scholarly journals Glomerular filtration and podocyte tensional homeostasis: importance of the minor type IV collagen network

2020 ◽  
Vol 19 (6) ◽  
pp. 2433-2442
Author(s):  
Lauren M. Bersie-Larson ◽  
Lazarina Gyoneva ◽  
Daniel J. Goodman ◽  
Kevin D. Dorfman ◽  
Yoav Segal ◽  
...  
Keyword(s):  
Glomerular Filtration ◽  
Type Iv Collagen ◽  
Collagen Network ◽  
Type Iv ◽  
Tensional Homeostasis

scholarly journals Identification of the NC1 Domain of α3 Chain as Critical for α3α4α5 Type IV Collagen Network Assembly

2010 ◽  
Vol 285 (53) ◽  
pp. 41874-41885 ◽  
Author(s):  
Valerie LeBleu ◽  
Malin Sund ◽  
Hikaru Sugimoto ◽  
Gabriel Birrane ◽  
Keizo Kanasaki ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Collagen Network ◽  
Type Iv ◽  
Nc1 Domain

Complexity of type IV collagens: from network assembly to function

2019 ◽  
Vol 400 (5) ◽  
pp. 565-574 ◽  
Author(s):  
Yuexin Wu ◽  
Gaoxiang Ge
Keyword(s):  
Type Iv Collagen ◽  
Network Formation ◽  
Basement Membranes ◽  
Structural Components ◽  
Collagen Network ◽  
Complex Type ◽  
Form Complex ◽  
Structural Support ◽  
Type Iv ◽  
Covalent Crosslinking

Abstract Collagens form complex networks in the extracellular space that provide structural support and signaling cues to cells. Network-forming type IV collagens are the key structural components of basement membranes. In this review, we discuss how the complexity of type IV collagen networks is established, focusing on collagen α chain selection in type IV collagen protomer and network formation; covalent crosslinking in type IV collagen network stabilization; and the differences between solid-state type IV collagen in the extracellular matrix and soluble type IV collagen fragments. We further discuss how complex type IV collagen networks exert their physiological and pathological functions through cell surface integrin and nonintegrin receptors.

scholarly journals Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network.

1987 ◽  
Vol 105 (6) ◽  
pp. 2559-2568 ◽  
Author(s):  
P D Yurchenco ◽  
G C Ruben
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Thin Sheet ◽  
Great Part ◽  
Molecular Architecture ◽  
Branch Points ◽  
Collagen Network ◽  
Type Iv

To determine molecular architecture of the type IV collagen network in situ, the human amniotic basement membrane has been studied en face in stereo relief by high resolution unidirectional metal shadow casting aided by antibody decoration and morphometry. The appearance of the intact basement membrane is that of a thin sheet in which there are regions of branching strands. Salt extraction further exposes these strands to reveal an extensive irregular polygonal network that can be specifically decorated with gold-conjugated anti-type IV collagen antibody. At high magnification one sees that the network, which contains integral (9-11 nm net diameter) globular domains, is formed in great part by lateral association of monomolecular filaments to form branching strands of variable but narrow diameters. Branch points are variably spaced apart by an average of 45 nm with 4.4 globular domains per micron of strand length. Monomolecular filaments (1.7-nm net diameter) often appear to twist around each other along the strand axis; we propose that super helix formation is an inherent characteristic of lateral assembly. A previous study (Yurchenco, P. D., and H. Furthmayr. 1984. Biochemistry. 23:1839) presented evidence that purified murine type IV collagen dimers polymerize to form polygonal arrays of laterally as well as end-domain-associated molecules. The architecture of this polymer is similar to the network seen in the amnion, with lateral binding a major contributor to each. Thus, to a first approximation, isolated type IV collagen can reconstitute in vitro the polymeric molecular architecture it assumes in vivo.

Evidence for lateral associations in the Type IV collagen network from freeze-dried platinum-carbon replicated amniotic basement membrane

1987 ◽  
Vol 45 ◽  
pp. 968-969
Author(s):  
George C. Ruben ◽  
Peter D. Yurchenco
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Collagen Iv ◽  
Present Knowledge ◽  
Globular Domain ◽  
Collagen Network ◽  
Type Iv ◽  
Interstitial Collagens ◽  
Freeze Dried

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.

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

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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