the fibronectin gene.
Dean DC.
Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.
Fibronectin (FN) is an extracellular matrix protein that acts as a substrate for cell migration and adhesion during development. FN adheres to cells through a dimeric membrane protein, the FN receptor. Antibodies to FN and synthetic peptides that inhibit FN-receptor interaction inhibit gastrulation, block neural crest cell migration, arrest cardiac development, and block the fusion of myoblasts to form myotubes. FN and its receptor also appear to be important for lung development, where their expression coincides with the onset of branching morphogenesis, but drops to barely detectable levels in adult lung, indicating developmental specificity. FN expression is generally low in most adult tissues. However, synthesis is drastically increased during injury and wound healing, a process that in many ways mimics development. FN synthesis is also drastically increased in fibroproliferative lung lesions associated with major architectural changes in the lung. Expression of FN is regulated by a variety of growth factors and hormones. Several of these inducers (cAMP, transforming growth factor-beta, epidermal growth factor, platelet-derived growth factor, glucocorticoids, and vitamin D3) have themselves been implicated in developmental processes, and both cAMP and transforming growth factor-beta are known to stimulate expression of other matrix genes. One role of these hormones and growth factors in development may be to control expression of matrix genes, thereby controlling cell migration and adhesion. In the following report, the effect of hormones and growth factors on expression of the FN gene is reviewed.
Publication Types:
Review
PMID: 2696510 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Nutr Rev. 1988 Apr;46(4):168-70.
Vitamin A controls fibronectin gene expression.
[No authors listed]
Publication Types:
Review
PMID: 3285252 [PubMed - indexed for MEDLINE]
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