Peroxidasin: a novel enzyme-matrix protein of Drosophila development.

Nelson, Robert E.; Fessler, Liselotte I.; Takagi, Yasuaki; Blumberg, Bruce; Keene, Douglas R.; Olson, Pamela F.; Parker, Carol; Fessler, John H.

doi:10.1002/j.1460-2075.1994.tb06649.x

Cited by 265 publications

(223 citation statements)

References 48 publications

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“…Close to its C-terminus, the Drosophila PXDN contains an amphipatic -helical region, which was proposed to form homotrimeric coiled coil (6). A homologous region between amino acids 1383 and 1411 is also recognizable in the mammalian protein and we assume that trimerization via this region positions the C736 and C1315 residues to form intermolecular disulfide bonds leading to the assembly of a stabilized PXDN trimer.…”

Section: Discussionmentioning

confidence: 95%

Structure–function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking

Lázár

Péterfi

Sirokmány

et al. 2015

Free Radical Biology and Medicine

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Basement membranes provide structural support and convey regulatory signals to cells in diverse tissues. Assembly of collagen IV into a sheet-like network is a fundamental mechanism during the formation of basement membranes. Peroxidasin (PXDN) was recently described to catalyze crosslinking of collagen IV through the formation of sulfilimine bonds.Despite the significance of this pathway in tissue genesis, our understanding of PXDN function is far from complete. In this work we demonstrate that collagen IV crosslinking is a physiological function of mammalian PXDN. Moreover, we carried out structure-function analysis of PXDN to get a better insight into its role in collagen IV synthesis. We identify conserved cysteines in PXDN which mediate the oligomerization of the protein into a trimeric complex. We also demonstrate that oligomerization is not an absolute requirement for enzymatic activity but optimal collagen IV coupling is only catalyzed by the PXDN trimers.Localization experiments of different PXDN mutants in two different cell models revealed that PXDN oligomers, but not monomers, adhere on cell-surface in "hot spots", which represent previously unknown locations of collagen IV crosslinking.

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Section: Discussionmentioning

confidence: 95%

Structure–function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking

Lázár

Péterfi

Sirokmány

et al. 2015

Free Radical Biology and Medicine

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“…Therefore, another possible function of the 120-kDa protein is recognition of the extracellular matrix of larval tissues, which leads to tissue disintegration. It has been shown that scavenger receptors are implicated in cell±matrix interactions, suggesting this possibility [35,36].…”

Section: Discussionmentioning

confidence: 99%

A novel hemocyte‐specific membrane protein of Sarcophaga (flesh fly)

Hori

Kobayashi

Natori

2000

European Journal of Biochemistry

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Extensive tissue remodeling takes place during metamorphosis of holometabolous insects. It has been shown that hemocytes play crucial roles in the recognition and elimination of apoptotic cells and larval tissue fragments produced during metamorphosis. We report the immunoaffinity purification, cDNA cloning, and characterization of a prepupal hemocyte membrane protein of Sarcophaga (flesh fly) with a molecular mass of 120 kDa. This protein is a novel type I transmembrane protein with 18 repeats of an epidermal growth factor-like domain in the predicted extracellular region. Expression of the protein was restricted exclusively to prepupal hemocytes. This protein is suggested to be a scavenger receptor for tissue remodeling.

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“…The trimeric Drosophila protein peroxidasin has also been found to contain a procollagen module near its proposed oligomerization site (54). TSP1 lacking C was primarily expressed as dimers and monomers by mouse NIH 3T3 cells (13).…”

Section: Table IIImentioning

confidence: 99%

Physical Characterization of the Procollagen Module of Human Thrombospondin 1 Expressed in Insect Cells

Misenheimer

Huwiler

Annis

et al. 2000

Journal of Biological Chemistry

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Thrombospondin 1 (TSP1) is a homotrimeric glycoprotein composed of 150-kDa subunits connected by disulfide bridges. The procollagen module of thrombospondin 1 has been implicated in antiangiogenic activity. Procollagen modules are found in a number of extracellular proteins and are identifiable by 10 cysteines with characteristic spacing. We expressed and studied the procollagen module (C) of human TSP1, both by itself and in the context of the adjoining oligomerization sequence (o) and N-terminal module (N). The coding sequences were introduced into baculoviruses along with an N-terminal signal sequence and C-terminal polyhistidine tag. Proteins were purified from conditioned medium of infected insect cells by nickel-chelate chromatography. NoC is a disulfide bonded trimer and cleaves readily at a site of preferential proteolysis to yield monomeric N and trimeric oC. These are known properties of full-length TSP1. Mass spectroscopy indicated that C is N-glycosylated, and all 10 cysteine residues of C are in disulfides. By equilibrium ultracentrifugation, C is a monomer in physiological salt solution. Circular dichroism, intrinsic fluorescence, and differential scanning calorimetry experiments suggest that the stability of C is determined by the disulfides. The two tryptophans of C are in a polar, exposed environment as assessed by iodide fluorescence quenching and solvent perturbation. The oC far UV circular dichroism spectrum could be modeled as the sum of C and a coiled-coil oligomerization domain. The results indicate that the recombinant C folds autonomously into its native structure, and trimerization of the modules in TSP1 does not perturb their structures.

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Peroxidasin: a novel enzyme-matrix protein of Drosophila development.

Cited by 265 publications

References 48 publications

Structure–function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking

Structure–function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking

A novel hemocyte‐specific membrane protein of Sarcophaga (flesh fly)

Physical Characterization of the Procollagen Module of Human Thrombospondin 1 Expressed in Insect Cells

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