LIVIVO - Search results -

Search results

Result 1 - 10 of total 11

Search options

Article ; Online: Editorial Expression of Concern: Class 3 semaphorins control vascular morphogenesis by inhibiting integrin function.

Serini, Guido / Valdembri, Donatella / Zanivan, Sara / Morterra, Giulia / Burkhardt, Constanze / Caccavari, Francesca / Zammataro, Luca / Primo, Luca / Tamagnone, Luca / Logan, Malcolm / Tessier-Lavigne, Marc / Taniguchi, Masahiko / Püschel, Andreas W / Bussolino, Federico

Nature

2024 Volume 627, Issue 8002, Page(s) E7

Language	English
Publishing date	2024-02-21
Publishing country	England
Document type	Expression of Concern
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-024-07195-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Angiogenesis: a balancing act between integrin activation and inhibition?

Bussolino, Federico / Caccavari, Francesca / Valdembri, Donatella / Serini, Guido

European cytokine network

2010 Volume 20, Issue 4, Page(s) 191–196

Abstract: Acquisition of new genes encoding for extracellular matrix (ECM) proteins and their cognate integrin adhesive receptors, as well as secreted pro- and anti-angiogenic factors, proved to be essential for the development of functional vascular networks in ... ...

Abstract	Acquisition of new genes encoding for extracellular matrix (ECM) proteins and their cognate integrin adhesive receptors, as well as secreted pro- and anti-angiogenic factors, proved to be essential for the development of functional vascular networks in the vertebrate embryo. There is now clear evidence that post-natal, pathological tissue neo-vascularization is crucial for cancer growth and therapy as well. Integrins are major ECM receptors that can exist in different functional states with respect to their affinity for ECM proteins. Regulation of integrin activation is crucial for their biological functions. In the embryo, the development of a properly patterned network of blood vessels relies upon the fine modulation of integrin activation by chemoattractant and chemorepulsive cues, such as angiogenic growth factors and semaphorins. Such a fine-tuning of endothelial integrin function is likely to be disrupted in cancer. Here, the vasculature is structurally and functionally abnormal and therefore inadequate for an efficient drug and oxygen delivery, which is a mandatory pre-requisite for successful chemotherapy and radiotherapy. It is thus important to identify the molecular mechanisms that regulate integrin function in normal ECs and which are altered in tumor ECs.
MeSH term(s)	Animals ; Blood Vessels/growth & development ; Blood Vessels/pathology ; Humans ; Integrins/antagonists & inhibitors ; Integrins/metabolism ; Monomeric GTP-Binding Proteins/metabolism ; Neovascularization, Pathologic/metabolism ; Protein Structure, Tertiary ; Tissue Adhesions
Chemical Substances	Integrins ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2010-01-25
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1118857-1
ISSN	1952-4005 ; 1148-5493
ISSN (online)	1952-4005
ISSN	1148-5493
DOI	10.1684/ecn.2009.0168
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3447: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Integrin signaling and lung cancer.

Caccavari, Francesca / Valdembri, Donatella / Sandri, Chiara / Bussolino, Federico / Serini, Guido

Cell adhesion & migration

2010 Volume 4, Issue 1, Page(s) 124–129

Abstract: The poor prognosis of most non small cell lung carcinomas is due to their ability to efficiently invade surrounding tissues and blood vessels, finally metastasizing to distant organs. Integrin mediated adhesive interaction with the surrounding ... ...

Abstract	The poor prognosis of most non small cell lung carcinomas is due to their ability to efficiently invade surrounding tissues and blood vessels, finally metastasizing to distant organs. Integrin mediated adhesive interaction with the surrounding extracellular matrix is a key limiting step in the regulation of the invasive properties of several cancer cell types. Here, we examine the rising evidences about the role that integrins can play in the physiopathology of non small cell lung carcinomas by regulating cell adhesion as well as the activation of growth factors and the traffic of their cognate receptors. Modulation of the signaling pathways controlled by integrins in lung cancer cells might offer the opportunity to design and develop new drugs that might be successfully combined with conventional chemotherapy and radiotherapy.
MeSH term(s)	Animals ; Humans ; Integrins/metabolism ; Lung Neoplasms/enzymology ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Models, Biological ; Neoplasm Invasiveness ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction
Chemical Substances	Integrins ; integrin-linked kinase (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2010-01-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2268518-2
ISSN	1933-6926 ; 1933-6918
ISSN (online)	1933-6926
ISSN	1933-6918
DOI	10.4161/cam.4.1.10976
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Semaphoring vascular morphogenesis.

Bussolino, Federico / Valdembri, Donatella / Caccavari, Francesca / Serini, Guido

Endothelium : journal of endothelial cell research

2006 Volume 13, Issue 2, Page(s) 81–91

Abstract: In vertebrate embryos, development of an architecturally optimized blood vessel network allows the efficient transport of oxygen and nutrients to all other tissues. The final shape of the vascular system results from vasculogenesis and angiogenesis, ... ...

Abstract	In vertebrate embryos, development of an architecturally optimized blood vessel network allows the efficient transport of oxygen and nutrients to all other tissues. The final shape of the vascular system results from vasculogenesis and angiogenesis, during which motile endothelial cells (ECs) modify their integrin-mediated interactions with the extracellular matrix (ECM) in response to pro- and anti-angiogenic factors. There is mounting evidence that different members of the semaphorin (SEMA) family of neural guidance cues participate in developmental and postnatal vessel formation and patterning as well. It turns out that paracrine secretion of class 3 SEMA (SEMA3) by nonendothelial tissues cooperates with vascular endothelial growth factor in regulating EC precursor migration and assembly during vasculogenesis and funnels navigating blood vessel through tissue boundaries during sprouting angiogenesis. Autocrine loops of endothelial SEMA3 instead appears to regulate vascular remodeling, which occurs through blood vessel intussusception and fusion. SEMA3 activity both on the vascular and nervous systems relies upon their ability to hamper the affinity of integrin receptors towards ECM ligands. Indeed, signaling from SEMA-activated plexin receptors negatively regulates cell-ECM adhesive interactions by inhibiting two key integrin activators, such as the small GTPase R-Ras and the focal adhesion protein talin.
MeSH term(s)	Animals ; Blood Vessels/anatomy & histology ; Blood Vessels/embryology ; Blood Vessels/growth & development ; Humans ; Morphogenesis/physiology ; Neovascularization, Physiologic/physiology ; Semaphorins/immunology ; Semaphorins/physiology
Chemical Substances	Semaphorins
Language	English
Publishing date	2006-05-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1230639-3
ISSN	1543-5261 ; 1062-3329
ISSN (online)	1543-5261
ISSN	1062-3329
DOI	10.1080/10623320600698003
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4840: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: The R-Ras/RIN2/Rab5 complex controls endothelial cell adhesion and morphogenesis via active integrin endocytosis and Rac signaling.

Sandri, Chiara / Caccavari, Francesca / Valdembri, Donatella / Camillo, Chiara / Veltel, Stefan / Santambrogio, Martina / Lanzetti, Letizia / Bussolino, Federico / Ivaska, Johanna / Serini, Guido

Cell research

2012 Volume 22, Issue 10, Page(s) 1479–1501

Abstract: During developmental and tumor angiogenesis, semaphorins regulate blood vessel navigation by signaling through plexin receptors that inhibit the R-Ras subfamily of small GTPases. R-Ras is mainly expressed in vascular cells, where it induces adhesion to ... ...

Abstract	During developmental and tumor angiogenesis, semaphorins regulate blood vessel navigation by signaling through plexin receptors that inhibit the R-Ras subfamily of small GTPases. R-Ras is mainly expressed in vascular cells, where it induces adhesion to the extracellular matrix (ECM) through unknown mechanisms. We identify the Ras and Rab5 interacting protein RIN2 as a key effector that in endothelial cells interacts with and mediates the pro-adhesive and -angiogenic activity of R-Ras. Both R-Ras-GTP and RIN2 localize at nascent ECM adhesion sites associated with lamellipodia. Upon binding, GTP-loaded R-Ras converts RIN2 from a Rab5 guanine nucleotide exchange factor (GEF) to an adaptor that first interacts at high affinity with Rab5-GTP to promote the selective endocytosis of ligand-bound/active β1 integrins and then causes the translocation of R-Ras to early endosomes. Here, the R-Ras/RIN2/Rab5 signaling module activates Rac1-dependent cell adhesion via TIAM1, a Rac GEF that localizes on early endosomes and is stimulated by the interaction with both Ras proteins and the vesicular lipid phosphatidylinositol 3-monophosphate. In conclusion, the ability of R-Ras-GTP to convert RIN2 from a GEF to an adaptor that preferentially binds Rab5-GTP allows the triggering of the endocytosis of ECM-bound/active β1 integrins and the ensuing funneling of R-Ras-GTP toward early endosomes to elicit the pro-adhesive and TIAM1-mediated activation of Rac1.
MeSH term(s)	Carrier Proteins/antagonists & inhibitors ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Adhesion ; Cells, Cultured ; Endocytosis ; Endosomes/metabolism ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Extracellular Matrix/metabolism ; Guanine Nucleotide Exchange Factors/antagonists & inhibitors ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; HeLa Cells ; Humans ; Integrin beta1/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Protein Binding ; RNA Interference ; RNA, Small Interfering/metabolism ; Signal Transduction ; T-Lymphoma Invasion and Metastasis-inducing Protein 1 ; rab5 GTP-Binding Proteins/metabolism ; rac GTP-Binding Proteins/metabolism ; ras Proteins/antagonists & inhibitors ; ras Proteins/genetics ; ras Proteins/metabolism
Chemical Substances	Carrier Proteins ; Guanine Nucleotide Exchange Factors ; Integrin beta1 ; Phosphatidylinositol Phosphates ; RIN2 protein, human ; RNA, Small Interfering ; T-Lymphoma Invasion and Metastasis-inducing Protein 1 ; TIAM1 protein, human ; phosphatidylinositol 3-phosphate ; RRAS protein, human (EC 3.6.1.-) ; rab5 GTP-Binding Proteins (EC 3.6.5.2) ; rac GTP-Binding Proteins (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2012-07-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1319303-x
ISSN	1748-7838 ; 1001-0602
ISSN (online)	1748-7838
ISSN	1001-0602
DOI	10.1038/cr.2012.110
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5283: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Hypothalamic-pituitary-adrenal axis responses to stress in subjects with 3,4-methylenedioxy-methamphetamine ('ecstasy') use history: correlation with dopamine receptor sensitivity.

Gerra, Gilberto / Bassignana, Sara / Zaimovic, Amir / Moi, Gabriele / Bussandri, Monica / Caccavari, Rocco / Brambilla, Francesca / Molina, Enzo

Psychiatry research

2003 Volume 120, Issue 2, Page(s) 115–124

Abstract: Fifteen 3,4-methylenedioxymethamphetamine (MDMA, 'ecstasy') users who did not have other drug dependencies or prolonged alcohol abuse and 15 control subjects were studied. All the subjects were exposed to the same psychosocial stressor (Stroop Color-Word ...

Abstract	Fifteen 3,4-methylenedioxymethamphetamine (MDMA, 'ecstasy') users who did not have other drug dependencies or prolonged alcohol abuse and 15 control subjects were studied. All the subjects were exposed to the same psychosocial stressor (Stroop Color-Word Interference Task, public speaking and mental arithmetic in front of an audience) 3 weeks after MDMA discontinuation. Plasma concentrations of adrenocorticotropic hormone (ACTH) and cortisol were measured immediately before the tests began and at their end, 30 min later. Growth hormone (GH) responses to the dopaminergic agonist bromocriptine and psychometric measures (Tridimensional Personality Questionnaire, Minnesota Multiphasic Personality Inventory, Buss-Durkee Hostility Inventory) were also obtained 4 weeks after MDMA discontinuation for the same subjects. ACTH and cortisol basal levels were significantly higher in ecstasy users than in control subjects. In contrast, ACTH and cortisol responses to stress were significantly blunted in MDMA users. The sensitivity of dopamine D2 receptors, reflected by GH responses to bromocriptine challenge, was reduced in MDMA users compared with controls. The responsiveness of the hypothalamic-pituitary-adrenal (HPA) axis (ACTH and cortisol delta peaks) correlated directly with GH areas under curves in response to bromocriptine, and inversely with psychometric measures of aggressiveness and novelty seeking. No correlation was found between hormonal measures and the extent of MDMA exposure. Reduced D2 receptor sensitivity, HPA basal hyperactivation and reduced responsiveness to stress may represent a complex neuroendocrine dysfunction associated with MDMA use. The present findings do not exclude the possibility that dopamine dysfunction partly predated MDMA exposure.
MeSH term(s)	Adrenocorticotropic Hormone/metabolism ; Adult ; Bromocriptine/pharmacology ; Cognition/physiology ; Diagnostic and Statistical Manual of Mental Disorders ; Hormone Antagonists/pharmacology ; Human Growth Hormone/metabolism ; Humans ; Hydrocortisone/metabolism ; Hypothalamo-Hypophyseal System/metabolism ; Male ; N-Methyl-3,4-methylenedioxyamphetamine ; Neuropsychological Tests ; Personality Inventory ; Pituitary-Adrenal System/metabolism ; Receptors, Dopamine/metabolism ; Stress, Psychological/metabolism ; Substance-Related Disorders/diagnosis ; Substance-Related Disorders/metabolism ; Substance-Related Disorders/psychology ; Surveys and Questionnaires
Chemical Substances	Hormone Antagonists ; Receptors, Dopamine ; Human Growth Hormone (12629-01-5) ; Bromocriptine (3A64E3G5ZO) ; Adrenocorticotropic Hormone (9002-60-2) ; N-Methyl-3,4-methylenedioxyamphetamine (KE1SEN21RM) ; Hydrocortisone (WI4X0X7BPJ)
Language	English
Publishing date	2003-08-28
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	445361-x
ISSN	1872-7123 ; 1872-7506 ; 0165-1781 ; 0925-4927
ISSN (online)	1872-7123 ; 1872-7506
ISSN	0165-1781 ; 0925-4927
DOI	10.1016/s0165-1781(03)00175-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1541: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Neuropilin-1/GIPC1 signaling regulates alpha5beta1 integrin traffic and function in endothelial cells.

Valdembri, Donatella / Caswell, Patrick T / Anderson, Kurt I / Schwarz, Juliane P / König, Ireen / Astanina, Elena / Caccavari, Francesca / Norman, Jim C / Humphries, Martin J / Bussolino, Federico / Serini, Guido

PLoS biology

2008 Volume 7, Issue 1, Page(s) e25

Abstract: Neuropilin 1 (Nrp1) is a coreceptor for vascular endothelial growth factor A165 (VEGF-A165, VEGF-A164 in mice) and semaphorin 3A (SEMA3A). Nevertheless, Nrp1 null embryos display vascular defects that differ from those of mice lacking either VEGF-A164 or ...

Abstract	Neuropilin 1 (Nrp1) is a coreceptor for vascular endothelial growth factor A165 (VEGF-A165, VEGF-A164 in mice) and semaphorin 3A (SEMA3A). Nevertheless, Nrp1 null embryos display vascular defects that differ from those of mice lacking either VEGF-A164 or Sema3A proteins. Furthermore, it has been recently reported that Nrp1 is required for endothelial cell (EC) response to both VEGF-A165 and VEGF-A121 isoforms, the latter being incapable of binding Nrp1 on the EC surface. Taken together, these data suggest that the vascular phenotype caused by the loss of Nrp1 could be due to a VEGF-A164/SEMA3A-independent function of Nrp1 in ECs, such as adhesion to the extracellular matrix. By using RNA interference and rescue with wild-type and mutant constructs, we show here that Nrp1 through its cytoplasmic SEA motif and independently of VEGF-A165 and SEMA3A specifically promotes alpha5beta1-integrin-mediated EC adhesion to fibronectin that is crucial for vascular development. We provide evidence that Nrp1, while not directly mediating cell spreading on fibronectin, interacts with alpha5beta1 at adhesion sites. Binding of the homomultimeric endocytic adaptor GAIP interacting protein C terminus, member 1 (GIPC1), to the SEA motif of Nrp1 selectively stimulates the internalization of active alpha5beta1 in Rab5-positive early endosomes. Accordingly, GIPC1, which also interacts with alpha5beta1, and the associated motor myosin VI (Myo6) support active alpha5beta1 endocytosis and EC adhesion to fibronectin. In conclusion, we propose that Nrp1, in addition to and independently of its role as coreceptor for VEGF-A165 and SEMA3A, stimulates through its cytoplasmic domain the spreading of ECs on fibronectin by increasing the Rab5/GIPC1/Myo6-dependent internalization of active alpha5beta1. Nrp1 modulation of alpha5beta1 integrin function can play a causal role in the generation of angiogenesis defects observed in Nrp1 null mice.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Animals ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Adhesion ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Fibronectins/genetics ; Fibronectins/metabolism ; Humans ; Integrin alpha5beta1/genetics ; Integrin alpha5beta1/metabolism ; Mice ; Mice, Knockout ; Neovascularization, Physiologic ; Neuropeptides/genetics ; Neuropeptides/metabolism ; Neuropilin-1/antagonists & inhibitors ; Neuropilin-1/genetics ; Neuropilin-1/metabolism ; Protein Binding ; RNA Interference ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Signal Transduction ; Umbilical Arteries/cytology ; Umbilical Arteries/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Fibronectins ; Gipc1 protein, mouse ; Integrin alpha5beta1 ; Neuropeptides ; RNA, Small Interfering ; Neuropilin-1 (144713-63-3)
Language	English
Publishing date	2008-10-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.1000025
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6193: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Temporal and spatial modulation of Rho GTPases during in vitro formation of capillary vascular network. Adherens junctions and myosin light chain as targets of Rac1 and RhoA.

Cascone, Ilaria / Giraudo, Enrico / Caccavari, Francesca / Napione, Lucia / Bertotti, Elisa / Collard, John G / Serini, Guido / Bussolino, Federico

The Journal of biological chemistry

2003 Volume 278, Issue 50, Page(s) 50702–50713

Abstract: Endothelial cells (ECs) self-organize into capillary networks when plated on extracellular matrix. In this process, Rho GTPases-mediated cytoskeletal dynamics control cell movement and organization of cell-to-matrix and cell-to-cell contacts. Time course ...

Abstract	Endothelial cells (ECs) self-organize into capillary networks when plated on extracellular matrix. In this process, Rho GTPases-mediated cytoskeletal dynamics control cell movement and organization of cell-to-matrix and cell-to-cell contacts. Time course analysis of RhoA and Rac1 activation matches specific morphological aspects of nascent pattern. RhoA-GTP increases early during EC adhesion and accumulates at sites of membrane ruffling. Rac1 is activated later and localizes in lamellipodia and at cell-to-cell contacts of organized cell chains. When ECs stretch and remodel to form capillary structures, RhoA-GTP increases again and associates with stress fibers running along the major cell axis. N17Rac1 and N19RhoA mutants impair pattern formation. Cell-to-cell contacts and myosin light chains (MLC) are targets of Rac1 and RhoA, respectively. N17Rac1 reduces the shift of beta-catenin and vascular endothelial cadherin to Triton X-100-insoluble fraction and impairs beta-catenin distribution at adherens junctions, suggesting that Rac1 controls the dynamics of cadherin-catenin complex with F-actin. During the remodeling phase of network formation, ECs show an intense staining for phosphorylated MLC along the plasma membrane; in contrast, MLC is less phosphorylated and widely diffused in N19RhoA ECs. Both N17Rac1 and N19RhoA have been used to investigate the role of wild type molecules in the main steps characterizing in vitro angiogenesis: (i) cell adhesion to the substrate, (ii) cell movement, and (iii) mechanical remodeling of matrix. N17Rac1 has a striking inhibitory effect on haptotaxis, whereas N19RhoA slightly inhibits EC adhesion and motility but more markedly Matrigel contraction. We conclude that different Rho GTPases control distinct morphogenetic aspects of vascular morphogenesis.
MeSH term(s)	Adherens Junctions/metabolism ; Cadherins/metabolism ; Capillaries/metabolism ; Cell Adhesion ; Cell Line ; Cell Movement ; Cells, Cultured ; Collagen/pharmacology ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Dermis/cytology ; Detergents/pharmacology ; Drug Combinations ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Formaldehyde/pharmacology ; Gene Expression Regulation, Enzymologic ; Genetic Vectors ; Glutathione Transferase/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Laminin/pharmacology ; Microscopy, Fluorescence ; Microscopy, Video ; Neovascularization, Pathologic ; Octoxynol/pharmacology ; Phosphorylation ; Polymers/pharmacology ; Proteoglycans/pharmacology ; Time Factors ; Trans-Activators/metabolism ; beta Catenin ; rac1 GTP-Binding Protein/metabolism ; rho GTP-Binding Proteins/biosynthesis ; rho GTP-Binding Proteins/chemistry ; rhoA GTP-Binding Protein/metabolism
Chemical Substances	CTNNB1 protein, human ; Cadherins ; Cytoskeletal Proteins ; Detergents ; Drug Combinations ; Laminin ; Polymers ; Proteoglycans ; Trans-Activators ; beta Catenin ; matrigel (119978-18-6) ; Formaldehyde (1HG84L3525) ; Guanosine Triphosphate (86-01-1) ; Octoxynol (9002-93-1) ; Collagen (9007-34-5) ; Glutathione Transferase (EC 2.5.1.18) ; rac1 GTP-Binding Protein (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2) ; rhoA GTP-Binding Protein (EC 3.6.5.2) ; paraform (Y19UC83H8E)
Language	English
Publishing date	2003-09-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M307234200
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Neuropilin-1/GIPC1 signaling regulates alpha5beta1 integrin traffic and function in endothelial cells.

Donatella Valdembri / Patrick T Caswell / Kurt I Anderson / Juliane P Schwarz / Ireen König / Elena Astanina / Francesca Caccavari / Jim C Norman / Martin J Humphries / Federico Bussolino / Guido Serini

PLoS Biology, Vol 7, Iss 1, p e

2009 Volume 25

Abstract	Neuropilin 1 (Nrp1) is a coreceptor for vascular endothelial growth factor A165 (VEGF-A165, VEGF-A164 in mice) and semaphorin 3A (SEMA3A). Nevertheless, Nrp1 null embryos display vascular defects that differ from those of mice lacking either VEGF-A164 or Sema3A proteins. Furthermore, it has been recently reported that Nrp1 is required for endothelial cell (EC) response to both VEGF-A165 and VEGF-A121 isoforms, the latter being incapable of binding Nrp1 on the EC surface. Taken together, these data suggest that the vascular phenotype caused by the loss of Nrp1 could be due to a VEGF-A164/SEMA3A-independent function of Nrp1 in ECs, such as adhesion to the extracellular matrix. By using RNA interference and rescue with wild-type and mutant constructs, we show here that Nrp1 through its cytoplasmic SEA motif and independently of VEGF-A165 and SEMA3A specifically promotes alpha5beta1-integrin-mediated EC adhesion to fibronectin that is crucial for vascular development. We provide evidence that Nrp1, while not directly mediating cell spreading on fibronectin, interacts with alpha5beta1 at adhesion sites. Binding of the homomultimeric endocytic adaptor GAIP interacting protein C terminus, member 1 (GIPC1), to the SEA motif of Nrp1 selectively stimulates the internalization of active alpha5beta1 in Rab5-positive early endosomes. Accordingly, GIPC1, which also interacts with alpha5beta1, and the associated motor myosin VI (Myo6) support active alpha5beta1 endocytosis and EC adhesion to fibronectin. In conclusion, we propose that Nrp1, in addition to and independently of its role as coreceptor for VEGF-A165 and SEMA3A, stimulates through its cytoplasmic domain the spreading of ECs on fibronectin by increasing the Rab5/GIPC1/Myo6-dependent internalization of active alpha5beta1. Nrp1 modulation of alpha5beta1 integrin function can play a causal role in the generation of angiogenesis defects observed in Nrp1 null mice.
Keywords	Biology (General) ; QH301-705.5
Subject code	571
Language	English
Publishing date	2009-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Class 3 semaphorins control vascular morphogenesis by inhibiting integrin function.

Nature

2005 Volume 424, Issue 6947, Page(s) 391–397

Abstract: The motility and morphogenesis of endothelial cells is controlled by spatio-temporally regulated activation of integrin adhesion receptors, and integrin activation is stimulated by major determinants of vascular remodelling. In order for endothelial ... ...

Abstract	The motility and morphogenesis of endothelial cells is controlled by spatio-temporally regulated activation of integrin adhesion receptors, and integrin activation is stimulated by major determinants of vascular remodelling. In order for endothelial cells to be responsive to changes in activator gradients, the adhesiveness of these cells to the extracellular matrix must be dynamic, and negative regulators of integrins could be required. Here we show that during vascular development and experimental angiogenesis, endothelial cells generate autocrine chemorepulsive signals of class 3 semaphorins (SEMA3 proteins) that localize at nascent adhesive sites in spreading endothelial cells. Disrupting endogenous SEMA3 function in endothelial cells stimulates integrin-mediated adhesion and migration to extracellular matrices, whereas exogenous SEMA3 proteins antagonize integrin activation. Misexpression of dominant negative SEMA3 receptors in chick embryo endothelial cells locks integrins in an active conformation, and severely impairs vascular remodelling. Sema3a null mice show vascular defects as well. Thus during angiogenesis endothelial SEMA3 proteins endow the vascular system with the plasticity required for its reshaping by controlling integrin function.
MeSH term(s)	Animals ; Autocrine Communication ; Cell Adhesion ; Cell Movement ; Chick Embryo ; Endothelium, Vascular/cytology ; Endothelium, Vascular/embryology ; Endothelium, Vascular/metabolism ; Extracellular Matrix/metabolism ; Gene Deletion ; Gene Expression Regulation ; Genes, Dominant ; Humans ; Integrins/antagonists & inhibitors ; Integrins/chemistry ; Integrins/metabolism ; Mice ; Mice, Knockout ; Morphogenesis ; Neovascularization, Physiologic ; Phenotype ; Semaphorin-3A/genetics ; Semaphorin-3A/metabolism
Chemical Substances	Integrins ; Semaphorin-3A
Language	English
Publishing date	2005-11-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature01784
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito