Quondamatteo, Fabio

[["dc.bibliographiccitation.artnumber","PII S0945-053X(03)00016-7"],["dc.bibliographiccitation.firstpage","93"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Matrix Biology"],["dc.bibliographiccitation.lastpage","96"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Reinhardt, D. P."],["dc.contributor.author","Charbonneau, N. L."],["dc.contributor.author","Pophal, G."],["dc.contributor.author","Sakai, L. Y."],["dc.contributor.author","Herken, R."],["dc.date.accessioned","2018-11-07T10:40:41Z"],["dc.date.available","2018-11-07T10:40:41Z"],["dc.date.issued","2003"],["dc.identifier.doi","10.1016/S0945-053X(03)00016-7"],["dc.identifier.isi","000182967400010"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46358"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0945-053X"],["dc.title","Fibrillin-1 and fibrillin-2 in human embryonic and early fetal development (vol 21, pg 637, 2002)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Glia"],["dc.contributor.author","Nico, B."],["dc.contributor.author","Corsi, P."],["dc.contributor.author","Frigeri, A."],["dc.contributor.author","Nicchia, G. P."],["dc.contributor.author","Mangieri, D."],["dc.contributor.author","Frontino, A."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Ribatti, D."],["dc.contributor.author","Svelto, M."],["dc.contributor.author","Roncali, L."],["dc.date.accessioned","2018-11-07T10:36:31Z"],["dc.date.available","2018-11-07T10:36:31Z"],["dc.date.issued","2003"],["dc.format.extent","29"],["dc.identifier.isi","000184938300123"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45347"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.publisher.place","New york"],["dc.relation.conference","6th European Meeting on Glial Cell Function in Health and Disease"],["dc.relation.eventlocation","BERLIN, GERMANY"],["dc.relation.issn","0894-1491"],["dc.title","Blood-brain barrier alterations in dystrophic mdx mice"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","215"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Developmental Dynamics"],["dc.bibliographiccitation.lastpage","221"],["dc.bibliographiccitation.volume","234"],["dc.contributor.author","Mueller, M."],["dc.contributor.author","Berger, Joachim"],["dc.contributor.author","Gersdorff, Nikolaus"],["dc.contributor.author","Cecconi, F."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.date.accessioned","2018-11-07T10:56:02Z"],["dc.date.available","2018-11-07T10:56:02Z"],["dc.date.issued","2005"],["dc.description.abstract","Apoptosis is an essential ubiquitous process that controls the duration of the life span of cells, thus playing a crucial role in morphogenetic, histogenetic, and phylogenetic developmental processes. Apaf1 (apoptosis protease activating factor 1) is one of the central mediators of the intrinsic apoptotic pathway and a part of the apoptosome, which activates procaspase-3 and promotes cell death. Gene knockout of Apaf1 in mice leads to late embryonic lethality with malformations such as the persistence of interdigital webs and hyperplasia of brain and retina. Therefore, Apaf1 is generally believed to play a crucial role in developmental apoptosis and have a widespread expression. However, its pattern of expression in early development remains unknown. To specify whether Apaf1 indeed plays this key role, we investigated the pattern of gene expression for Apaf1 in mouse embryos on day 7,9, and 12 of development. Our results show, that gene expression for Apafl first occurs within the embryo between day 7 and 9 of development, becoming more widespread toward day 12 and then includes structures, such as yolk sac, mesenchyme, cartilage, heart anlage, otic vesicle, peridermis, and anlagen of the spinal ganglia and vertebral bodies. Our results also show that gene expression for Apaf1 is not ubiquitous in early mouse development. This finding indicates that cell death processes are independent of or less dependent on Apaf1 during this time. Of interest, an active gene expression for Apafl is also present in organ anlagen such as heart or intestine, in which no obvious phenotype is seen after Apafl deletion. This finding suggests a possible role for Apafl in such anlagen as a putative alternative compensatory pathway, which could he switched on in the case of defects in the mediators that are normally involved in such organs. (c) 2005 Wiley-Liss, Inc."],["dc.description.sponsorship","Telethon [TCP99038]"],["dc.identifier.doi","10.1002/dvdy.20534"],["dc.identifier.isi","000231353700022"],["dc.identifier.pmid","16086359"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49920"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1058-8388"],["dc.title","Localization of Apafl1 gene expression in the early development of the mouse by means of in situ reverse transcriptase-polymerase chain reaction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","799"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","806"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Kempkensteffen, C."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Sonnenberg, Anton S. M."],["dc.contributor.author","Herken, R."],["dc.date.accessioned","2018-11-07T10:47:40Z"],["dc.date.available","2018-11-07T10:47:40Z"],["dc.date.issued","2004"],["dc.description.abstract","Normal liver sinusoids are not lined by a basement membrane (BM). In contrast, in the course of development of liver cirrhosis, a structured BM is formed de novo in the space of Disse. This BM contributes to the inhibition of the metabolic function of the liver but the pathogenic background of the formation of this perisinusoidal BM is still unclear. Integrins of the beta1-class are generally essential for BM stability and some of them (such as alpha2beta1, alpha3beta1 and alpha6beta1) appear de novo in the perisinusoidal space of the cirrhotic liver. Their cellular distribution in capillarized sinusoids as well as the correlation between their cellular distribution and the formation of the microvascular BM in the cirrhotic liver has not been shown at the ultrastructural level. In the present work we aimed to clarify this issue. We focused on integrins alpha3beta1 and alpha6beta1 and localised them ultrastructurally in human cirrhotic liver microvessels using postembedding immunogold which allows the ultrastructural localization of antigens with high resolution in the tissue. The newly formed basement membrane of capillarized sinusoids was visualized by means of fixation with addition of tannic acid, which enables the visualization of structures of the extracellular matrix with the highest resolution. Also, we carried out laminin detection using postembedding immunogold. Our results show that both alpha3beta1 and alpha6beta1 are expressed on the surface of both hepatocytes and endothelial cells, i.e. on both sides of the newly formed basement membrane. This latter shows zones of higher density both in close proximity to the endothelial and to the hepatocytic surfaces which resemble laminae densae. We propose that hepatocytes and endothelial cells may, therefore, by expressing such integrins, contribute to the formation of this pathological BM in the microvessels of the human cirrhotic liver. On stellate cells, which are major producers of BM components, both integrins alpha3beta1 and alpha6beta1 were also localized."],["dc.identifier.isi","000222112300018"],["dc.identifier.pmid","15168343"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48015"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","Ultrastructural localization of integrin subunits alpha 3 and alpha 6 in capillarized sinusoids of the human cirrhotic liver"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1199"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","HISTOLOGY AND HISTOPATHOLOGY"],["dc.bibliographiccitation.lastpage","1207"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Diedrich, A."],["dc.contributor.author","Bock, Hans-Christoph"],["dc.contributor.author","Koenig, Fatima Barbara"],["dc.contributor.author","Schulz, Thomas G."],["dc.contributor.author","Ludwig, H.-C."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.date.accessioned","2018-11-07T09:01:18Z"],["dc.date.available","2018-11-07T09:01:18Z"],["dc.date.issued","2006"],["dc.description.abstract","Glutathione S-transferases (GSTs) play a central role in a number of metabolic processes. Glutathione S-transferase T1 (GSTT1) is a polymorphic cytosolic enzyme and a member of the theta class of GSTs. Typical substrates for GSTT1 are industrial compounds, such as dichloromethane and ethylene oxide. It has been shown that also chemotherapeutic drugs such as BCNU [i.e. 1,3-bis(2-chloroethyl)-1nitrosourea] are efficiently inactivated by GSTT1. BCNU is a drug which is increasingly used locally in the chemotherapy of glioblastoma multiforme WHO grade IV. Therefore, if GSTT1 were expressed in neoplastic cells of brain tumours it could be a factor for chemoresistance. In order to clarify a possible role of GSTT1 in chemoresistance, as a first step, we localized this enzyme in malignant gliomas such as glioblastoma multiforme WHO grade IV and oligodendroglioma WHO grade II. Because of its polymorphism we first genotyped the samples for GSTT1 by PCR. Using in situ hybridization, we then demonstrated that GSTT1 transcripts are expressed in neoplastic cells of both tumour types. Immunohistochemistry revealed then that whereas neoplastic cells in glioblastoma multiforme WHO grade IV contain GSTT1, it was not localized in oligodendroglioma cells. Given the polymorphism of GSTT1 and its potential activity towards BCNU, the localization of GSTT1 in glioblastoma cells can be considered as a possible factor of non-homogeneous chemotherapy response among patients with different GSTT1 genotypes."],["dc.identifier.isi","000239239800008"],["dc.identifier.pmid","16874663"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24391"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","F Hernandez"],["dc.relation.issn","0213-3911"],["dc.title","Expression of glutathione S-transferase T1 (GSTT1) in human brain tumours"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1297"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","1307"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Nico, B."],["dc.contributor.author","Frigeri, A."],["dc.contributor.author","Nicchia, G. P."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Errede, M."],["dc.contributor.author","Ribatti, D."],["dc.contributor.author","Svelto, M."],["dc.contributor.author","Roncali, L."],["dc.date.accessioned","2018-11-07T09:12:56Z"],["dc.date.available","2018-11-07T09:12:56Z"],["dc.date.issued","2001"],["dc.description.abstract","In this study, we have investigated the expression of aquaporin 4 during blood-brain barrier development in the optic tectum of chick embryos and newly hatched chicks, by means of western-blot! reverse transcriptase-polymerase chain reaction, immunohistochemistry, and freeze-fracture and high-resolution immunogold electron microscopy In the optic tecta of day-14 embryos, western blot analysis revealed an approx, 30 kDa band, immunoreactive for aquaporin-4, which was increased in day-20 embryos and in chicks, Semi-quantitative reverse transcriptase chain reaction experiments showed that there was already a high level of aquaporin-4 mRNA in day-9 embryos as well as in the subsequent stages and in newly hatched chicks, Immunohistochemically, reactivity for aquaporin-4 was detected in the optic tectum of day-14 embryos; similar results were obtained in telencephalon and cerebellum, Ultrastructurally; the microvessels of the tectum showed immunoreactivity. for aquaporin-4 on the astroglial endfeet, which discontinuously surrounded endothelial cells joined hy immature tight junctions, In the tectum, telencephalon and cerebellum of 20-day embryos and chicks, aquaporin-4 strongly labeled the ependymal cells and the subpial glial membranes, as well as the bodies and processes of astroglial cells. A continuous aquaporin-4 staining was found around the microvessel endothelial cells, which were sealed off from one another by extensive tight junctions, A complete astrocytic sheath, labeled hg anti-aquaporin-4 gold particles, enveloped the endothelial-pericyte layer. Orthogonal arrays of particles were observed on fractured astrocytic membranes, starting from embryonic day 14 when the aquaporin-4 immunogold staining revealed clusters of gold particles, often forming square or rectangular clusters, The results showed that aquaporin-4 expression and organization of the intramembrane particles in orthogonal arrays followed the same temporal sequence, Finally, the lipopolysaccharide, a substance that induces blood-brain barrier distruption, determines a remarkable reduction in aquaporin-4 labeling, expressed by a few aquaporin-4 gold particles attached on swollen perivascular glial membranes, All these data show that aquaporin-4 expression occurs in the chick embryonic brain, in parallel with maturation and functioning of the blood-brain barrier and suggest that there is a close relationship between water transport regulation and brain development."],["dc.description.sponsorship","Telethon [983]"],["dc.identifier.isi","000168205200007"],["dc.identifier.pmid","11256996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27058"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.title","Role of aquaporin-4 water channel in the development and integrity of the blood-brain barrier"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","229"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Histochemistry and Cytochemistry"],["dc.bibliographiccitation.lastpage","237"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Klenczar, Christina"],["dc.contributor.author","Herken, Rainer"],["dc.date.accessioned","2018-08-20T09:46:59Z"],["dc.date.available","2018-08-20T09:46:59Z"],["dc.date.issued","2000"],["dc.description.abstract","Nidogen-1, a key component of basement membranes, is considered to function as a link between laminin and collagen Type IV networks and is expressed by mesenchymal cells during embryonic and fetal development. It is not clear which cells produce nidogen-1 in early developmental stages when no mesenchyme is present. We therefore localized nidogen-1 and its corresponding mRNA at the light and electron microscopic level in Day 7 mouse embryos during the onset of mesoderm formation by in situ hybridization, light microscopic immunostaining, and immunogold histochemistry. Nidogen-1 mRNA was found not only in the cells of the ectoderm-derived mesoderm but also in the cytoplasm of the endoderm and ectoderm, indicating that all three germ layers express it. Nidogen-1 was localized only in fully developed basement membranes of the ectoderm and was not seen in the developing endodermal basement membrane or in membranes disrupted during mesoderm formation. In contrast, laminin-1 and collagen Type IV were present in all basement membrane types at this developmental stage. The results indicate that, in the early embryo, nidogen-1 may be expressed by epithelial and mesenchymal cells, that both cell types contribute to embryonic basement membrane formation, and that nidogen-1 might serve to stabilize basement membranes in vivo. (J Histochem Cytochem 48:229-237, 2000)"],["dc.identifier.doi","10.1177/002215540004800208"],["dc.identifier.pmid","10639489"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15412"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","0022-1554"],["dc.title","Nidogen-1. Expression and ultrastructural localization during the onset of mesoderm formation in the early mouse embryo"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","593"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Histochemistry & Cytochemistry"],["dc.bibliographiccitation.lastpage","604"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Tornte, L. T."],["dc.contributor.author","Annatshah, Y."],["dc.contributor.author","Schlueter, N. K."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Herken, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.date.accessioned","2018-11-07T09:53:08Z"],["dc.date.available","2018-11-07T09:53:08Z"],["dc.date.issued","2006"],["dc.description.abstract","Nidogen-1 and -2 are key components of basement membranes (BMs). Despite the presence of nidogen molecules in the parenchyma of the developing liver, no BMs are formed therein. This suggests that, in the liver, nidogens may also have functions other than BM formation. As a first step toward the elucidation of the possible cell biological functions of nidogens in the developing liver, we aimed to study their cellular origin. We localized expression of nidogen-1 and nidogen-2 on prenatal days 12, 14, and 16 in the developing mouse liver using in situ hybridization at the light and electron microscopic level and light microscopic immunohistochemistry. Our results show that nidogens are produced both in portal anlagen and in the parenchyma during liver development. In the parenchyma, transcripts can be found in hepatocytes, precursors of stellate cells, endothelial cells and, most interestingly, hematopoietic cells. Using real-time PCR, we found that the gene expression for both proteins shows a decrease from day 14 to day 16 concomitant with a decrease in the hepatic hematopoiesis. We suggest that nidogens may, to some extent, take part in the regulation of hepatic hematopoiesis."],["dc.identifier.doi","10.1369/jhc.5A6810.2006"],["dc.identifier.isi","000237101200011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36269"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Histochemical Soc Inc"],["dc.relation.issn","0022-1554"],["dc.title","Hematopoietic cells are a source of nidogen-1 and nidogen-2 during mouse liver development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","G1075"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","AJP Gastrointestinal and Liver Physiology"],["dc.bibliographiccitation.lastpage","G1081"],["dc.bibliographiccitation.volume","290"],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Krick, W."],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Krüger, Marie Helen"],["dc.contributor.author","Neubauer-Saile, K."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Ramadori, Giuliano"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:50:06Z"],["dc.date.available","2018-11-07T09:50:06Z"],["dc.date.issued","2006"],["dc.description.abstract","Although the sulfate/anion transporter (sat-1; SLC26A1) was isolated from a rat liver cDNA library by expression cloning, localization of sat-1 within the liver and its contribution to the transport of sulfate and organo sulfates have remained unresolved. In situ hybridization and immunohistochemical studies were undertaken to demonstrate the localization of sat-1 in liver tissue. RT-PCR studies on isolated hepatocytes and liver endothelial and stellate cells in culture were performed to test for the presence of sat-1 in these cells. In sulfate uptake and efflux experiments, the substrate specificity of sat-1 was evaluated. Sat-1 mRNA was found in hepatocytes and endothelial cells. Sat-1 protein was localized in sinusoidal membranes and along the borders of hepatocytes. The canalicular region and bile capillaries were not stained. Sulfate uptake was only slightly affected by sulfamoyl diuretics or organo sulfates. Sulfate efflux from sat-1-expressing oocytes was enhanced in the presence of bicarbonate, indicating sulfate/bicarbonate exchange. Estrone sulfate was not transported by sat-1. Sat-1 may be responsible for the uptake of inorganic sulfate from the blood into hepatocytes to enable sulfation reactions. In hepatocytes and endothelial cells, sat-1 may also supply sulfate for proteoglycan synthesis."],["dc.identifier.doi","10.1152/ajpgi.00492.2005"],["dc.identifier.isi","000236663300027"],["dc.identifier.pmid","16357056"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35646"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0193-1857"],["dc.title","Localization of the sulfate/anion exchanger in the rat liver"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3990"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","4003"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Brakebusch, C."],["dc.contributor.author","Grose, R."],["dc.contributor.author","Quondamatteo, Fabio"],["dc.contributor.author","Ramirez, Alfredo"],["dc.contributor.author","Jorcano, J. L."],["dc.contributor.author","Pirro, A."],["dc.contributor.author","Svensson, M."],["dc.contributor.author","Herken, R."],["dc.contributor.author","Sasaki, T."],["dc.contributor.author","Timpl, R."],["dc.contributor.author","Werner, S."],["dc.contributor.author","Fassler, R."],["dc.date.accessioned","2018-11-07T10:35:10Z"],["dc.date.available","2018-11-07T10:35:10Z"],["dc.date.issued","2000"],["dc.description.abstract","beta 1 integrins are ubiquitously expressed receptors that mediate cell-cell and cell-extracellular matrix interactions. To analyze the function of beta 1 integrin in skin we generated mice with a keratinocyte-restricted deletion of the beta 1 integrin gene using the cre-loxP system. Mutant mice developed severe hair loss due to a reduced proliferation of hair matrix cells and severe hair follicle abnormalities. Eventually, the malformed hair follicles were removed by infiltrating macrophages. The epidermis of the back skin became hyperthickened, the basal keratinocytes showed reduced expression of alpha 6 beta 4 integrin, and the number of hemidesmosomes decreased. Basement membrane components were atypically deposited and, at least in the case of laminin-5, improperly processed, leading to disruption of the basement membrane and blister formation at the dermal-epidermal junction. In contrast, the integrity of the basement membrane surrounding the beta 1-deficient hair follicle was not affected. Finally, the dermis became fibrotic. These results demonstrate an important role of beta 1 integrins in hair follicle morphogenesis, in the processing of basement membrane components, in the maintenance of some, but not all basement membranes, in keratinocyte differentiation and proliferation, and in the formation and/or maintenance of hemidesmosomes."],["dc.identifier.doi","10.1093/emboj/19.15.3990"],["dc.identifier.isi","000088681800015"],["dc.identifier.pmid","10921880"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45029"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","EMBO Workshop on Functional Organization of the Cell Nucleus"],["dc.relation.eventlocation","PRAGUE, CZECH REPUBLIC"],["dc.relation.issn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Skin and hair follicle integrity is crucially dependent on beta 1 integrin expression on keratinocytes"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]