The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane

FEBS Letters ◽  
1990 ◽  
Vol 273 (1-2) ◽  
pp. 168-172 ◽  
Author(s):  
Karlheinz Mann ◽  
Renate Jander ◽  
Eberhard Korsching ◽  
Klaus Kühn ◽  
Jürgen Rauterberg
Keyword(s):  
Primary Structure ◽  
Collagen Type ◽  
Type Viii ◽  
Helical Domain ◽  
Descemet's Membrane ◽  
Descemet’S Membrane ◽  
Triple Helical Domain

The collagenous protein with elastin crosslinks from Descemet's membrane is not related to type VIII collagen

1990 ◽  
Vol 171 (1) ◽  
pp. 260-265 ◽  
Author(s):  
Paul F Davis ◽  
Patricia A Ryan ◽  
Reinhold Kittelberger ◽  
Nicholas S Greenhill
Keyword(s):  
Type Viii ◽  
Descemet's Membrane ◽  
Descemet’S Membrane

scholarly journals Characterization of the collagen in the hexagonal lattice of Descemet's membrane: its relation to type VIII collagen.

1990 ◽  
Vol 110 (1) ◽  
pp. 219-227 ◽  
Author(s):  
H Sawada ◽  
H Konomi ◽  
K Hirosawa
Keyword(s):  
Monoclonal Antibodies ◽  
Lattice Structure ◽  
Hexagonal Lattice ◽  
Corneal Endothelial Cells ◽  
Type Viii ◽  
Descemet's Membrane ◽  
Descemet’S Membrane

To investigate the nature of the hexagonal lattice structure in Descemet's membrane, monoclonal antibodies were raised against a homogenate of bovine Descemet's membranes. They were screened by immunofluorescence microscopy to obtain antibodies that label Descement's membrane. Some monoclonal antibodies labeled both Descemet's membrane and fine filaments within the stroma. In electron microscopy, with immunogold labeling on a critical point dried specimen, the antibodies labeled the hexagonal lattices and long-spacing structures produced by the bovine corneal endothelial cells in culture; 6A2 antibodies labeled the nodes of the lattice and 9H3 antibodies labeled the sides of the lattice. These antibodies also labeled the hexagonal lattice of Descemet's membrane in situ in ultrathin frozen sectioning. In immunofluorescence, these antibodies stained the sclera, choroid, and optic nerve sheath and its septum. They also labeled the dura mater of the spinal cord, and the perichondrium of the tracheal cartilage. In immunoblotting, the antibodies recognized 64-kD collagenous peptides both in tissue culture and in Descemet's membrane in vivo. They also recognized 50-kD pepsin-resistant fragments from Descemet's membranes that are related to type VIII collagen. However, they did not react either in immunoblotting or in immunoprecipitation with medium of subconfluent cultures from which type VIII collagen had been obtained. The results are discussed with reference to the nature of type VIII collagen, which is currently under dispute. This lattice collagen may be a member of a novel class of long-spacing fibrils.

scholarly journals Type VIII collagen has a restricted distribution in specialized extracellular matrices.

1988 ◽  
Vol 107 (2) ◽  
pp. 721-730 ◽  
Author(s):  
R Kapoor ◽  
L Y Sakai ◽  
S Funk ◽  
E Roux ◽  
P Bornstein ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Endothelial Cells ◽  
Basement Membranes ◽  
Extracellular Matrices ◽  
Corneal Endothelial Cells ◽  
Type Viii ◽  
Competition Elisa ◽  
Descemet's Membrane ◽  
Immunofluorescence Studies ◽  
Descemet’S Membrane

A pepsin-resistant triple helical domain (chain 50,000 Mr) of type VIII collagen was isolated from bovine corneal Descemet's membrane and used as an immunogen for the production of mAbs. An antibody was selected for biochemical and tissue immunofluorescence studies which reacted both with Descemet's membrane and with type VIII collagen 50,000-Mr polypeptides by competition ELISA and immunoblotting. This antibody exhibited no crossreactivity with collagen types I-VI by competition ELISA. The mAb specifically precipitated a high molecular mass component of type VIII collagen (EC2, of chain 125,000 Mr) from the culture medium of subconfluent bovine corneal endothelial cells metabolically labeled for 24 h. In contrast, confluent cells in the presence of FCS and isotope for 7 d secreted a collagenous component of chain 60,000 Mr that did not react with the anti-type VIII collagen IgG. Type VIII collagen therefore appears to be synthesized as a discontinuous triple helical molecule with a predominant chain 125,000 Mr by subconfluent, proliferating cells in culture. Immunofluorescence studies with the mAb showed that type VIII collagen was deposited as fibrils in the extracellular matrix of corneal endothelial cells. In the fetal calf, type VIII collagen was absent from basement membranes and was found in a limited number of tissues. In addition to the linear staining pattern observed in the Descemet's membrane, type VIII collagen was found in highly fibrillar arrays in the ocular sclera, in the meninges surrounding brain, spinal cord, and optic nerve, and in periosteum and perichondrium. Fine fibrils were evident in the white matter of spinal cord, whereas a more generalized staining was apparent in the matrices of cartilage and bone. Despite attempts to unmask the epitope, type VIII collagen was not found in aorta, kidney, lung, liver, skin, and ligament. We conclude that this unusual collagen is a component of certain specialized extracellular matrices, several of which are derived from the neural crest.

scholarly journals Amino acid sequence of the triple-helical domain of human collagen type VI.

1988 ◽  
Vol 263 (35) ◽  
pp. 18601-18606 ◽  
Author(s):  
M L Chu ◽  
D Conway ◽  
T C Pan ◽  
C Baldwin ◽  
K Mann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Collagen Type ◽  
Helical Domain ◽  
Collagen Type Vi ◽  
Human Collagen ◽  
Triple Helical Domain

Cleavage plane after liquid‐bubble preparation of Descemet’s membrane

2020 ◽  
Author(s):  
Annekatrin Rickmann ◽  
Silke Wahl ◽  
Alisa Katsen‐Globa ◽  
André Schulz ◽  
Norbert Pütz ◽  
...  
Keyword(s):  
Cleavage Plane ◽  
Descemet's Membrane ◽  
Liquid Bubble ◽  
Descemet’S Membrane

scholarly journals Corneal pachymetry by AS-OCT after Descemet’s membrane endothelial keratoplasty

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Friso G. Heslinga ◽  
Ruben T. Lucassen ◽  
Myrthe A. van den Berg ◽  
Luuk van der Hoek ◽  
Josien P. W. Pluim ◽  
...  
Keyword(s):  
Deep Learning ◽  
Endothelial Function ◽  
Corneal Thickness ◽  
Anterior Segment ◽  
Anatomical Landmarks ◽  
Endothelial Keratoplasty ◽  
Descemet’S Membrane Endothelial Keratoplasty ◽  
Descemet's Membrane ◽  
Descemet’S Membrane ◽  
Thickness Measurements

AbstractCorneal thickness (pachymetry) maps can be used to monitor restoration of corneal endothelial function, for example after Descemet’s membrane endothelial keratoplasty (DMEK). Automated delineation of the corneal interfaces in anterior segment optical coherence tomography (AS-OCT) can be challenging for corneas that are irregularly shaped due to pathology, or as a consequence of surgery, leading to incorrect thickness measurements. In this research, deep learning is used to automatically delineate the corneal interfaces and measure corneal thickness with high accuracy in post-DMEK AS-OCT B-scans. Three different deep learning strategies were developed based on 960 B-scans from 50 patients. On an independent test set of 320 B-scans, corneal thickness could be measured with an error of 13.98 to 15.50 μm for the central 9 mm range, which is less than 3% of the average corneal thickness. The accurate thickness measurements were used to construct detailed pachymetry maps. Moreover, follow-up scans could be registered based on anatomical landmarks to obtain differential pachymetry maps. These maps may enable a more comprehensive understanding of the restoration of the endothelial function after DMEK, where thickness often varies throughout different regions of the cornea, and subsequently contribute to a standardized postoperative regime.

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