The predicted collagen-binding domains of Drosophila SPARC are essential for survival and for collagen IV distribution and assembly into basement membranes

AbstractThe assembly of basement membranes (BMs) into tissue-specific morphoregulatory structures requires non-core BM components. Work in Drosophila indicates a principal role of collagen-binding matricellular glycoprotein SPARC (Secreted Protein, Acidic, Rich in Cysteine) in larval fat body BM assembly. We report that SPARC and collagen IV (Col(IV)) first colocalize in the trans-Golgi of hemocytes. Mutating the collagen-binding epitopes of SPARC leads to 2nd instar larval lethality, indicating that SPARC binding to Col(IV) is essential for survival. Analysis of this mutant reveals increased Col(IV) puncta within adipocytes and intense perimeter Col(IV) staining surrounding the fat body as compared to wild-type larvae, reflecting a disruption in chaperone-like activity. In addition, Col(IV) in the wing imaginal disc was absent. Removal of the disulfide bridge in EF-hand2, which is known to enhance Col(IV) binding by SPARC, did not lead to larval lethality; however, a similar but less intense fat body phenotype was observed. Additionally, both SPARC mutants have altered fat body BM pore topography. Wing imaginal disc-derived SPARC did not localize within Col(IV)-rich matrices, indicating a distinct variant. Collectively, these data demonstrate the essential role of Col(IV) chaperone-like activity of SPARC to Drosophila development and indicate tissue-specific variants with differential functions.

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Collagen-binding domains of gelatinase A and thrombospondin-derived peptides impede endocytic clearance of active gelatinase A and promote HT1080 fibrosarcoma cell invasion

Life Sciences ◽

10.1016/j.lfs.2007.11.018 ◽

2008 ◽

Vol 82 (7-8) ◽

pp. 376-382 ◽

Cited By ~ 6

Author(s):

Arnaud Robinet ◽

Hervé Emonard ◽

Laszlo Banyai ◽

Jean-Yves Laronze ◽

Lazlo Patthy ◽

...

Keyword(s):

Cell Invasion ◽

Gelatinase A ◽

Collagen Binding ◽

Fibrosarcoma Cell ◽

Binding Domains

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Vitamin A Deficiency Alters the Structure and Collagen IV Composition of Rat Renal Basement Membranes

Journal of Nutrition ◽

10.1093/jn/135.4.695 ◽

2005 ◽

Vol 135 (4) ◽

pp. 695-701 ◽

Cited By ~ 19

Author(s):

M. Pilar Marín ◽

Guillermo Esteban-Pretel ◽

Ruth Alonso ◽

Yoshikazu Sado ◽

Teresa Barber ◽

...

Keyword(s):

Vitamin A ◽

Vitamin A Deficiency ◽

Collagen Iv ◽

Basement Membranes

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Extracellular chloride signals collagen IV network assembly during basement membrane formation

The Journal of Cell Biology ◽

10.1083/jcb.201510065 ◽

2016 ◽

Vol 213 (4) ◽

pp. 479-494 ◽

Cited By ~ 32

Author(s):

Christopher F. Cummings ◽

Vadim Pedchenko ◽

Kyle L. Brown ◽

Selene Colon ◽

Mohamed Rafi ◽

...

Keyword(s):

Cell Culture ◽

Basement Membrane ◽

Collagen Iv ◽

Atomic Level ◽

Basement Membranes ◽

Tissue Architecture ◽

Dynamic Interactions ◽

Conformational Switch ◽

And Function ◽

Fundamental Mechanism

Basement membranes are defining features of the cellular microenvironment; however, little is known regarding their assembly outside cells. We report that extracellular Cl− ions signal the assembly of collagen IV networks outside cells by triggering a conformational switch within collagen IV noncollagenous 1 (NC1) domains. Depletion of Cl− in cell culture perturbed collagen IV networks, disrupted matrix architecture, and repositioned basement membrane proteins. Phylogenetic evidence indicates this conformational switch is a fundamental mechanism of collagen IV network assembly throughout Metazoa. Using recombinant triple helical protomers, we prove that NC1 domains direct both protomer and network assembly and show in Drosophila that NC1 architecture is critical for incorporation into basement membranes. These discoveries provide an atomic-level understanding of the dynamic interactions between extracellular Cl− and collagen IV assembly outside cells, a critical step in the assembly and organization of basement membranes that enable tissue architecture and function. Moreover, this provides a mechanistic framework for understanding the molecular pathobiology of NC1 domains.

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Anti-Ace monoclonal antibody reduces Enterococcus faecalis aortic valve infection in a rat infective endocarditis model

Pathogens and Disease ◽

10.1093/femspd/fty084 ◽

2018 ◽

Vol 76 (8) ◽

Cited By ~ 1

Author(s):

Kavindra V Singh ◽

Kenneth L Pinkston ◽

Peng Gao ◽

Barrett R Harvey ◽

Barbara E Murray

Keyword(s):

Monoclonal Antibody ◽

Infective Endocarditis ◽

Enterococcus Faecalis ◽

Collagen Iv ◽

Aortic Valves ◽

Collagen Binding ◽

Passive Protection ◽

A Cell ◽

Pre Treatment

AbstractAce (Adhesin to collagen from Enterococcus faecalis) is a cell-wall anchored protein that is expressed conditionally and is important for virulence in a rat infective endocarditis (IE) model. Previously, we showed that rats immunized with the collagen binding domain of Ace (domain A), or administered anti-Ace domain A polyclonal antibody, were less susceptible to E. faecalis endocarditis than sham-immunized controls. In this work, we demonstrated that a sub nanomolar monoclonal antibody (mAb), anti-Ace mAb70, significantly diminished E. faecalis binding to ECM collagen IV in in vitro adherence assays and that, in the endocarditis model, anti-Ace mAb70 pre-treatment significantly reduced E. faecalis infection of aortic valves. The effectiveness of anti-Ace mAb against IE in the rat model suggests it might serve as a beneficial agent for passive protection against E. faecalis infections.

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Expression of collagen type IV in human kidney during prenatal development

Vojnosanitetski pregled ◽

10.2298/vsp200927111p ◽

2020 ◽

pp. 111-111

Author(s):

Vladimir Petrovic ◽

Ivan Nikolic ◽

Marko Jovic ◽

Vladimir Zivkovic ◽

Miodrag Jocic ◽

...

Keyword(s):

Type Iv Collagen ◽

Collagen Type ◽

Kidney Tissue ◽

Volume Density ◽

Collagen Iv ◽

Basement Membranes ◽

Collagen Type Iv ◽

Type Iv ◽

Metanephric Kidney ◽

Collecting System

Background / Aim. Type IV collagen belongs to the group of non-fibrillar collagens and is an important component of the basement membranes where it accounts for approximately 50% of its structural elements. The aim of the paper was to describe the expression and distribution of collagen type IV in embryonic and fetal metanephric kidney, and to determine the volume density of collagen type IV in kidney tissue in each trimester of development. Methods. The material consisted of 19 human embryos/fetuses, in the gestational age from 8th to 37th week. Kidney tissue specimens were routinely processed to paraffin molds and stained with hematoxylin and eosin and immunohistochemically using polyclonal anti-collagen IV antibody. Stained slides were examined using light microscope and images of the selected areas, under different lens magnification were captured with digital camera. Volume density of collagen type IV was determined by using ImageJ 1.48v and a plugin of the software which inserted a grid system with 336 points. For the data comparison One-Way Analysis of Variance was used. Results. Strong collagen IV immunopositivity was seen in all specimens, with a distribution in the basement membranes of urinary bud, parietal leaf of Bowman?s capsule, glomerular basement membrane, basement membrane of interstitial blood vessels, and basement membranes of nephron tubules and collecting ducts. No statistically significant difference in the volume density of type IV collagen was found between the different trimesters of development. Conclusion. The synthesis and secretion of collagen type IV simultaneously follows the development of nephron structures, collecting system and blood vessels. The volume density of collagen type IV remains constant throughout all the trimesters of metanephric kidney development, indicating that it plays a crucial role in normal development of nephron and collecting system structures, as well as in maintaining the normal kidney function.

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Isolation and characterization of collagen-binding domains from human von Willebrand factor

Molecular Genetics Microbiology and Virology ◽

10.3103/s0891416809030082 ◽

2009 ◽

Vol 24 (3) ◽

pp. 150-154 ◽

Cited By ~ 1

Author(s):

N. E. Sharapova ◽

A. P. Kotnova ◽

Z. M. Galushkina ◽

N. N. Poletaeva ◽

N. V. Lavrova ◽

...

Keyword(s):

Von Willebrand Factor ◽

Collagen Binding ◽

Binding Domains ◽

Isolation And Characterization ◽

Von Willebrand ◽

Willebrand Factor

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Ca 2+ ‐induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation

FEBS Journal ◽

10.1111/febs.14611 ◽

2018 ◽

Vol 285 (17) ◽

pp. 3254-3269 ◽

Cited By ~ 2

Author(s):

Perry Caviness ◽

Ryan Bauer ◽

Keisuke Tanaka ◽

Katarzyna Janowska ◽

Jeffrey Randall Roeser ◽

...

Keyword(s):

Collagen Fibril ◽

Fibril Formation ◽

Collagen Binding ◽

Binding Domains

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Peroxidasin-mediated bromine enrichment of basement membranes

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.2007749117 ◽

2020 ◽

Vol 117 (27) ◽

pp. 15827-15836

Author(s):

Cuiwen He ◽

Wenxin Song ◽

Thomas A. Weston ◽

Caitlyn Tran ◽

Ira Kurtz ◽

...

Keyword(s):

Basement Membrane ◽

Knockout Mice ◽

Structural Integrity ◽

Secondary Ion Mass Spectrometry ◽

Human Kidney ◽

Collagen Iv ◽

Basement Membranes ◽

Basement Membrane Protein ◽

Mammalian Tissues ◽

Cross Links

Bromine and peroxidasin (an extracellular peroxidase) are essential for generating sulfilimine cross-links between a methionine and a hydroxylysine within collagen IV, a basement membrane protein. The sulfilimine cross-links increase the structural integrity of basement membranes. The formation of sulfilimine cross-links depends on the ability of peroxidasin to use bromide and hydrogen peroxide substrates to produce hypobromous acid (HOBr). Once a sulfilimine cross-link is created, bromide is released into the extracellular space and becomes available for reutilization. Whether the HOBr generated by peroxidasin is used very selectively for creating sulfilimine cross-links or whether it also causes oxidative damage to bystander molecules (e.g., generating bromotyrosine residues in basement membrane proteins) is unclear. To examine this issue, we used nanoscale secondary ion mass spectrometry (NanoSIMS) imaging to define the distribution of bromine in mammalian tissues. We observed striking enrichment of bromine (79Br,81Br) in basement membranes of normal human and mouse kidneys. In peroxidasin knockout mice, bromine enrichment of basement membranes of kidneys was reduced by ∼85%. Proteomic studies revealed bromination of tyrosine-1485 in the NC1 domain of α2 collagen IV from kidneys of wild-type mice; the same tyrosine was brominated in collagen IV from human kidney. Bromination of tyrosine-1485 was reduced by >90% in kidneys of peroxidasin knockout mice. Thus, in addition to promoting sulfilimine cross-links in collagen IV, peroxidasin can also brominate a bystander tyrosine. Also, the fact that bromine enrichment is largely confined to basement membranes implies that peroxidasin activity is largely restricted to basement membranes in mammalian tissues.

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