Where is basement membrane found




















The basal lamina provides support to the overlying epithelium, limits contact between epithelial cells and the other cell types in the tissue and acts as a filter allowing only water and small molecules to pass through. If the epithelial cells become transformed cancerous and become 'malignant', they are able to break through the basement membrane and invade the tissues beneath. This characteristic is one used in the diagnosis of malignant epithelial tumors. The basal lamina consists of a mixture of collagens, laminin glycoprotein , perlecan heparan sulphate glycoprotein , entactin glycoprotein.

These proteins can bind to each other to make a highly crosslinked extracellular matrix as shown in this diagram. All epithelia have a basal lamina which lies between the cells and the underlying connective tissue. This layer is so thin that it is often difficult to see with conventional light microscopy and is usually only clearly defined under the electron microscope.

The basal lamina helps to attach and anchor the cells to the underlying connective tissue. Proteins integrins and proteglycans in the cell membranes attach to proteins in the basal lamina, which in turn is linked to the extracellular matrix of connective tissue. Kahsai, T. Seminiferous tubule basement membrane. A program of cell death and extracellular matrix degradation is activated in the amnion before the onset of labor.

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The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor. Miosge, N. Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice.

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DNA 8 , — Altered synthesis of laminin 1 and absence of basement membrane component deposition in beta 1 integrin-deficient embryoid bodies. Cell Sci. Ancsin, J. Laminin interactions important for basement membrane assembly are promoted by zinc and implicate laminin zinc finger-like sequences. Tsiper, M. Laminin assembles into separate basement membrane and fibrillar matrices in Schwann cells.

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Talts, J. Mutation of a basic sequence in the laminin alpha2LG3 module leads to a lack of proteolytic processing and has different effects on beta1 integrin-mediated cell adhesion and alpha-dystroglycan binding.

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Ramchandran, R. Antiangiogenic activity of restin, NC10 domain of human collagen XV: comparison to endostatin. Rehn, M. Alpha 1 XVIII , a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen. A network model for the organization of type IV collagen molecules in basement membranes. Kuhn, K. Macromolecular structure of basement membrane collagens. Hagg, P. Cloning of mouse type XV collagen sequences and mapping of the corresponding gene to 4B Comparison of mouse and human alpha 1 XV collagen sequences indicates divergence in the number of small collagenous domains.

Genomics 45 , 31—41 Muragaki, Y. The human alpha 1 XV collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1 XVIII collagen. Muona, A. Myers, J.

Identification of a previously unknown human collagen chain, alpha 1 XV , characterized by extensive interruptions in the triple-helical region. USA 89 , — Gene , — Type XV collagen exhibits a widespread distribution in human tissues but a distinct localization in basement membrane zones.

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Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity. Structure and function of collagen-derived endostatin inhibitors of angiogenesis.

Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin. Eklund, L. Lack of type XV collagen causes a skeletal myopathy and cardiovascular defects in mice. USA 98 , — Oh, S. Genomics 19 , — Hohenester, E. Crystal structure of the angiogenesis inhibitor endostatin at 1. Suzuki, O. Molecular analysis of collagen XVIII reveals novel mutations, presence of a third isoform, and possible genetic heterogeneity in Knobloch syndrome.

Folkman, J. Anti-angiogenesis: new concept for therapy of solid tumors. Tumor angiogenesis: therapeutic implications. Isolation of a tumor factor responsible or angiogenesis. Regulation of angiogenesis. Blood 82 , 60 Carmeliet, P. Angiogenesis in cancer and other diseases. Nature , — Jain, R.

Vessels of death or life. Incipient angiogenesis. Natl Cancer Inst. Hanahan, D. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 86 , — The hallmarks of cancer. Cell , 57—70 Blood vessel formation: what is its molecular basis? Cell 87 , — Clark, E. Microscopic observation on the growth of blood capillaries in the living organisms. Form, D. Endothelial cell proliferation during angiogenesis. In vitro modulation by basement membrane components. Madri, J.

Endothelial cell-matrix interactions: in vitro models of angiogenesis. Extracellular matrix modulation of vascular cell behaviour. Ingber, D. Mechanochemical switching between growth and differentiation during fibroblast growth factor-stimulated angiogenesis in vitro : role of extracellular matrix. Angiogenesis in cancer, vascular, rheumatoid and other disease.

Nature Med. Egeblad, M. New functions for the matrix metalloproteinases in cancer progression. Nature Rev. Cancer 2 , — Eliceiri, B. Adhesion events in angiogenesis. Increasing evidence suggests that BMs are unique signal input devices that likely fine tune cellular function.

Additionally, the resulting endothelial and epithelial heterogeneity in human body is a direct contribution of cell-matrix interaction facilitated by the diverse compositions of BMs. Abstract Basement membranes BMs are present in every tissue of the human body.



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