Expression of capillary basement membrane components during sequential phases of wound angiogenesis. 1996

G C Sephel, and R Kennedy, and S Kudravi
Research Service, Department of Veterans Affairs Medical Center, Nashville, Tennessee, USA.

Before capillaries sprout to form new vessels in a wound, the endothelial cells are sequestered from the surrounding stromal or provisional matrix by a well organized protein envelope called the basement membrane (BM). After breaching the BM, endothelial cells are exposed to the wound provisional matrix and begin to migrate and proliferate. Endothelial derived basement membrane proteins and molecules of the provisional matrix are mutually accessible to the endothelial cell surface during migration. Eventually, new capillaries again segregate in a formed envelope of basement membrane and resume a tubular morphology. Endothelial cell recognition of the architecture and concentration of basement membrane ligands appears to be an important determinant of capillary morphology during angiogenesis. In this study, we characterized the molecular composition, expression and steady-state transcript levels of BM proteins during sequential stages of wound angiogenesis. Specific analysis of rat capillary BM transcripts was achieved by employing a space-filling wound model which did not have non-capillary BM. Invading capillaries appeared between days 3 and 5 and matured by day 12. Occasionally, vessels larger than capillaries were observed to form by a process resembling vasculogenesis. Steady-state transcript levels for subunits of all major BM proteins studied were readily measured by day 3, and laminin and type IV collagen immunostaining were evident at the periphery of all vessels studied. From vessel initiation to regression, the transcript levels most changed were the alpha 1 and alpha 2 transcripts of type IV collagen; after an early peak, they exhibited a sharp three-fold decline as the response progressed. Conversely, entactin and laminin subunits did not decline as the response progressed, suggesting an increasing ratio of expression relative to type IV collagen. Perlecan expression was inconsistent, but it appeared to decline during the late phase of the response. Laminin beta 1 and gamma 1, but not alpha 1 or beta 2, transcripts were expressed by forming capillaries, providing evidence that the laminin 1, 3, 4 and 7 isotypes are not expressed by growing capillaries. These results also demonstrate that the steady-state ratios of type IV collagen transcripts to laminin and entactin transcripts are greatest during the early proliferative-migratory phase of angiogenesis but decrease significantly in later phases, when vessel maturation and tube formation predominate.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D007797 Laminin Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion. Merosin,Glycoprotein GP-2,Laminin M,Laminin M Chain,Chain, Laminin M,Glycoprotein GP 2,M Chain, Laminin
D008297 Male Males
D008562 Membrane Glycoproteins Glycoproteins found on the membrane or surface of cells. Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell
D011142 Polyvinyl Alcohol A polymer prepared from polyvinyl acetates by replacement of the acetate groups with hydroxyl groups. It is used as a pharmaceutic aid and ophthalmic lubricant as well as in the manufacture of surface coatings artificial sponges, cosmetics, and other products. Liquifilm Tears,Polyviol,Alcohol, Polyvinyl,Tears, Liquifilm
D011509 Proteoglycans Glycoproteins which have a very high polysaccharide content. Proteoglycan,Proteoglycan Type H
D002196 Capillaries The minute vessels that connect arterioles and venules. Capillary Beds,Sinusoidal Beds,Sinusoids,Bed, Sinusoidal,Beds, Sinusoidal,Capillary,Capillary Bed,Sinusoid,Sinusoidal Bed
D003094 Collagen A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D004730 Endothelium, Vascular Single pavement layer of cells which line the luminal surface of the entire vascular system and regulate the transport of macromolecules and blood components. Capillary Endothelium,Vascular Endothelium,Capillary Endotheliums,Endothelium, Capillary,Endotheliums, Capillary,Endotheliums, Vascular,Vascular Endotheliums
D006497 Heparitin Sulfate A heteropolysaccharide that is similar in structure to HEPARIN. It accumulates in individuals with MUCOPOLYSACCHARIDOSIS. Heparan Sulfate,Sulfate, Heparan,Sulfate, Heparitin

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