scholarly journals Analysis of the collagen types synthesized by bovine corneal endothelial cells in culture

1981 ◽  
Vol 198 (3) ◽  
pp. 707-710 ◽  
Author(s):  
E A Sankey ◽  
F E Bown ◽  
L F Morton ◽  
D M Scott ◽  
M J Barnes
Keyword(s):  
Endothelial Cells ◽  
Type Iii Collagen ◽  
Corneal Endothelial Cells ◽  
Collagen Types ◽  
Type Iii ◽  
Cells In Culture ◽  
Type Iv ◽  
Coated Surface

Bovine corneal endothelial cells synthesize in culture predominantly type III collagen, with lesser amounts of types I and V and apparently little if any type IV. This pattern of synthesis is observed in both dividing and post-confluent cultures and irrespective of whether cells are attached to plastic or collagen-coated surface.

scholarly journals Connective tissue of rat lung. II: Ultrastructural localization of collagen types III, IV, and VI.

1988 ◽  
Vol 36 (9) ◽  
pp. 1167-1173 ◽  
Author(s):  
P S Amenta ◽  
J Gil ◽  
A Martinez-Hernandez
Keyword(s):  
Type I Collagen ◽  
Ultrastructural Localization ◽  
Basement Membranes ◽  
Type Iii Collagen ◽  
Similar Distribution ◽  
Type I ◽  
Rat Lung ◽  
Collagen Types ◽  
Type Iii ◽  
Type Iv

We localized collagen types III, IV, and VI in normal rat lung by light and electron immunohistochemistry. Type IV collagen was present in every basement membrane examined and was absent from all other structures. Although types III and VI had a similar distribution, being present in the interstitium of major airways, blood vessels, and alveolar septa, as in other organs, they had different morphologies. Type III collagen formed beaded fibers, 15-20 nm in diameter, whereas type VI collagen formed fine filaments, 5-10 nm in diameter. Both collagen types were found exclusively in the interstitium, often associated with thick (30-35 nm) cross-banded type I collagen fibers. Occasionally, type III fibers and type VI filaments could be found bridging from the interstitium to the adventitial aspect of some basement membranes. Furthermore, the association of collagen type VI with types I and III and basement membranes suggests that type VI may contribute to integration of the various components of the pulmonary extracellular matrix into a functional unit.

scholarly journals A procedure for light and electron microscopic intracellular immunolocalization of collagen and fibronectin in rat liver.

1985 ◽  
Vol 33 (5) ◽  
pp. 407-414 ◽  
Author(s):  
B Clement ◽  
M Rissel ◽  
S Peyrol ◽  
Y Mazurier ◽  
J A Grimaud ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Type Iii Collagen ◽  
Collagen Types ◽  
Electron Microscopic ◽  
Experimental Conditions ◽  
The Matrix ◽  
Matrix Components ◽  
Indirect Immunoperoxidase

Experimental conditions have been designed that permit both extracellular and intracellular immunolocalization of various collagen types and fibronectin in rat liver. The procedure involves paraformaldehyde fixation by perfusion of the organ, use of saponin as a membrane permeabilizing agent, and visualization of the matrix components by indirect immunoperoxidase. Intracellular demonstration of collagens was particularly sensitive to the composition of the fixative and the duration of fixation. Hepatocytes contained fibronectin and types I and IV collagen, whereas fat-storing and endothelial cells evidenced type III collagen in addition. All the components were specifically located in the endoplasmic reticulum and/or the Golgi apparatus.

scholarly journals Abnormal type III collagen produced by an exon-17-skipping mutation of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the extracellular matrix

1995 ◽  
Vol 311 (3) ◽  
pp. 939-943 ◽  
Author(s):  
A A Chiodo ◽  
D O Sillence ◽  
W G Cole ◽  
J F Bateman
Keyword(s):  
Extracellular Matrix ◽  
Triple Helix ◽  
Type Iii Collagen ◽  
Syndrome Type ◽  
Ehlers Danlos Syndrome ◽  
Type Iii ◽  
Type Iv ◽  
Col3a1 Gene ◽  
Collagen Molecules ◽  
Danlos Syndrome

A novel heterozygous mutation of the COL3A1 gene that encodes the alpha 1(III) chains of type III collagen was identified in a family with the acrogeric form of Ehlers-Danlos syndrome type IV (EDS-IV). Cultured dermal fibroblasts produced normal and shortened alpha 1(III) chains. The triple helix of the latter chain was shortened owing to a 33 amino acid deletion of Gly-184 to Pro-216. The corresponding region of cDNA lacked 99 base pairs from nucleotides 1051 to 1149. The deletions corresponded exactly to the normal sequence encoded by exon 17 of the COL3A1 gene. The proband was heterozygous for a T to G transversion at position +2 of intron 17, which resulted in skipping of exon 17. The splicing defect was not corrected by growing the fibroblasts at 33 degrees C and no other splicing variants were identified at 33 or 37 degrees C. The affected brother had the same mutation but his unaffected mother did not. Heterotrimeric type III collagen molecules containing normal and mutant chains were retained within the cell. The mutant homotrimeric molecules were modified and secreted normally and were thermally stable. These normal characteristics of the mutant homotrimers suggested that the loss of ten Gly-Xaa-Yaa triplets (where Gly-Xaa-Yaa is a repetitive amino acid triplet structure in which Xaa and Yaa are other amino acids, proline and hydroxyproline being more common in the Yaa position) did not adversely affect the formation and stability of the triple helix or the structural requirements for secretion. However, the mutant homotrimers were not incorporated into the extracellular matrix of an in vitro model of EDS-IV dermis. The EDS-IV phenotype in this family was probably due to a deficiency in the amount of normal type III collagen available for formation of the heterotypic collagen fibrils of the extracellular matrix. Intracellular and extracellular quality-control mechanisms prevented the incorporation of heterotrimeric and homotrimeric mutant type III collagen molecules into the cross-linked extracellular matrix.

scholarly journals Multiple antigenic determinants on type III collagen

1991 ◽  
Vol 274 (3) ◽  
pp. 895-898 ◽  
Author(s):  
J A Werkmeister ◽  
J A M Ramshaw
Keyword(s):  
Monoclonal Antibodies ◽  
Connective Tissue ◽  
Tryptic Digestion ◽  
Antigenic Determinants ◽  
Type Iii Collagen ◽  
Collagen Types ◽  
Type Iii ◽  
Wide Range

Eight monoclonal antibodies have been produced against human pepsin-soluble type III collagen. All antibodies were shown to be highly specific for type III collagen and did not cross-react with a range of other collagen types or connective-tissue proteins. Examination of type III collagen from other species showed that these antibodies had a wide range of species specificities, indicating that several distinct epitopes were being recognized. The location of the epitopes was investigated by using reactivity of the antibodies to CNBr fragments and to sequential fragments formed by tryptic digestion of renaturing type III collagen. These data also indicated that several distinct epitopes were recognized and that they were located over the length of the type III collagen.

A 27-bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV

1992 ◽  
Vol 88 (3) ◽  
pp. 325-330 ◽  
Author(s):  
A. J. Richards ◽  
J. C. Lloyd ◽  
P. Narcisi ◽  
P. N. Ward ◽  
A. C. Nicholls ◽  
...  
Keyword(s):  
Large Family ◽  
Type Iii Collagen ◽  
Collagen Gene ◽  
Syndrome Type ◽  
Ehlers Danlos Syndrome ◽  
Type Iii ◽  
Type Iv ◽  
Danlos Syndrome
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