scholarly journals A fat body-derived apical extracellular matrix enzyme is transported to the tracheal lumen and is required for tube morphogenesis in Drosophila

Development ◽  
2014 ◽  
Vol 141 (21) ◽  
pp. 4104-4109 ◽  
Author(s):  
B. Dong ◽  
G. Miao ◽  
S. Hayashi
Keyword(s):  
Extracellular Matrix ◽  
Fat Body ◽  
Tracheal Lumen ◽  
Tube Morphogenesis ◽  
Matrix Enzyme

Juvenile hormone signaling promotes ovulation and maintains egg shape by inducing expression of extracellular matrix genes

2021 ◽  
Vol 118 (39) ◽  
pp. e2104461118
Author(s):  
Wei Luo ◽  
Suning Liu ◽  
Wenqiang Zhang ◽  
Liu Yang ◽  
Jianhua Huang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Extracellular Matrix ◽  
Muscle Contraction ◽  
Juvenile Hormone ◽  
Fat Body ◽  
Collagen Iv ◽  
Hormone Signaling ◽  
Gonadotropic Hormone ◽  
Egg Shape ◽  
Insect Reproduction

It is well documented that the juvenile hormone (JH) can function as a gonadotropic hormone that stimulates vitellogenesis by activating the production and uptake of vitellogenin in insects. Here, we describe a phenotype associated with mutations in the Drosophila JH receptor genes, Met and Gce: the accumulation of mature eggs with reduced egg length in the ovary. JH signaling is mainly activated in ovarian muscle cells and induces laminin gene expression in these cells. Meanwhile, JH signaling induces collagen IV gene expression in the adult fat body, from which collagen IV is secreted and deposited onto the ovarian muscles. Laminin locally and collagen IV remotely contribute to the assembly of ovarian muscle extracellular matrix (ECM); moreover, the ECM components are indispensable for ovarian muscle contraction. Furthermore, ovarian muscle contraction externally generates a mechanical force to promote ovulation and maintain egg shape. This work reveals an important mechanism for JH-regulated insect reproduction.

scholarly journals Overexpression of Soluble Recombinant Human Lysyl Oxidase by Using Solubility Tags: Effects on Activity and Solubility

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Madison A. Smith ◽  
Jesica Gonzalez ◽  
Anjum Hussain ◽  
Rachel N. Oldfield ◽  
Kathryn A. Johnston ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Enzymatic Activity ◽  
Lysyl Oxidase ◽  
The Other ◽  
Glutathione S Transferase ◽  
E Coli ◽  
N Terminus ◽  
Low Solubility ◽  
Total Enzyme ◽  
Matrix Enzyme

Lysyl oxidase is an important extracellular matrix enzyme that has not been fully characterized due to its low solubility. In order to circumvent the low solubility of this enzyme, three solubility tags (Nus-A, Thioredoxin (Trx), and Glutathione-S-Transferase (GST)) were engineered on the N-terminus of mature lysyl oxidase. Total enzyme yields were determined to be 1.5 mg for the Nus-A tagged enzyme (0.75 mg/L of media), 7.84 mg for the Trx tagged enzyme (3.92 mg/L of media), and 9.33 mg for the GST tagged enzyme (4.67 mg/L of media). Enzymatic activity was calculated to be 0.11 U/mg for the Nus-A tagged enzyme and 0.032 U/mg for the Trx tagged enzyme, and no enzymatic activity was detected for the GST tagged enzyme. All three solubility-tagged forms of the enzyme incorporated copper; however, the GST tagged enzyme appears to bind adventitious copper with greater affinity than the other two forms. The catalytic cofactor, lysyl tyrosyl quinone (LTQ), was determined to be 92% for the Nus-A and Trx tagged lysyl oxidase using the previously reported extinction coefficient of 15.4 mM−1 cm−1. No LTQ was detected for the GST tagged lysyl oxidase. Given these data, it appears that Nus-A is the most suitable tag for obtaining soluble and active recombinant lysyl oxidase from E. coli culture.

scholarly journals Tiggrin, a novel Drosophila extracellular matrix protein that functions as a ligand for Drosophila alpha PS2 beta PS integrins

Development ◽  
1994 ◽  
Vol 120 (7) ◽  
pp. 1747-1758 ◽  
Author(s):  
F.J. Fogerty ◽  
L.I. Fessler ◽  
T.A. Bunch ◽  
Y. Yaron ◽  
C.G. Parker ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Fat Body ◽  
Cell Spreading ◽  
Embryo Cell ◽  
Extracellular Matrix Protein ◽  
Recognition Sequence ◽  
Biochemical Purification ◽  
Rgd Peptides ◽  
Coated Surfaces

Genetic and other studies of Drosophila integrins have implicated these extracellular matrix receptors in various morphogenetic events, but identification of their endogenous ligands has been elusive. We report the biochemical purification and cloning of tiggrin, a novel extracellular matrix protein from Drosophila. This 255 × 10(3) M(r) polypeptide contains the potential integrin recognition sequence Arg-Gly-Asp (RGD) and 16 repeats of a novel 73–77 amino acid motif. The tiggrin gene is at chromosome locus 26D1-2 and is expressed by embryonic hemocytes and fat body cells. Tiggrin protein is detected in matrices, especially at muscle attachment sites that also strongly express integrins. Tiggrin-coated surfaces support primary embryo cell culture and provide excellent substrates for alpha PS2 beta PS integrin-mediated cell spreading. Soluble RGD-peptides inhibit this cell spreading.

scholarly journals Extracellular matrix protein N-glycosylation mediates immune self-tolerance in Drosophila melanogaster

2021 ◽  
Vol 118 (39) ◽  
pp. e2017460118
Author(s):  
Nathan T. Mortimer ◽  
Mary L. Fischer ◽  
Ashley L. Waring ◽  
Pooja KR ◽  
Balint Z. Kacsoh ◽  
...  
Keyword(s):  
Immune Response ◽  
Extracellular Matrix ◽  
Matrix Protein ◽  
Fat Body ◽  
Extracellular Matrix Proteins ◽  
Recognition System ◽  
Janus Kinase ◽  
Matrix Proteins ◽  
Extracellular Matrix Protein ◽  
Self Tolerance

In order to respond to infection, hosts must distinguish pathogens from their own tissues. This allows for the precise targeting of immune responses against pathogens and also ensures self-tolerance, the ability of the host to protect self tissues from immune damage. One way to maintain self-tolerance is to evolve a self signal and suppress any immune response directed at tissues that carry this signal. Here, we characterize the Drosophila tuSz1 mutant strain, which mounts an aberrant immune response against its own fat body. We demonstrate that this autoimmunity is the result of two mutations: 1) a mutation in the GCS1 gene that disrupts N-glycosylation of extracellular matrix proteins covering the fat body, and 2) a mutation in the Drosophila Janus Kinase ortholog that causes precocious activation of hemocytes. Our data indicate that N-glycans attached to extracellular matrix proteins serve as a self signal and that activated hemocytes attack tissues lacking this signal. The simplicity of this invertebrate self-recognition system and the ubiquity of its constituent parts suggests it may have functional homologs across animals.

The Structure and Development of Microbodies in the Fat Body and other Tissues of an Insect (Calpodes Ethlius)

1970 ◽  
Vol 28 ◽  
pp. 148-149
Author(s):  
M. Locke ◽  
J. T. McMahon
Keyword(s):  
Electron Microscopy ◽  
Liquid Crystals ◽  
Fat Body ◽  
Competitive Inhibitor ◽  
Dense Core ◽  
Urate Oxidase ◽  
Blood Proteins ◽  
Free Base ◽  
The Core ◽  
The Matrix

The fat body of insects has always been compared functionally to the liver of vertebrates. Both synthesize and store glycogen and lipid and are concerned with the formation of blood proteins. The comparison becomes even more apt with the discovery of microbodies and the localization of urate oxidase and catalase in insect fat body.The microbodies are oval to spherical bodies about 1μ across with a depression and dense core on one side. The core is made of coiled tubules together with dense material close to the depressed membrane. The tubules may appear loose or densely packed but always intertwined like liquid crystals, never straight as in solid crystals (Fig. 1). When fat body is reacted with diaminobenzidine free base and H2O2 at pH 9.0 to determine the distribution of catalase, electron microscopy shows the enzyme in the matrix of the microbodies (Fig. 2). The reaction is abolished by 3-amino-1, 2, 4-triazole, a competitive inhibitor of catalase. The fat body is the only tissue which consistantly reacts positively for urate oxidase. The reaction product is sharply localized in granules of about the same size and distribution as the microbodies. The reaction is inhibited by 2, 6, 8-trichloropurine, a competitive inhibitor of urate oxidase.

Cardiac myocytes cultured on a basement membrane extract of the ehs tumor

1986 ◽  
Vol 44 ◽  
pp. 270-271
Author(s):  
L. Terracio ◽  
A. Dewey ◽  
K. Rubin ◽  
T.K. Borg
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Cardiac Myocytes ◽  
Normal Tissue ◽  
Cell Spreading ◽  
Collagen Iv ◽  
Basement Membrane Extract ◽  
Membrane Extract ◽  
Growth Development ◽  
Multicellular Organisms

The recognition and interaction of cells with the extracellular matrix (ECM) effects the normal physiology as well as the pathology of all multicellular organisms. These interactions have been shown to influence the growth, development, and maintenance of normal tissue function. In previous studies, we have shown that neonatal cardiac myocytes specifically interacts with a variety of ECM components including fibronectin, laminin, and collagens I, III and IV. Culturing neonatal myocytes on laminin and collagen IV induces an increased rate of both cell spreading and sarcomerogenesis.

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