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Journal ArticleDOI

Rat myoblast fusion requires metalloendoprotease activity

Christine B. Couch, +1 more
- 01 Jan 1983 - 
- Vol. 32, Iss: 1, pp 257-265
TLDR
The calcium-dependent fusion of cultured rat myoblasts to multinucleate myotubes appears to require the activity of a neutral metalloendoprotease at the time of fusion, which is inhibited by the same compounds that prevent fusion.
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This article is published in Cell.The article was published on 1983-01-01. It has received 139 citations till now. The article focuses on the topics: Myoblast fusion.

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Citations
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Journal ArticleDOI

A metalloprotease-disintegrin participating in myoblast fusion.

TL;DR: Three new, myoblast-expressed gene products, meltrin-αβ and γ, with homology to both viper haemorrhagic factors and fertilin (PH-30)14,15, a membrane protein involved in eggá¤-sperm fusion are reported.
Journal ArticleDOI

Transfection of a DNA locus that mediates the conversion of 10T1 2 fibroblasts to myoblasts

TL;DR: Results indicate that an azacytidine-induced structural modification (presumably demethylation) in the DNA of a single locus is sufficient to convert 10T1/2 cells into determined myoblasts.
Journal ArticleDOI

The fusion of myoblasts

TL;DR: Myoblast fusion provides a naturally occurring process in which mechanistic proposals from the study of fusion in moder fusion systems can be tested and profitably applied to appropriate vesicular model systems.
Journal ArticleDOI

Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: a study in experimentally injured and mdx muscles.

TL;DR: The data allow the correlation of the differential expression of pro and/or active forms of M MP-2 and MMP-9 with different stages of the degeneration-regeneration process: MMP -9 expression is related to the inflammatory response and probably to the activation of satellite cells, whereas Mmp-2 activation is concomitant with the regeneration of new myofibers.
Journal ArticleDOI

Neutral metalloendopeptidase in human lung tissue and cultured cells.

TL;DR: The distribution of a neutral metalloendopeptidase (NEP) in human lung tissue and cultured cells was compared with that of angiotensin I converting enzyme (ACE), which suggests that they act sequentially on circulating peptides or those released within microvascular beds.
References
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Book

Critical Stability Constants

TL;DR: Erratum to: Aminocarboxylic Acids to: Iminodiacetic Acid Derivatives to: Peptides to: Aliphatic Amines to: Protonation Values for other Ligands.
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.

TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
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Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents

TL;DR: A hypothetical model of the active site of angiotensin-converting enzyme, based on known chemical and kinetic properties of the enzyme, has enabled a new class of potent and specific inhibitors, carboxyalkanoyl and mercaptoalkanoysl derivatives of proline, to be designed.
Journal ArticleDOI

Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide.

TL;DR: The increase in infectivity caused by proteolytic cleavage of the HA polypeptide provides a biochemical explanation for the previously observed enhancement of plaquing efficiency of influenza viruses by the inclusion of pancreation or trypsin in the agar overlay.
Journal ArticleDOI

The timing of calcium action during neuromuscular transmission.

TL;DR: Brief depolarizing pulses applied to a motor nerve ending cause packets of acetylcholine to be released and evoke end‐plate potentials (e.p.s), provided calcium ions are present in the extracellular fluid.
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