Glomerular Basement Membrane

Gunwar, Sripad; Ballester, Fernando; Noelken, Milton E.; Sado, Yoshikazu; Ninomiya, Yoshifumi; Hudson, Billy G.

doi:10.1074/jbc.273.15.8767

Cited by 209 publications

(74 citation statements)

References 62 publications

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“…For twodimensional PAGE, the NC1 hexamers (2-10 g) were separated in the first dimension by non-equilibrium pH gradient electrophoresis (22) and then in the second dimension by SDS-PAGE using a 10 -22% gel gradient. The gels were silver-stained or transferred to nitrocellulose for Western blot analysis.…”

Section: Methodsmentioning

confidence: 99%

“…2a). Moreover, digestion of glomerular BM at 4°C followed by digestion at 25°C differentially solubilized two distinct networks, one composed of the ␣1 and ␣2 chains and the other composed of the ␣3, ␣4, and ␣5 chains (3,4). Thus, pseudolysin cleavage can reveal information about the protomer and network organization of chains.…”

Section: Arrangement Of Chains In Protomers and Networkmentioning

confidence: 99%

“…Analysis of the Type IV Collagen Networks from Aorta BM by Digestion with Pseudolysin-Our previous studies (4,23) showed that pseudolysin digestion solubilizes truncated protomers of collagen IV with retention of a portion of the triplehelical domain and the complete NC1-NC1 connection between protomers (Fig. 2a).…”

Section: Arrangement Of Chains In Protomers and Networkmentioning

confidence: 99%

“…In this study, bovine aorta and bladder BMs were chosen as prototypes for the smooth muscle BMs of the vasculature and viscera because bovine tissues are amenable for isolation of sufficient quantities of type IV collagen for biochemical analyses (3,4,17,23). Immunostaining with chain-specific mAbs ( Fig.…”

Section: Chain Composition Of Type IV Collagen Of Bovine Smooth Musclmentioning

confidence: 99%

“…Second, the NC1 domain confers specificity to the chain-specific assembly of networks (3); thus, yet unidentified recognition sequences must exist within the NC1 domain that direct the selection of chains to form triple-helical protomers and of triple-helical protomers to form networks. For instance, although the ␣1-␣5 chains are coexpressed in glomerular BM, they segregate into an ␣1⅐␣2 network and a disulfide cross-linked ␣3⅐␣4⅐␣5 network, characterized by loops and supercoiling (4). The existence of the latter network provides an explanation for the glomerular BM defect in Alport's syndrome, in which mutations in the genes encoding any of the ␣3, ␣4, and ␣5 chains perturb the assembly of the ␣3⅐␣4⅐␣5 network with the consequent loss of all three chains and progressive renal failure (3,4).…”

mentioning

confidence: 99%

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The NC1 Domain of Collagen IV Encodes a Novel Network Composed of the α1, α2, α5, and α6 Chains in Smooth Muscle Basement Membranes

Borza¹,

Bondar²,

Ninomiya³

et al. 2001

Journal of Biological Chemistry

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133

119

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Type IV collagen, the major component of basement membranes (BMs), is a family of six homologous chains (␣1-␣6) that have a tissue-specific distribution. The chains assemble into supramolecular networks that differ in the chain composition. In this study, a novel network was identified and characterized in the smooth muscle BMs of aorta and bladder. The noncollagenous (NC1) hexamers solubilized by collagenase digestion were fractionated by affinity chromatography using monoclonal antibodies against the ␣5 and ␣6 NC1 domains and then characterized by two-dimensional gel electrophoresis and Western blotting. Both BMs were found to contain a novel ␣1⅐␣2⅐␣5⅐␣6 network besides the classical ␣1⅐␣2 network. The ␣1⅐␣2⅐␣5⅐␣6 network represents a new arrangement in which a protomer (triplehelical isoform) containing the ␣5 and ␣6 chains is linked through NC1-NC1 interactions to an adjoining protomer composed of the ␣1 and ␣2 chains. Re-association studies revealed that the NC1 domains contain recognition sequences sufficient to encode the assembly of both networks. These findings, together with previous ones, indicate that the six chains of type IV collagen are distributed in three major networks (␣1⅐␣2, ␣3⅐␣4⅐␣5, and ␣1⅐␣2⅐␣5⅐␣6) whose chain composition is encoded by the NC1 domains. The existence of the ␣1⅐␣2⅐␣5⅐␣6 network provides a molecular explanation for the concomitant loss of ␣5 and ␣6 chains from the BMs of patients with X-linked Alport's syndrome. The basement membrane (BM),1 a continuous sheet of extracellular matrix, separates epithelial cells from the underlying stroma and plays important roles in normal biological functions (such as cell adhesion, growth, and differentiation; tissue repair; and molecular ultrafiltration) as well as in pathological events (such as cancer cell invasion and metastasis). Moreover, degradation and de novo synthesis of vascular BMs are critical events in the angiogenesis processes. BMs function is impaired in hereditary and acquired diseases in which type IV collagen is affected, including Alport's syndrome, a hereditary form of progressive renal disease; diffuse leiomyomatosis, a benign proliferation of smooth muscle cells; and Goodpasture syndrome, an anti-type IV collagen autoimmune disease (1).Type IV collagen is the major structural component of the BM, and it consists of a family of six homologous ␣(IV) chains, designated ␣1-␣6 (1). Each chain is characterized by a long collagenous domain of ϳ1400 residues of Gly-X-Y repeats, interrupted by ϳ20 short noncollagenous sequences, and by a noncollagenous (NC1) domain of ϳ230 residues at the carboxyl terminus. Three ␣(IV) chains assemble into triple-helical molecules (protomers) that further associate to form supramolecular networks by dimerization at the carboxyl terminus through NC1 domains and by formation of tetramers at the amino terminus (2). The chain composition, and thus the properties of the type IV collagen networks are influenced by two factors. First, the chain composition of networks is limited by chain availability...

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Section: Methodsmentioning

confidence: 99%

Section: Arrangement Of Chains In Protomers and Networkmentioning

confidence: 99%

Section: Arrangement Of Chains In Protomers and Networkmentioning

confidence: 99%

Section: Chain Composition Of Type IV Collagen Of Bovine Smooth Musclmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

The NC1 Domain of Collagen IV Encodes a Novel Network Composed of the α1, α2, α5, and α6 Chains in Smooth Muscle Basement Membranes

Borza¹,

Bondar²,

Ninomiya³

et al. 2001

Journal of Biological Chemistry

Self Cite

133

119

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Differential expression of collagen type IV alpha-chains in the tubulointerstitial compartment in experimental chronic serum sickness nephritis

et al. 1999

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Cell‐Derived Extracellular Matrix‐Rich Biomimetic Substrate Supports Podocyte Proliferation, Differentiation, and Maintenance of Native Phenotype

Satyam

Tsokos

Tresback

et al. 2020

Adv Funct Materials

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Current technologies and available scaffold materials do not support longterm cell viability, differentiation, and maintenance of podocytes, the ultraspecialized kidney resident cells that are responsible for the filtration of the blood. A new platform which imitates the native kidney microenvironment by decellularizing fibroblasts grown on surfaces with macromolecular crowding is developed. Human immortalized podocytes cultured on this platform display superior viability and metabolic activity up to 28 days compared to podocytes cultured on tissue culture plastic surfaces. The new platform displays a softer surface and an abundance of growth factors and associated molecules. More importantly, it enables podocytes to display molecules responsible for their structure and function and a superior development of intercellular connections/interdigitations, consistent with maturation. The new platform can be used to study podocyte biology, test drug toxicity, and determine whether sera from patients with podocytopathies are involved in the expression of glomerular pathology.

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Glomerular Basement Membrane

Cited by 209 publications

References 62 publications

The NC1 Domain of Collagen IV Encodes a Novel Network Composed of the α1, α2, α5, and α6 Chains in Smooth Muscle Basement Membranes

The NC1 Domain of Collagen IV Encodes a Novel Network Composed of the α1, α2, α5, and α6 Chains in Smooth Muscle Basement Membranes

Differential expression of collagen type IV alpha-chains in the tubulointerstitial compartment in experimental chronic serum sickness nephritis

Cell‐Derived Extracellular Matrix‐Rich Biomimetic Substrate Supports Podocyte Proliferation, Differentiation, and Maintenance of Native Phenotype

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