Physical and immunochemical studies of the globular domain of type IV collagen. Cryptic properties of the Goodpasture antigen.

The structural scaffolding of basement membrane (BM) is formed by a polymerized and covalently cross-linked network of type IV collagen whose molecular structure in situ has eluded detailed analysis. The monomeric unit of assembly of this collagen is a 424nm linear protein which, compared to other interstitial collagens, is longer, more flexible, contains frequent interruptions by non-collagenous type sequences, and possesses distinct end-region domains. Type IV collagen, unlike the interstitial collagens I, II & III, does not assemble into long bundled fibers. Our present knowledge of collagen IV's intermole- cular associations comes from biochemical characterizations correlated with low angle rotary shadowed glycerol spreads of proteolytically extracted fragments’ and reconstituted collagen IV oligomeric complexes and networks Earlier work led to the identification of an amino(N)-terminal 30nm region that binds three other N-termini in an overlapping fashion to produce a four-armed tetramer (7s domain) and a carboxyl(C)-terminal globular domain (NC-1) of a given monomer which attaches to the same domain of another monomer to form a linear dimer.

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Goodpasture antigen of the glomerular basement membrane: localization to noncollagenous regions of type IV collagen.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.81.12.3838 ◽

1984 ◽

Vol 81 (12) ◽

pp. 3838-3842 ◽

Cited By ~ 134

Author(s):

J. Wieslander ◽

J. F. Barr ◽

R. J. Butkowski ◽

S. J. Edwards ◽

P. Bygren ◽

...

Keyword(s):

Basement Membrane ◽

Glomerular Basement Membrane ◽

Type Iv Collagen ◽

Membrane Localization ◽

Type Iv ◽

Goodpasture Antigen

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Nephritogenicity of glomerular basement membrane: a molecular aspect

Paediatrica Indonesiana ◽

10.14238/pi41.6.2001.273-8 ◽

2001 ◽

Vol 41 (6) ◽

pp. 273

Author(s):

Syarifuddin Rauf

Keyword(s):

Basement Membrane ◽

Glomerular Basement Membrane ◽

Type Iv Collagen ◽

Globular Domain ◽

Genetic Studies ◽

X Chromosomes ◽

Type Iv ◽

Human Gbm ◽

Main Component ◽

Helical Molecules

Glomerular basement membrane (GBM) has multifunctions. One of its functions is having nephritogenicitywhich means the ability of an antigen originally from GBM in causing glomerulonephritis, either in experimental animal or in human being. Recent studies on GBM have revealed that its main component is type IV collagen, consists of 6 different isoforms, α1 (IV) to α 6 (IV) chains. Genetic studies show that all of the six α chains are encoded by genes located in 2, 13, and X chromosomes. Nephritogenic antigen in GBM has been identified as α3, α4, α5 chains. They are molecules of type IV collagen located in globular domain (NC1 domain) at the carboxyl terminus of the type IV collagen of GBM. They are thought to assemble into a α3- α4- α5 (IV) chain helical molecules in human GBM. Other α chains, namely α1 and α2 chain, are not nephritogenic or poorly nephritogenic, while the α6 chain is not located in GBM. The nephritogenicity of GBM has been elucidated as a cause in experimental anti-GMB nephritis, and in Goodpasture and Alport syndromes.

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The use of 1nm silver enhanced gold probes for the detection of skin antigens

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100162077 ◽

1990 ◽

Vol 48 (3) ◽

pp. 902-903

Author(s):

J.P Cassella ◽

H. Shimizu ◽

A. Ishida-Yamamoto ◽

R.A.J. Eady

Keyword(s):

Type Iv Collagen ◽

Freeze Substitution ◽

Collagen Type Iv ◽

Electron Microscopic ◽

Normal Human Skin ◽

Type Iv ◽

Type Vii Collagen ◽

Keratin Filaments ◽

Normal Human ◽

Phosphate Buffered Saline

1nm colloidal gold with silver enhancement has been used in conjunction with a low-temperature post-embedding (post-E) technique for the demonstration of skin antigens at both the light microscopic (LM) and electron microscopic (EM) levels.Keratin filaments and basement membrane zone (BMZ) associated antigens in normal human skin (NHS) were immunolabelled using antibodies against keratin 14, 10, and 1, the carboxy-terminus and collagenous portion of type VII collagen, type IV collagen and bullous pemphigoid antigen (BP-Ag).Fresh samples of NHS were cryoprotected in 15% glycerol, cryofixed in propane at -190°C, subjected to freeze substitution in methanol at -80°C and embedded in Lowicryl K11M at -60°C. Polymerisation of the resin was initiated under UVR at - 60°C for 48 hours and continued at room temperature for a further 48 hours. Semith in sections were air dried onto slides coated with 3-aminopropyltriethoxysilane. The following immunolabelling protocol was adopted: Primary antibody was applied for 2 hours at 37°C or overnight at 4°C. Following washing in Dulbecco’s phosphate buffered saline (PBSA) a biotinylated secondary antibody was applied for 2 hours at 37°C. The sections were further washed in PBSA and 1nm gold avidin was applied. Sections were finally washed in PBSA and silver enhanced.

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