scholarly journals The effect of fixatives and paraffin embedding on the histochemical reactivity of a monoclonal antibody against human type IV collagen (JK-199).

1989 ◽  
Vol 52 (5) ◽  
pp. 477-483 ◽  
Author(s):  
Jun KINO ◽  
Toshihiko HAYAHI ◽  
Yoshihisa SATO ◽  
Paulo H. HASHIMOTO ◽  
Eijiro ADACHI
Keyword(s):  
Monoclonal Antibody ◽  
Type Iv Collagen ◽  
Paraffin Embedding ◽  
Human Type ◽  
Type Iv ◽  
Histochemical Reactivity

The Localization and Secretion of Type IV Collagen in Synovial Capillaries by Immunohistochemistry Using a Monoclonal Antibody against Human Type IV Collagen

Pathobiology ◽  
1984 ◽  
Vol 52 (3) ◽  
pp. 159-169 ◽  
Author(s):  
Tsukasa Matsubara ◽  
Beat Trüeb ◽  
Kurt Fehr ◽  
Jacques R. Rüttner ◽  
Bernhard F. Odermatt
Keyword(s):  
Monoclonal Antibody ◽  
Type Iv Collagen ◽  
Human Type ◽  
Type Iv

scholarly journals Monoclonal antibodies against chicken type IV and V collagens: electron microscopic mapping of the epitopes after rotary shadowing.

1984 ◽  
Vol 98 (5) ◽  
pp. 1637-1644 ◽  
Author(s):  
R Mayne ◽  
H Wiedemann ◽  
M H Irwin ◽  
R D Sanderson ◽  
J M Fitch ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cleavage Site ◽  
Type Iv Collagen ◽  
Collagen Molecule ◽  
Electron Microscopic ◽  
Type V Collagen ◽  
Type Iv ◽  
Type V ◽  
Rotary Shadowing

The location of the epitopes for monoclonal antibodies against chicken type IV and type V collagens were directly determined in the electron microscope after rotary shadowing of antibody/collagen mixtures. Three monoclonal antibodies against type IV collagen were examined, each one of which was previously demonstrated to be specific for only one of the three pepsin-resistant fragments of the molecule. The three native fragments were designated (F1)2F2, F3, and 7S, and the antibodies that specifically recognize each fragment were called, respectively, IA8 , IIB12 , and ID2 . By electron microscopy, monoclonal antibody IA8 recognized an epitope located in the center of fragment (F1)2F2 and in tetramers of type IV collagen at a distance of 288 nm from the 7S domain, the region of overlap of four type IV molecules. Monoclonal antibody IIB12 , in contrast, recognized an epitope located only 73 nm from the 7S domain. This result therefore provides direct visual evidence that the F3 fragment is located closest to the 7S domain and the order of the fragments must be 7S-F3-(F1)2F2. The epitope for antibody ID2 was located in the overlap region of the 7S domain, and often several antibody molecules were observed to binding to a single 7S domain. The high frequency with which antibody molecules were observed to bind to fragments of type IV collagen suggests that there is a single population of type IV molecules of chain organization [alpha 1(IV)]2 alpha 2(IV), and that four identical molecules must form a tetramer that is joined in an antiparallel manner at the 7S domain. The monoclonal antibodies against type V collagen, called AB12 and DH2 , were both found to recognize epitopes close to one another, the epitopes being located 45-48 nm from one end of the type V collagen molecule. The significance of this result still remains uncertain, but suggests that this site is probably highly immunoreactive. It may also be related to the specific cleavage site of type V collagen by selected metalloproteinases and by alpha-thrombin. This cleavage site is also known to be located close to one end of the type V molecule.

In vitro and post-transplantation differentiation of human keratinocytes grown on the human type IV collagen film of a bilayered dermal substitute

1991 ◽  
Vol 193 (2) ◽  
pp. 310-319 ◽  
Author(s):  
Estelle Tinois ◽  
Jerome Tiollier ◽  
Martine Gaucherand ◽  
Henri Dumas ◽  
Michel Tardy ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Human Keratinocytes ◽  
Dermal Substitute ◽  
Post Transplantation ◽  
Collagen Film ◽  
Human Type ◽  
Type Iv

scholarly journals An Ehrlich chromogen in collagen cross-links

1983 ◽  
Vol 209 (1) ◽  
pp. 263-264 ◽  
Author(s):  
J E Scott ◽  
R G Qian ◽  
W Henkel ◽  
R W Glanville
Keyword(s):  
Type Iv Collagen ◽  
Rich Source ◽  
Type Iii Collagen ◽  
Cross Link ◽  
Type Iii ◽  
Human Type ◽  
Type Iv ◽  
Cross Links

A well-characterized three-chain peptide [(Col1)2 X T9] from human type III collagen was a rich source of Ehrlich chromogen. The corresponding two-chain peptide [(Col1)2] was not, implying that the Ehrlich chromogen is a trifunctional cross-link. (Col1)2 X T9 also contained pyridinoline, which is not an Ehrlich chromogen. The 7S domain of type IV collagen also contained an Ehrlich chromogen.

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