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Articoli di riviste sul tema "Membrane, Basement"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 20 febbraio 2023

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1

Murshed, Monzur, Neil Smyth, Nicolai Miosge, Jörg Karolat, Thomas Krieg, Mats Paulsson e Roswitha Nischt. "The Absence of Nidogen 1 Does Not Affect Murine Basement Membrane Formation". Molecular and Cellular Biology 20, n. 18 (15 settembre 2000): 7007–12. http://dx.doi.org/10.1128/mcb.20.18.7007-7012.2000.

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ABSTRACT Nidogen 1 is a highly conserved protein in mammals,Drosophila melanogaster, Caenorhabditis elegans, and ascidians and is found in all basement membranes. It has been proposed that nidogen 1 connects the laminin and collagen IV networks, so stabilizing the basement membrane, and integrates other proteins, including perlecan, into the basement membrane. To define the role of nidogen 1 in basement membranes in vivo, we produced a null mutation of the NID-1 gene in embryonic stem cells and used these to derive mouse lines. Homozygous animals produce neither nidogen 1 mRNA nor protein. Surprisingly, they show no overt abnormalities and are fertile, their basement membrane structures appearing normal. Nidogen 2 staining is increased in certain basement membranes, where it is normally only found in scant amounts. This occurs by either redistribution from other extracellular matrices or unmasking of nidogen 2 epitopes, as its production does not appear to be upregulated. The results show that nidogen 1 is not required for basement membrane formation or maintenance.

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2

Hagedorn, Elliott J., Joshua W. Ziel, Meghan A. Morrissey, Lara M. Linden, Zheng Wang, Qiuyi Chi, Sam A. Johnson e David R. Sherwood. "The netrin receptor DCC focuses invadopodia-driven basement membrane transmigration in vivo". Journal of Cell Biology 201, n. 6 (10 giugno 2013): 903–13. http://dx.doi.org/10.1083/jcb.201301091.

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Though critical to normal development and cancer metastasis, how cells traverse basement membranes is poorly understood. A central impediment has been the challenge of visualizing invasive cell interactions with basement membrane in vivo. By developing live-cell imaging methods to follow anchor cell (AC) invasion in Caenorhabditis elegans, we identify F-actin–based invadopodia that breach basement membrane. When an invadopodium penetrates basement membrane, it rapidly transitions into a stable invasive process that expands the breach and crosses into the vulval tissue. We find that the netrin receptor UNC-40 (DCC) specifically enriches at the site of basement membrane breach and that activation by UNC-6 (netrin) directs focused F-actin formation, generating the invasive protrusion and the cessation of invadopodia. Using optical highlighting of basement membrane components, we further demonstrate that rather than relying solely on proteolytic dissolution, the AC’s protrusion physically displaces basement membrane. These studies reveal an UNC-40–mediated morphogenetic transition at the cell–basement membrane interface that directs invading cells across basement membrane barriers.

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3

Nazari, Shayan S., Andrew D. Doyle e Kenneth M. Yamada. "Mechanisms of Basement Membrane Micro-Perforation during Cancer Cell Invasion into a 3D Collagen Gel". Gels 8, n. 9 (7 settembre 2022): 567. http://dx.doi.org/10.3390/gels8090567.

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Cancer invasion through basement membranes represents the initial step of tumor dissemination and metastasis. However, little is known about how human cancer cells breach basement membranes. Here, we used a three-dimensional in vitro invasion model consisting of cancer spheroids encapsulated by a basement membrane and embedded in 3D collagen gels to visualize the early events of cancer invasion by confocal microscopy and live-cell imaging. Human breast cancer cells generated large numbers of basement membrane perforations, or holes, of varying sizes that expanded over time during cell invasion. We used a wide variety of small molecule inhibitors to probe the mechanisms of basement membrane perforation and hole expansion. Protease inhibitor treatment (BB94), led to a 63% decrease in perforation size. After myosin II inhibition (blebbistatin), the basement membrane perforation area decreased by only 15%. These treatments produced correspondingly decreased cellular breaching events. Interestingly, inhibition of actin polymerization dramatically decreased basement membrane perforation by 80% and blocked invasion. Our findings suggest that human cancer cells can primarily use proteolysis and actin polymerization to perforate the BM and to expand perforations for basement membrane breaching with a relatively small contribution from myosin II contractility.

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4

LAURIE, G. W., e C. P. LEBLOND. "Basement membrane nomenclature". Nature 313, n. 6000 (gennaio 1985): 272. http://dx.doi.org/10.1038/313272b0.

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5

Weber, Manfred. "Basement membrane proteins". Kidney International 41, n. 3 (marzo 1992): 620–28. http://dx.doi.org/10.1038/ki.1992.95.

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6

Gunwar, Sripad, Fernando Ballester, Milton E. Noelken, Yoshikazu Sado, Yoshifumi Ninomiya e Billy G. Hudson. "Glomerular Basement Membrane". Journal of Biological Chemistry 273, n. 15 (10 aprile 1998): 8767–75. http://dx.doi.org/10.1074/jbc.273.15.8767.

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7

Ray, Marilyn C., e Leonard E. Gately. "Basement membrane zone". Clinics in Dermatology 14, n. 4 (luglio 1996): 321–30. http://dx.doi.org/10.1016/0738-081x(96)00061-2.

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8

Li, A. C. Y. "Basement membrane components". Journal of Clinical Pathology 56, n. 12 (1 dicembre 2003): 885–87. http://dx.doi.org/10.1136/jcp.56.12.885.

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9

Eady, Robin A. J. "The Basement Membrane". Archives of Dermatology 124, n. 5 (1 maggio 1988): 709. http://dx.doi.org/10.1001/archderm.1988.01670050053021.

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10

Bosman, Fred T., Jack Cleutjens, Cor Beek e Michael Havenith. "Basement membrane heterogeneity". Histochemical Journal 21, n. 11 (novembre 1989): 629–33. http://dx.doi.org/10.1007/bf01002481.

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11

Desjardins, M., e M. Bendayan. "Ontogenesis of glomerular basement membrane: structural and functional properties." Journal of Cell Biology 113, n. 3 (1 maggio 1991): 689–700. http://dx.doi.org/10.1083/jcb.113.3.689.

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Protein A-gold immunocytochemistry was applied in combination with morphometrical approaches to reveal the alpha 1(IV), alpha 2(IV), and alpha 3(IV) chains of type IV collagen as well as entactin on renal basement membranes, particularly on the glomerular one, during maturation. The results have indicated that a heterogeneity between renal basement membranes appears during the maturation process. In the glomerulus at the capillary loop stage, both the epithelial and endothelial cell basement membranes were labeled for the alpha 1(IV) and alpha 2(IV) chains of type IV collagen and entactin. After fusion, both proteins were present on the entire thickness of the typical glomerular basement membrane. At later stages, the labeling for alpha 1(IV) and alpha 2(IV) chains of type IV collagen decreased and drifted towards the endothelial side, whereas the labeling for the alpha 3(IV) chain increased and remained centrally located. Entactin remained on the entire thickness of the basement membrane during maturation and in adult stage. The distribution of endogenous serum albumin in the glomerular wall was studied during maturation, as a reference for the functional properties of the glomerular basement membrane. This distribution, dispersed through the entire thickness of the basement membrane at early stages, shifted towards the endothelial side of the lamina densa with maturation, demonstrating a progressive acquisition of the permselectivity. These results demonstrate that modifications in the content and organization of the different constituents of basement membranes occur with maturation and are required for the establishment of the filtration properties of the glomerular basement membrane.

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12

Nishi, S., M. Ueno, R. Karasawa, S. Kawashima, H. In, H. Hayashi, N. Saito et al. "Morphometric study of glomerular basement membrane and proximal tubular basement membrane in adult thin basement membrane disease". Clinical and Experimental Nephrology 3, n. 4 (20 dicembre 1999): 290–95. http://dx.doi.org/10.1007/s101570050049.

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13

Pastor-Pareja, José C. "Atypical basement membranes and basement membrane diversity – what is normal anyway?" Journal of Cell Science 133, n. 8 (15 aprile 2020): jcs241794. http://dx.doi.org/10.1242/jcs.241794.

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14

Bader, Bernhard L., Neil Smyth, Sabine Nedbal, Nicolai Miosge, Anke Baranowsky, Sharada Mokkapati, Monzur Murshed e Roswitha Nischt. "Compound Genetic Ablation of Nidogen 1 and 2 Causes Basement Membrane Defects and Perinatal Lethality in Mice". Molecular and Cellular Biology 25, n. 15 (1 agosto 2005): 6846–56. http://dx.doi.org/10.1128/mcb.25.15.6846-6856.2005.

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ABSTRACT Nidogen 1 and 2 are basement membrane glycoproteins, and previous biochemical and functional studies indicate that they may play a crucial role in basement membrane assembly. While they show a divergent expression pattern in certain adult tissues, both have a similar distribution during development. Gene knockout studies in mice demonstrated that the loss of either isoform has no effect on basement membrane formation and organ development, suggesting complementary functions. Here, we show that this is indeed the case. Deficiency of both nidogens in mice resulted in perinatal lethality. Nidogen 1 and 2 do not appear to be crucial in establishing tissue architecture during organ development; instead, they are essential for late stages of lung development and for maintenance and/or integrity of cardiac tissue. These organ defects are not compatible with postnatal survival. Ultrastructural analysis suggests that the phenotypes directly result from basement membrane changes. However, despite the ubiquitous presence of nidogens in basement membranes, defects do not occur in all tissues or in all basement membranes, suggesting a varying spectrum of roles for nidogens in the basement membrane.

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15

McCarthy, K. J., K. Bynum, P. L. St John, D. R. Abrahamson e J. R. Couchman. "Basement membrane proteoglycans in glomerular morphogenesis: chondroitin sulfate proteoglycan is temporally and spatially restricted during development." Journal of Histochemistry & Cytochemistry 41, n. 3 (marzo 1993): 401–14. http://dx.doi.org/10.1177/41.3.8429203.

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We previously reported the presence of a basement membrane-specific chondroitin sulfate proteoglycan (BM-CSPG) in basement membranes of almost all adult tissues. However, an exception to this ubiquitous distribution was found in the kidney, where BM-CSPG was absent from the glomerular capillary basement membrane (GBM) but present in other basement membranes of the nephron, including collecting ducts, tubules, Bowman's capsule, and the glomerular mesangium. In light of this unique pattern of distribution and of the complex histoarchitectural reorganization occurring during nephrogenesis, the present study used light and electron microscopic immunohistochemistry to examine the distribution of BM-CSPG and basement membrane heparan sulfate proteoglycan (BM-HSPG) during prenatal and postnatal renal development in the rat. Our results show that the temporal and spatial pattern of expression of BM-CSPG during nephrogenesis is unlike that reported for other basement membrane components such as laminin, fibronectin, and BM-HSPG, all of which can be found in the earliest formed basement membranes of the vesicle-stage nephron. Although BM-CSPG is present in the basement membranes of the invading vasculature and ureteric buds, its first appearance in nephron basement membrane occurs during the late comma stage. In capillary loop-stage glomeruli of prenatal animals, BM-CSPG is present in the presumptive mesangial matrix but undetectable in the GBM. However, as postnatal glomerular maturation progresses BM-CSPG is also found in both the lamina rara interna and lamina densa of the GBM in progressively increasing amounts, being most evident in the GBM of 21-day-old animals. Micrographs of glomeruli from 42-day-old animals show that BM-CSPG gradually disappears from the GBM and, by 56 days after birth, appears to be completely absent from the GBM, its pattern of distribution resembling that of the adult animal. Our results show that BM-CSPG is not required for the initial assembly of basement membranes but may in fact serve to stabilize basement membrane structure after histoarchitectural reorganization is completed.

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16

Ball, E. E., H. G. de Couet, P. L. Horn e J. M. Quinn. "Haemocytes secrete basement membrane components in embryonic locusts". Development 99, n. 2 (1 febbraio 1987): 255–59. http://dx.doi.org/10.1242/dev.99.2.255.

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Several monoclonal antibodies raised against a glycoprotein-enriched fraction of adult muscle membranes of Locusta migratoria selectively stain particles within haemocytes and basement membrane in developing locust embryos. Haemocytes containing immunoreactive particles are found associated with areas where basement membrane is being laid down. The underlying ectoderm does not show immunoreactivity. We conclude that haemocytes contribute to basement membrane formation in embryonic locusts.

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17

Boyd, RB, JP Burke, J. Atkin, VW Thompson e JF Nugent. "Significance of capillary basement membrane changes in diabetes mellitus". Journal of the American Podiatric Medical Association 80, n. 6 (1 giugno 1990): 307–13. http://dx.doi.org/10.7547/87507315-80-6-307.

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Diabetes mellitus is a disease in which the capillary basement membranes are substantially altered. This diabetic microangiopathy is characterized by a thickening of the basement membrane and changes in its permeability characteristic due to a disturbance in the production and distribution of its functional components. Glucose metabolism and insulin imbalance have been implicated in these basement membrane modifications. The authors describe normal capillary basement membrane architecture and then discuss how pathologic changes caused by diabetes mellitus are related to diabetic foot pathology.

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18

Schymeinsky, Jürgen, Sabine Nedbal, Nicolai Miosge, Ernst Pöschl, Cherie Rao, David R. Beier, William C. Skarnes, Rupert Timpl e Bernhard L. Bader. "Gene Structure and Functional Analysis of the Mouse Nidogen-2 Gene: Nidogen-2 Is Not Essential for Basement Membrane Formation in Mice". Molecular and Cellular Biology 22, n. 19 (1 ottobre 2002): 6820–30. http://dx.doi.org/10.1128/mcb.22.19.6820-6830.2002.

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ABSTRACT Nidogens are highly conserved proteins in vertebrates and invertebrates and are found in almost all basement membranes. According to the classical hypothesis of basement membrane organization, nidogens connect the laminin and collagen IV networks, so stabilizing the basement membrane, and integrate other proteins. In mammals two nidogen proteins, nidogen-1 and nidogen-2, have been discovered. Nidogen-2 is typically enriched in endothelial basement membranes, whereas nidogen-1 shows broader localization in most basement membranes. Surprisingly, analysis of nidogen-1 gene knockout mice presented evidence that nidogen-1 is not essential for basement membrane formation and may be compensated for by nidogen-2. In order to assess the structure and in vivo function of the nidogen-2 gene in mice, we cloned the gene and determined its structure and chromosomal location. Next we analyzed mice carrying an insertional mutation in the nidogen-2 gene that was generated by the secretory gene trap approach. Our molecular and biochemical characterization identified the mutation as a phenotypic null allele. Nidogen-2-deficient mice show no overt abnormalities and are fertile, and basement membranes appear normal by ultrastructural analysis and immunostaining. Nidogen-2 deficiency does not lead to hemorrhages in mice as one may have expected. Our results show that nidogen-2 is not essential for basement membrane formation or maintenance.

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19

Jung, Chi Young, Sun-Jae Lee, Min-Kyung Kim, Dong Jik Ahn e In Hee Lee. "Anti-glomerular basement membrane disease associated with thin basement membrane nephropathy". Medicine 100, n. 20 (21 maggio 2021): e26095. http://dx.doi.org/10.1097/md.0000000000026095.

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20

Nguyen, Nguyet M., Yushi Bai, Katsumi Mochitate e Robert M. Senior. "Laminin α-chain expression and basement membrane formation by MLE-15 respiratory epithelial cells". American Journal of Physiology-Lung Cellular and Molecular Physiology 282, n. 5 (1 maggio 2002): L1004—L1011. http://dx.doi.org/10.1152/ajplung.00379.2001.

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Basement membranes have a critical role in alveolar structure and function. Alveolar type II cells make basement membrane constituents, including laminin, but relatively little is known about the production of basement membrane proteins by murine alveolar type II cells and a convenient system is not available to study basement membrane production by murine alveolar type II cells. To facilitate study of basement membrane production, with particular focus on laminin chains, we examined transformed murine distal respiratory epithelial cells (MLE-15), which have many structural and biochemical features of alveolar type II cells. We found that MLE-15 cells produce laminin-α5, a trace amount of laminin-α3, laminins-β1 and -γ1, type IV collagen, and perlecan. Transforming growth factor-β1 significantly induces expression of laminin-α1. When grown on a fibroblast-embedded collagen gel, MLE-15 cells assemble a basement membrane-like layer containing laminin-α5. These findings indicate that MLE-15 cells will be useful in modeling basement membrane production and assembly by alveolar type II cells.

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21

Pusey, Charles, e Stephen McAdoo. "Antiglomerular Basement Membrane Disease". Seminars in Respiratory and Critical Care Medicine 39, n. 04 (agosto 2018): 494–503. http://dx.doi.org/10.1055/s-0038-1669413.

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AbstractAntiglomerular basement membrane (anti-GBM) disease is a rare but life-threatening autoimmune vasculitis that is characterized by the development of pathogenic autoantibodies to type IV collagen antigens expressed in the glomerular and alveolar basement membranes. Once deposited in tissue, these autoantibodies incite a local capillaritis which manifests as rapidly progressive glomerulonephritis (GN) in 80 to 90% of patients, and with concurrent alveolar hemorrhage in ∼50%. A small proportion of cases may present with pulmonary disease in isolation. Serological testing for anti-GBM antibodies may facilitate rapid diagnosis, though renal biopsy is often required to confirm the presence of necrotizing or crescentic GN and linear deposition of autoantibody on the glomerular basement membrane. Alveolar hemorrhage may be evident clinically, or detected on imaging, pulmonary function testing, or bronchoscopy. Prompt treatment with plasmapheresis, cyclophosphamide, and steroids is usually indicated to remove pathogenic autoantibodies, to prevent their ongoing production, and to ameliorate end-organ inflammation. Alveolar hemorrhage is usually responsive to this treatment, and long-term respiratory sequelae are uncommon. Renal prognosis is more variable, though with aggressive treatment, independent renal function is maintained at 1 year in more than 80% of patients not requiring renal replacement therapy at presentation. Relapse in uncommon in anti-GBM disease, unless there is a concomitant antineutrophil cytoplasm antibody (present in 30–40%), in which case maintenance immunosuppression is recommended.

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22

Borycki, Anne-Gaëlle. "The myotomal basement membrane". Cell Adhesion & Migration 7, n. 1 (gennaio 2013): 72–81. http://dx.doi.org/10.4161/cam.23411.

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23

Tryggvason, Karl, e Jaakko Patrakka. "Thin Basement Membrane Nephropathy". Journal of the American Society of Nephrology 17, n. 3 (8 febbraio 2006): 813–22. http://dx.doi.org/10.1681/asn.2005070737.

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24

Kearney, Phillip A. "Epithelial basement membrane dystrophy". Clinical and Experimental Optometry 78, n. 6 (novembre 1995): 221–22. http://dx.doi.org/10.1111/j.1444-0938.1995.tb00827.x.

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25

Miner, Jeffrey H. "Renal basement membrane components". Kidney International 56, n. 6 (dicembre 1999): 2016–24. http://dx.doi.org/10.1046/j.1523-1755.1999.00785.x.

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26

Yao, Yao. "Basement membrane and stroke". Journal of Cerebral Blood Flow & Metabolism 39, n. 1 (18 settembre 2018): 3–19. http://dx.doi.org/10.1177/0271678x18801467.

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Located at the interface of the circulation system and the CNS, the basement membrane (BM) is well positioned to regulate blood–brain barrier (BBB) integrity. Given the important roles of BBB in the development and progression of various neurological disorders, the BM has been hypothesized to contribute to the pathogenesis of these diseases. After stroke, a cerebrovascular disease caused by rupture (hemorrhagic) or occlusion (ischemic) of cerebral blood vessels, the BM undergoes constant remodeling to modulate disease progression. Although an association between BM dissolution and stroke is observed, how each individual BM component changes after stroke and how these components contribute to stroke pathogenesis are mostly unclear. In this review, I first briefly introduce the composition of the BM in the brain. Next, the functions of the BM and its major components in BBB maintenance under homeostatic conditions are summarized. Furthermore, the roles of the BM and its major components in the pathogenesis of hemorrhagic and ischemic stroke are discussed. Last, unsolved questions and potential future directions are described. This review aims to provide a comprehensive reference for future studies, stimulate the formation of new ideas, and promote the generation of new genetic tools in the field of BM/stroke research.

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27

Thompson, C. H., e S. Kalowski. "Anti-Glomerular Basement Membrane". Nephron 58, n. 2 (1991): 238–39. http://dx.doi.org/10.1159/000186424.

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28

Kahsai, Tesfamichael Z., George C. Enders, Sripad Gunwar, Charlott Brunmark, Jörgen Wieslander, Raghuram Kalluri, Jing Zhou, Milton E. Noelken e Billy G. Hudson. "Seminiferous Tubule Basement Membrane". Journal of Biological Chemistry 272, n. 27 (4 luglio 1997): 17023–32. http://dx.doi.org/10.1074/jbc.272.27.17023.

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29

Labbé, Antoine, Raphaël De Nicola, Bénédicte Dupas, François Auclin e Christophe Baudouin. "Epithelial Basement Membrane Dystrophy". Ophthalmology 113, n. 8 (agosto 2006): 1301–8. http://dx.doi.org/10.1016/j.ophtha.2006.03.050.

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Miner, Jeffrey H. "The glomerular basement membrane". Experimental Cell Research 318, n. 9 (maggio 2012): 973–78. http://dx.doi.org/10.1016/j.yexcr.2012.02.031.

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KLEINMAN, HYNDA K., GORDON W. LAURIE, JOHN R. HASSELL, FRANCES B. CANNON e VICKI L. STAR. "Basement Membrane Supramolecular Complexes". Annals of the New York Academy of Sciences 460, n. 1 Biology, Chem (dicembre 1985): 463–65. http://dx.doi.org/10.1111/j.1749-6632.1985.tb51210.x.

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32

Savige, Judy, Kesha Rana, Stephen Tonna, Mark Buzza, Hayat Dagher e Yan Yan Wang. "Thin basement membrane nephropathy". Kidney International 64, n. 4 (ottobre 2003): 1169–78. http://dx.doi.org/10.1046/j.1523-1755.2003.00234.x.

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Yurchenco, Peter D. "Macromolecular organization of basement membrane laminin". Proceedings, annual meeting, Electron Microscopy Society of America 49 (agosto 1991): 176–77. http://dx.doi.org/10.1017/s0424820100085186.

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Laminin isoforms are major structural and cell-interacting components of basement membranes. The most extensively studied isoform of this glycoprotein (800 kDa) is murine EHS laminin which consists of three polypeptide chains (A,B1,B2) disulfide linked to form a flexible four-armed molecule which in turn is often complexed to entactin, a smaller dumbell-shaped sulfated glycoprotein. One of the functions proposed for laminin is selfassembly into a polymer that constitutes a major part of basement membrane architecture. The principal evidence for this hypothesis has derived from biochemical and structural studies of laminin polymerization in vitro. Embryonal carcinoma cells (M1536B3) grown in suspension culture will differentiate into multicellular spherules that produce basement membrane cores rich in laminin/entactin but devoid of type IV collagen, a characteristic of some basement membranes of developing tissues. We now report that these cores share the same structural/biochemical features with reconstituted laminin polymers.

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34

Crary, Gretchen S., Avi Katz, Alfred J. Fish, Alfred F. Michael e Ralph J. Butkowski. "Role of a basement membrane glycoprotein in anti-tubular basement membrane nephritis". Kidney International 43, n. 1 (gennaio 1993): 140–46. http://dx.doi.org/10.1038/ki.1993.23.

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35

Singhal, Pooja, Kevin Yi Mi Ren, Bryan M. Curtis, Ian MacPherson e Carmen Avila-Casado. "Atypical Noncrescentic Antiglomerular Basement Membrane Disease With Concurrent Thin Basement Membrane Nephropathy". Kidney International Reports 3, n. 4 (luglio 2018): 991–96. http://dx.doi.org/10.1016/j.ekir.2018.03.012.

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36

Miosge, Nicolai, Fabio Quondamatteo, Christina Klenczar e Rainer Herken. "Nidogen-1: Expression and Ultrastructural Localization During the Onset of Mesoderm Formation in the Early Mouse Embryo". Journal of Histochemistry & Cytochemistry 48, n. 2 (febbraio 2000): 229–37. http://dx.doi.org/10.1177/002215540004800208.

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Abstract (sommario):

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.

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Abrahamson, D. R. "Origin of the glomerular basement membrane visualized after in vivo labeling of laminin in newborn rat kidneys." Journal of Cell Biology 100, n. 6 (1 giugno 1985): 1988–2000. http://dx.doi.org/10.1083/jcb.100.6.1988.

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To examine the origin and assembly of glomerular basement membranes (GBMs), affinity purified anti-laminin IgG was directly coupled to horseradish peroxidase (HRP) and intravenously injected into newborn rats. Kidneys were then processed for peroxidase histochemistry and microscopy. Within 1 h after injection, anti-laminin bound to basement membranes of nephrons in all developmental stages (vesicle, comma, S-shaped, developing capillary loop, and maturing glomeruli). In S-shaped and capillary loop glomeruli, anti-laminin-HRP labeled a double basal lamina between the endothelium and epithelium. Sections incubated with anti-laminin in vitro showed labeling within the rough endoplasmic reticulum of endothelium and epithelium, indicating that both cell types synthesized laminin for the double basement membrane. In maturing glomeruli, injected anti-laminin-HRP bound throughout the GBMs, and double basement membranes were rarely observed. At this stage, however, numerous knobs or outpockets of basement membrane material extending far into the epithelial side of the capillary wall were identified and these were also labeled throughout their full thickness. No such outpockets were found in the endothelial cell layer of newborn rats (and they normally are completely absent in fully mature, adult glomeruli). In contrast with these results, in kidneys fixed 4-6 d after anti-laminin IgG-HRP injection, basement membranes of vesicle, comma, and S-shaped nephrons were unlabeled, indicating that they were assembled after injection. GBM labeling was seen in maturing glomeruli, however. In addition, the outpockets of basement membrane extending into the epithelium were often completely unlabeled whereas GBMs lying immediately beneath them were labeled intensely, which indicates that the outpockets were probably assembled by the epithelium. Injections of sheep anti-laminin IgG followed 8 d later with injections of biotin-rabbit anti-laminin IgG and double-label immunofluorescence microscopy confirmed that GBM formation continued during individual capillary loop expansion. GBM assembly therefore occurs by at least two different processes at separate times in development: (a) fusion of endothelial and epithelial basement membranes followed by (b) addition of new basement membrane from the epithelium into existing GBMs.

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38

Basset-Seguin, N., M. Dersookian, K. Cehrs e K. B. Yancey. "C3d,g is present in normal human epidermal basement membrane." Journal of Immunology 141, n. 4 (15 agosto 1988): 1273–80. http://dx.doi.org/10.4049/jimmunol.141.4.1273.

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Abstract mAb as well as polyclonal anti-human C3d antibodies were found to specifically bind to the epidermal basement membrane zone of normal human adult and neonatal skin in a linear continuous pattern on direct immunofluorescence microscopy. No such binding was found in dermal microvascular basement membranes. Studies of normal adult human skin using a rat mAb specific for C3g revealed the same pattern of epidermal basement membrane staining. Control polyclonal antibodies directed against C3, C3c, C5, IgG, IgA, or IgM showed no evidence of epidermal basement membrane binding or in situ deposits of immune complexes in samples of normal human skin that were all positive for C3d and C3g. Pre-adsorption of monoclonal or polyclonal anti-human C3d with purified human C3d completely blocked these reagents' epidermal basement membrane reactivity. Anti-human C3d epidermal basement membrane binding was not diminished by pre-treatment of substrate with antibodies directed against C3, C3c, C5, laminin, fibronectin, or type IV collagen as well as bullous pemphigoid, KF-1, or epidermolysis bullosa acquisita Ag. Direct immunofluorescence microscopy studies on 1 M NaCl split human skin showed that C3d and C3g were found in the base of the cleavage plane created within the lamina lucida. By immunoelectron microscopy, C3d was found along the base of the lamina densa and in the sublamina densa region of normal human epidermal basement membrane. Although anti-human C3d epidermal basement membrane binding was not altered by treatment of 6 micron skin sections with buffers of varying pH and ionic concentration, binding was abolished by treating dermal portions of salt split skin with 0.1 M dithiothreitol in 8 M urea. Studies of a patient with congenital C3 deficiency revealed that there was no binding of anti-human C3d or anti-human C3g to this subject's epidermal basement membrane. Moreover, treatment of this patient's skin with aged human serum containing C3d,g or purified human C3 did not restore epidermal basement membrane anti-human C3d binding. These studies demonstrate that C3d,g or a closely related C3 fragment is present in the epidermal basement membrane zone of normal human skin.

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39

EBIHARA, Isao, e Hikaru KOIDE. "Structure and function of glomerular basement membrane." membrane 14, n. 1 (1989): 2–10. http://dx.doi.org/10.5360/membrane.14.2.

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40

Schaumburg-Lever, G., I. Lever, B. Fehrenbacher, H. Möller, B. Bischof e A. Blum. "Melanocytes in Nevi and melanomas synthesize basement membrane and basement membrane-like material". Journal of Dermatological Science 16 (marzo 1998): S105. http://dx.doi.org/10.1016/s0923-1811(98)83624-4.

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41

Bonsib, Stephen M. "The macula densa tubular basement membrane: A unique plaque of basement membrane specialization". Journal of Ultrastructure and Molecular Structure Research 97, n. 1-3 (ottobre 1986): 103–8. http://dx.doi.org/10.1016/s0889-1605(86)80010-6.

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42

Trzebiatowska, Agnieszka, Ulrike Topf, Ursula Sauder, Krzysztof Drabikowski e Ruth Chiquet-Ehrismann. "Caenorhabditis elegans Teneurin, ten-1, Is Required for Gonadal and Pharyngeal Basement Membrane Integrity and Acts Redundantly with Integrin ina-1 and Dystroglycan dgn-1". Molecular Biology of the Cell 19, n. 9 (settembre 2008): 3898–908. http://dx.doi.org/10.1091/mbc.e08-01-0028.

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Abstract (sommario):

The Caenorhabditis elegans teneurin ortholog, ten-1, plays an important role in gonad and pharynx development. We found that lack of TEN-1 does not affect germline proliferation but leads to local basement membrane deficiency and early gonad disruption. Teneurin is expressed in the somatic precursor cells of the gonad that appear to be crucial for gonad epithelialization and basement membrane integrity. Ten-1 null mutants also arrest as L1 larvae with malformed pharynges and disorganized pharyngeal basement membranes. The pleiotropic phenotype of ten-1 mutant worms is similar to defects found in basement membrane receptor mutants ina-1 and dgn-1 as well as in the mutants of the extracellular matrix component laminin, epi-1. We show that the ten-1 mutation is synthetic lethal with mutations of genes encoding basement membrane components and receptors due to pharyngeal or hypodermal defects. This indicates that TEN-1 could act redundantly with integrin INA-1, dystroglycan DGN-1, and laminin EPI-1 in C. elegans development. Moreover, ten-1 deletion sensitizes worms to loss of nidogen nid-1 causing a pharynx unattached phenotype in ten-1;nid-1 double mutants. We conclude that TEN-1 is important for basement membrane maintenance and/or adhesion in particular organs and affects the function of somatic gonad precursor cells.

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43

Stratman, Amber N., e George E. Davis. "Endothelial Cell-Pericyte Interactions Stimulate Basement Membrane Matrix Assembly: Influence on Vascular Tube Remodeling, Maturation, and Stabilization". Microscopy and Microanalysis 18, n. 1 (14 dicembre 2011): 68–80. http://dx.doi.org/10.1017/s1431927611012402.

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AbstractExtracellular matrix synthesis and deposition surrounding the developing vasculature are critical for vessel remodeling and maturation events. Although the basement membrane is an integral structure underlying endothelial cells (ECs), few studies, until recently, have been performed to understand its formation in this context. In this review article, we highlight new data demonstrating a corequirement for ECs and pericytes to properly deposit and assemble vascular basement membranes during morphogenic events. In EC only cultures or under conditions whereby pericyte recruitment is blocked, there is a lack of basement membrane assembly, decreased vessel stability (with increased susceptibility to pro-regressive stimuli), and increased EC tube widths (a marker of dysfunctional EC-pericyte interactions). ECs and pericytes both contribute basement membrane components and, furthermore, both cells induce the expression of particular components as well as integrins that recognize them. The EC-derived factors—platelet derived growth factor-BB and heparin binding-epidermal growth factor—are both critical for pericyte recruitment to EC tubes and concomitant vascular basement membrane formationin vitroandin vivo. Thus, heterotypic EC-pericyte interactions play a fundamental role in vascular basement membrane matrix deposition, a critical tube maturation event that is altered in key disease states such as diabetes and cancer.

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44

Couchman, J. R. "Heterogeneous distribution of a basement membrane heparan sulfate proteoglycan in rat tissues." Journal of Cell Biology 105, n. 4 (1 ottobre 1987): 1901–16. http://dx.doi.org/10.1083/jcb.105.4.1901.

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A heparan sulfate proteoglycan (HSPG) synthesized by murine parietal yolk sac (PYS-2) cells has been characterized and purified from culture supernatants. A monospecific polyclonal antiserum was raised against it which showed activity against the HSPG core protein and basement membrane specificity in immunohistochemical studies on frozen tissue sections from many rat organs. However, there was no reactivity with some basement membranes, notably those of several smooth muscle types and cardiac muscle. In addition, it was found that pancreatic acinar basement membranes also lacked the HSPG type recognized by this antiserum. Those basement membranes that lacked the HSPG strongly stained with antisera against laminin and type IV collagen. The striking distribution pattern is possibly indicative of multiple species of basement membrane HSPGs of which one type is recognized by this antiserum. Further evidence for multiple HSPGs was derived from the finding that skeletal neuromuscular junction and liver epithelia also did not contain this type of HSPG, though previous reports have indicated the presence of HSPGs at these sites. The PYS-2 HSPG was shown to be antigenically related to the large, low buoyant density HSPG from the murine Engelbreth-Holm swarm tumor. It was, however, confirmed that only a single population of antibodies was present in the serum. Despite the presence of similar epitopes on these two proteoglycans of different hydrodynamic properties, it was apparent that the PYS-2 HSPG represents a basement membrane proteoglycan of distinct properties reflected in its restricted distribution in vivo.

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45

Grant, D. S., e C. P. Leblond. "Immunogold quantitation of laminin, type IV collagen, and heparan sulfate proteoglycan in a variety of basement membranes." Journal of Histochemistry & Cytochemistry 36, n. 3 (marzo 1988): 271–83. http://dx.doi.org/10.1177/36.3.2963856.

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Abstract (sommario):

A series of basement membranes was immunolabeled for laminin, type IV collagen, and heparan sulfate proteoglycan in the hope of comparing the content of these substances. The basement membranes, including thin ones (less than 0.3 micron) from kidney, colon, enamel organ, and vas deferens, and thick ones (greater than 2 micron), i.e., Reichert's membrane, Descemet's membrane, and EHS tumor matrix, were fixed in formaldehyde, embedded in Lowicryl, and treated with specific antisera or antibodies followed by anti-rabbit immunoglobulin bound to gold. The density of gold particles, expressed per micron2, was negligible in controls (less than or equal to 1.1), but averaged 307, 146, and 23, respectively, for laminin, collagen IV, and proteoglycan over the thick basement membranes (except for Descemet's membranes, over which the density was 16, 5, and 34, respectively) and 117, 72, and 64, respectively, over the lamina densa of the thin basement membranes. Lower but significant reactions were observed over the lamina lucida. Interpretation of the gold particle densities was based on (a) the similarity between the ultrastructure of most thick basement membranes and of the lamina densa of most thin basement membranes, and (b) the biochemical content of the three substances under study in the EHS tumor matrix (Eur J Biochem 143:145, 1984). It was proposed that thick basement membranes (except Descemet's) contained more laminin and collagen IV but less heparan sulfate proteoglycan than the lamina densa of thin basement membranes. In the latter, there was a fair variation from tissue to tissue, but a tendency towards a similar molar content of the three substances.

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46

Uobe, K., S. Wada, M. Wato, T. Nishikawa, A. Tanaka, K. Nishida e M. Tsutsui. "Monoclonal Antibodies Against Gingival Components". Advances in Dental Research 2, n. 2 (novembre 1988): 240–44. http://dx.doi.org/10.1177/08959374880020020801.

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The aim of this study was to produce and characterize monoclonal antibodies against human gingival epithelial cells and gingival fibroblasts. By using these whole cells as immunogens, we were able to generate a large number of monoclonal antibodies reacting with tissue antigens, in particular antibodies that reacted with desmosomes (MoAbs 7 and 8) and basement membrane (MoAb FB-1) antigens. MoAbs 7 and 8 produced from epithelial cells stained cell membranes of epithelium and desmosomes, respectively, as shown by light and immunoelectron microscopy. The epitopes to which MoAbs 7 and 8 were reactive were stable against various treatments; only periodate oxidation abolished the tissue reactions with MoAb 8. Extraction of gingiva with SDS or NP-40, SDS-PAGE analysis, and Western blotting showed that the MoAb 8 identified an antigen with a molecular weight of 100,000 daltons. MoAb FB-1 produced from fibroblasts immunolabeled the basement membranes. The FB-1 antigen was clearly different from any of the known ubiquitous basement membrane components, such as type IV collagen, laminin, and fibronectin. Examination of the distribution and localization of the antigen showed that it was present in the basement membrane beneath stratified squamous epithelium. FB-1 did not react with any of types I-VI collagens in ELISA, but immunoelectron microscopy showed that the antigen reacting with FB-1 was present in the lamina fibroreticularis of the basement membrane and was comprised of collagen-like fibers. These results suggest the possible existence of a new collagen other than types I-VI in the basement membrane beneath stratified squamous epithelium.

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47

Ueda, Hideho, Takashi Gohdo e Shinichi Ohno. "β-Dystroglycan Localization in the Photoreceptor and Müller cells in the Rat Retina Revealed by Immunoelectron Microscopy". Journal of Histochemistry & Cytochemistry 46, n. 2 (febbraio 1998): 185–91. http://dx.doi.org/10.1177/002215549804600207.

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β-Dystroglycan (β-DG) is a dystrophin-associated glycoprotein that is expressed in skeletal muscle and other tissues. In the retina, dystrophin is present in the outer plexiform layer (OPL), where it is enriched under the photoreceptor cell membrane. In this study we determined the immunocytochemical localization of β-DG at both light and electron microscopic levels. β-DG immunoreactivity was detected at the inner limiting membrane, OPL, and around blood vessels. Immunoelectron microscopy detected β-DG immunoreactive products under the photoreceptor cell membrane, which are the same regions of dystrophin localization. In addition, β-DG was detected under the Müller cell membrane that is attached to the paravitreous or perivascular basement membrane. Our results suggest that β-DG may interact with dystrophin in photoreceptor membranes. However, β-DG-related interactions between Müller cells and basement membranes appear to be independent of dystrophin and raise the possibility that β-DG interacts with other molecules. We speculate that β-DG plays a role in maintaining the structural relationship between photoreceptor and bipolar cells or between Müller cells and basement membranes.

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48

Leivo, I., e E. Engvall. "C3d fragment of complement interacts with laminin and binds to basement membranes of glomerulus and trophoblast." Journal of Cell Biology 103, n. 3 (1 settembre 1986): 1091–100. http://dx.doi.org/10.1083/jcb.103.3.1091.

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Abstract (sommario):

Two mouse monoclonal antibodies generated against human placental homogenate were found to react specifically with human complement component C3. In immunofluorescence of human tissues, these antibodies gave a bright linear staining outlining the glomerular basement membrane of the adult kidney and the trophoblast basement membrane of placenta. An identical staining pattern was observed with a rabbit C3d antiserum which also prevented binding of the monoclonal antibodies to tissue sections. Only negligible basement membrane staining was observed in the same tissues with antisera to human C3c, C5, IgG, IgA, or IgM. When interactions of C3 with basement membrane proteins were tested in enzyme immunoassays and column chromatography, C3(H2O) was found to bind efficiently to solid-phase laminin. Native C3 from fresh plasma did not bind to laminin but C3 from plasma treated with methylamine bound efficiently. When C3 was cleaved with trypsin, C3b and C3d but not C3c bound to laminin-Sepharose. The interaction of C3 and laminin was inhibited by soluble laminin and by high ionic strength. The results indicate that C3d, a biologically active breakdown product of C3, can be found in glomerular and placental basement membranes in the absence of signs for ongoing local complement activation or immune complex deposition. It is possible that binding affinities between C3 and basement membrane molecules, especially laminin, are involved in the retention of C3d at these sites. Such interactions between C3 and components of the glomerular basement membrane could play important roles in complement-related pathological processes of the glomerulus.

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49

Streuli, C. H., e M. J. Bissell. "Expression of extracellular matrix components is regulated by substratum." Journal of Cell Biology 110, n. 4 (1 aprile 1990): 1405–15. http://dx.doi.org/10.1083/jcb.110.4.1405.

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Abstract (sommario):

Reconstituted basement membranes and extracellular matrices have been demonstrated to affect, positively and dramatically, the production of milk proteins in cultured mammary epithelial cells. Here we show that both the expression and the deposition of extracellular matrix components themselves are regulated by substratum. The steady-state levels of the laminin, type IV collagen, and fibronectin mRNAs in mammary epithelial cells cultured on plastic dishes and on type I collagen gels have been examined, as has the ability of these cells to synthesize, secrete, and deposit laminin and other, extracellular matrix proteins. We demonstrate de novo synthesis of a basement membrane by cells cultured on type I collagen gels which have been floated into the medium. Expression of the mRNA and proteins of basement membranes, however, are quite low in these cultures. In contrast, the levels of laminin, type IV collagen, and fibronectin mRNAs are highest in cells cultured on plastic surfaces, where no basement membrane is deposited. It is suggested that the interaction between epithelial cells and both basement membrane and stromally derived matrices exerts a negative influence on the expression of mRNA for extracellular matrix components. In addition, we show that the capacity for lactational differentiation correlates with conditions that favor the deposition of a continuous basement membrane, and argue that the interaction between specialized epithelial cells and stroma enables them to create their own microenvironment for accurate signal transduction and phenotypic function.

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50

Murray, P., e D. Edgar. "Regulation of the differentiation and behaviour of extra-embryonic endodermal cells by basement membranes". Journal of Cell Science 114, n. 5 (1 marzo 2001): 931–39. http://dx.doi.org/10.1242/jcs.114.5.931.

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Abstract (sommario):

Both the extracellular matrix and parathyroid hormone-related peptide (PTHrP) have been implicated in the differentiation and migration of extra-embryonic endodermal cells in the pre-implantation mammalian blastocyst. In order to define the individual roles and interactions between these factors in endodermal differentiation, we have used embryoid bodies derived from Lamc1(-/-) embryonic stem cells that lack basement membranes. The results show that in the absence of basement membranes, increased numbers of both visceral and parietal endodermal cells differentiate, but they fail to form organised epithelia. Furthermore, although parietal endodermal cells only migrate away from control embryoid bodies in the presence of PTHrP, they readily migrate from Lamc1(-/-) embryoid bodies in the absence of PTHrP, and this migration is unaffected by PTHrP. Thus, the basement membrane between epiblast and extra-embryonic endoderm is required for the proper organisation of visceral and parietal endodermal cells and also restricts their differentiation to maintain the population of primitive endodermal stem cells. Moreover, this basement membrane inhibits migration of parietal endodermal cells, the role of PTHrP being to stimulate delamination of parietal endodermal cells from the basement membrane rather than promoting migration per se.

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