- Digits and Muscles: Topology-Directed Muscle Attachment

2015 ◽  
pp. 78-83
Keyword(s):  
Muscle Attachment

Morphology of muscle attachment sites and microarhitecture of underlying bone as the markers of physical activities of past populations

2013 ◽  
Author(s):  
Ksenija Djukic ◽  
Petar Milovanovic ◽  
Michael Hahn ◽  
Bjoern Busse ◽  
Michael Amling ◽  
...  
Keyword(s):  
Physical Activities ◽  
Muscle Attachment ◽  
Attachment Sites ◽  
Muscle Attachment Sites

scholarly journals Mutations Affecting Nerve Attachment of Caenorhabditis elegans

Genetics ◽  
2001 ◽  
Vol 157 (4) ◽  
pp. 1611-1622 ◽  
Author(s):  
Go Shioi ◽  
Michinari Shoji ◽  
Masashi Nakamura ◽  
Takeshi Ishihara ◽  
Isao Katsura ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Nerve Cord ◽  
Ventral Nerve Cord ◽  
Body Wall ◽  
The Body ◽  
Genetic Loci ◽  
Muscle Attachment ◽  
C Elegans ◽  
Ventral Cord ◽  
Excretory Canal

Abstract Using a pan-neuronal GFP marker, a morphological screen was performed to detect Caenorhabditis elegans larval lethal mutants with severely disorganized major nerve cords. We recovered and characterized 21 mutants that displayed displacement or detachment of the ventral nerve cord from the body wall (Ven: ventral cord abnormal). Six mutations defined three novel genetic loci: ven-1, ven-2, and ven-3. Fifteen mutations proved to be alleles of previously identified muscle attachment/positioning genes, mup-4, mua-1, mua-5, and mua-6. All the mutants also displayed muscle attachment/positioning defects characteristic of mua/mup mutants. The pan-neuronal GFP marker also revealed that mutants of other mua/mup loci, such as mup-1, mup-2, and mua-2, exhibited the Ven defect. The hypodermis, the excretory canal, and the gonad were morphologically abnormal in some of the mutants. The pleiotropic nature of the defects indicates that ven and mua/mup genes are required generally for the maintenance of attachment of tissues to the body wall in C. elegans.

A novel basic helix-loop-helix protein is expressed in muscle attachment sites of the Drosophila epidermis

1994 ◽  
Vol 14 (6) ◽  
pp. 4145-4154
Author(s):  
P Armand ◽  
A C Knapp ◽  
A J Hirsch ◽  
E F Wieschaus ◽  
M D Cole
Keyword(s):  
Distinct Pattern ◽  
Bhlh Protein ◽  
Muscle Attachment ◽  
Muscle Creatine Kinase ◽  
Basic Helix Loop Helix ◽  
Helix Loop Helix ◽  
Attachment Sites ◽  
Bhlh Genes ◽  
Somatic Muscles ◽  
Muscle Attachment Sites

We have found that a novel basic helix-loop-helix (bHLH) protein is expressed almost exclusively in the epidermal attachments sites for the somatic muscles of Drosophila melanogaster. A Drosophila cDNA library was screened with radioactively labeled E12 protein, which can dimerize with many HLH proteins. One clone that emerged from this screen encoded a previously unknown protein of 360 amino acids, named delilah, that contains both basic and HLH domains, similar to a group of cellular transcription factors implicated in cell type determination. Delilah protein formed heterodimers with E12 that bind to the muscle creatine kinase promoter. In situ hybridization with the delilah cDNA localized the expression of the gene to a subset of cells in the epidermis which form a distinct pattern involving both the segmental boundaries and intrasegmental clusters. This pattern was coincident with the known sites of attachment of the somatic muscles to tendon cells in the epidermis. delilah expression persists in snail mutant embryos which lack mesoderm, indicating that expression of the gene was not induced by attachment of the underlying muscles. The similarity of this gene to other bHLH genes suggests that it plays an important role in the differentiation of epidermal cells into muscle attachment sites.

Epidermal tendon cells require Broad Complex function for correct attachment of the indirect flight muscles in Drosophila melanogaster

1999 ◽  
Vol 112 (22) ◽  
pp. 4051-4065 ◽  
Author(s):  
D.J. Sandstrom ◽  
L.L. Restifo
Keyword(s):  
Complex Function ◽  
Myotendinous Junction ◽  
Wild Type ◽  
Muscle Attachment ◽  
Attachment Sites ◽  
Tendon Cells ◽  
Flight Muscles ◽  
Broad Complex ◽  
Developing Muscle ◽  
Dorsal Epidermis

Drosophila Broad Complex, a primary response gene in the ecdysone cascade, encodes a family of zinc-finger transcription factors essential for metamorphosis. Broad Complex mutations of the rbp complementation group disrupt attachment of the dorsoventral indirect flight muscles during pupal development. We previously demonstrated that isoform BRC-Z1 mediates the muscle attachment function of rbp(+) and is expressed in both developing muscle fibers and their epidermal attachment sites. We now report two complementary studies to determine the cellular site and mode of action of rbp(+) during maturation of the myotendinous junctions of dorsoventral indirect flight muscles. First, genetic mosaics, produced using the paternal loss method, revealed that the muscle attachment phenotype is determined primarily by the genotype of the dorsal epidermis, with the muscle fiber and the ventral epidermis exerting little or no influence. When the dorsal epidermis was mutant, the vast majority of muscles detached or chose ectopic attachment sites, regardless of the muscle genotype. Conversely, wild-type dorsal epidermis could support attachment of mutant muscles. Second, ultrastructural analysis corroborated and extended these results, revealing defective and delayed differentiation of rbp mutant epidermal tendon cells in the dorsal attachment sites. Tendon cell processes, the stress-bearing links between the epidermis and muscle, were reduced in number and showed delayed appearance of microtubule bundles. In contrast, mutant muscle and ventral epidermis resembled the wild type. In conclusion, BRC-Z1 acts in the dorsal epidermis to ensure differentiation of the myotendinous junction. By analogy with the cell-cell interaction essential for embryonic muscle attachment, we propose that BRC-Z1 regulates one or more components of the epidermal response to a signal from the developing muscle.

scholarly journals wing blister, A New Drosophila Laminin α Chain Required for Cell Adhesion and Migration during Embryonic and Imaginal Development

1999 ◽  
Vol 145 (1) ◽  
pp. 191-201 ◽  
Author(s):  
Doris Martin ◽  
Susan Zusman ◽  
Xitong Li ◽  
Erin L. Williams ◽  
Narmada Khare ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Functional Characterization ◽  
Specific Pattern ◽  
Basement Membranes ◽  
Muscle Attachment ◽  
Attachment Sites ◽  
Cell Adhesion And Migration ◽  
Α Chain ◽  
Embryonic Viability ◽  
Muscle Attachment Sites

We report the molecular and functional characterization of a new α chain of laminin in Drosophila. The new laminin chain appears to be the Drosophila counterpart of both vertebrate α2 (also called merosin) and α1 chains, with a slightly higher degree of homology to α2, suggesting that this chain is an ancestral version of both α1 and α2 chains. During embryogenesis, the protein is associated with basement membranes of the digestive system and muscle attachment sites, and during larval stage it is found in a specific pattern in wing and eye discs. The gene is assigned to a locus called wing blister (wb), which is essential for embryonic viability. Embryonic phenotypes include twisted germbands and fewer pericardial cells, resulting in gaps in the presumptive heart and tracheal trunks, and myotubes detached from their target muscle attachment sites. Most phenotypes are in common with those observed in Drosophila laminin α3, 5 mutant embryos and many are in common with those observed in integrin mutations. Adult phenotypes show blisters in the wings in viable allelic combinations, similar to phenotypes observed in integrin genes. Mutation analysis in the eye demonstrates a function in rhabdomere organization. In summary, this new laminin α chain is essential for embryonic viability and is involved in processes requiring cell migration and cell adhesion.

scholarly journals A small proportion of Talin molecules transmit forces to achieve muscle attachment in vivo

2018 ◽  
Author(s):  
Sandra B. Lemke ◽  
Thomas Weidemann ◽  
Anna-Lena Cost ◽  
Carsten Grashoff ◽  
Frank Schnorrer
Keyword(s):  
Tissue Mechanics ◽  
Correlation Spectroscopy ◽  
Mechanical Forces ◽  
Muscle Attachment ◽  
Cell Fate Decisions ◽  
Mammalian Cell Lines ◽  
Attachment Sites ◽  
Molecular Forces ◽  
Muscle Attachment Sites

Cells in a developing organism are subjected to particular mechanical forces, which shape tissues and instruct cell fate decisions. How these forces are sensed and transmitted at the molecular level is thus an important question, which has mainly been investigated in cultured cells in vitro. Here, we elucidate how mechanical forces are transmitted in an intact organism. We studied Drosophila muscle attachment sites, which experience high mechanical forces during development and require integrin-mediated adhesion for stable attachment to tendons. Hence, we quantified molecular forces across the essential integrin-binding protein Talin, which links integrin to the actin cytoskeleton. Generating flies expressing three FRET-based Talin tension sensors reporting different force levels between 1 and 11 pN enabled us to quantify physiologically-relevant, molecular forces. By measuring primary Drosophila muscle cells, we demonstrate that Drosophila Talin experiences mechanical forces in cell culture that are similar to those previously reported for Talin in mammalian cell lines. However, in vivo force measurements at developing flight muscle attachment sites revealed that average forces across Talin are comparatively low and decrease even further while attachments mature and tissue-level tension increases. Concomitantly, Talin concentration at attachment sites increases five-fold as quantified by fluorescence correlation spectroscopy, suggesting that only few Talin molecules are mechanically engaged at any given time. We therefore propose that high tissue forces are shared amongst a large excess of adhesion molecules of which less than 15% are experiencing detectable forces at the same time. Our findings define an important new concept of how cells can adapt to changes in tissue mechanics to prevent mechanical failure in vivo.

Memoirs: The Muscles of the Adult Honey-bee (Apis mellifera L.)

1928 ◽  
Vol s2-71 (284) ◽  
pp. 563-651
Author(s):  
GUY D. MORISON
Keyword(s):  
Apis Mellifera ◽  
Alimentary Canal ◽  
Muscular Activity ◽  
Reproductive Organs ◽  
Muscle Fibres ◽  
Muscle Attachment ◽  
Apparent Lack ◽  
Histological Appearance ◽  
The Individual ◽  
Alary Muscles

1. The entire musculature of the alimentary canal is described in gross and in histological detail. The development of the muscle is considered. The innervation is described, likewise the tracheation and its relation to muscular activity and the bloodstream. 2. The heart is described with a detailed histological account of its muscle-fibres. Its tracheation is described and its apparent lack of innervation is discussed. 3. The ‘alary’ muscles of the dorsal diaphragm are described with a detailed account of their histology, innervation, and tracheation. 4. The ventral diaphragm is described as well as the histology, innervation, and tracheation of its muscle-fibres. The course of blood and physiological questions connected with it receive discussion. 5. The muscles of the reproductive organs of drone, queen, and worker are described with particular reference to the histology, innervation, tracheation, and physiology of their fibres. 6. The indirect muscles of the wings (fibrous muscle) have their histology, innervation, and tracheation described in detail. The method of contraction of the entire muscles and of the individual fibres and fibrils is discussed. The sarcosomes are described with their physiological significance to contraction. 7. The attachment of all the types of muscle found in the bee is described in histological detail. Different opinions of muscle attachment to chitin are summarized. 8. Throughout the paper, histological measurements are given for the various types of muscle-fibres and their nuclei in the three castes of bee. Since in the three castes the histological appearance is so similar for each type of muscle, the illustrations have been limited to portions of the muscles of worker bees.

A new Tardigrade species, Stygarctus keralensis sp. nov. (Arthrotardigrada: Stygarctidae) from the intertidal zone of Southwest coast of India

Zootaxa ◽  
2021 ◽  
Vol 4985 (3) ◽  
Author(s):  
N. K. VISHNUDATTAN ◽  
S. BIJOY NANDAN ◽  
J. G. HANSEN ◽  
P. R. JAYACHANDRAN
Keyword(s):  
New Species ◽  
Intertidal Zone ◽  
Seminal Receptacle ◽  
Morphological Similarity ◽  
Muscle Attachment ◽  
Southwest Coast Of India ◽  
Southwest Coast ◽  
Unique Character ◽  
Sandy Sediments

Stygarctus keralensis sp. nov. (Arthrotardigrada: Stygarctidae), is described from the intertidal sandy sediments of Vadakara beach, Kerala, Southwest coast of India. To a certain extent, this new species shows morphological similarity with Stygarctus gourbaultae Renaud-Mornant, 1981, however it can be differentiated by some significant distinguishable characters like double looped seminal receptacle ducts and the presence of a bow shaped internal thickening in between the opening of seminal receptacles situated below the level of gonopore and above the anus; unsculptured body plates I-III; paired sub-cephalic pore/muscle attachment; shape and structure of caudal processes. Presence of minute spikes on third lateral processes in the new species is another unique character by which it can be easily differentiated from S. gourbaultae.

The localized assembly of extracellular matrix integrin ligands requires cell-cell contact

2000 ◽  
Vol 113 (21) ◽  
pp. 3715-3723 ◽  
Author(s):  
M.D. Martin-Bermudo ◽  
N.H. Brown
Keyword(s):  
Extracellular Matrix ◽  
Drosophila Embryo ◽  
Cell Contact ◽  
Primary Role ◽  
Dependent Manner ◽  
Muscle Attachment ◽  
Matrix Assembly ◽  
Attachment Sites ◽  
Genetically Manipulated ◽  
Cell Cell

The assembly of an organism requires the interaction between different layers of cells, in many cases via an extracellular matrix. In the developing Drosophila larva, muscles attach in an integrin-dependent manner to the epidermis, via a specialized extracellular matrix called tendon matrix. Tiggrin, a tendon matrix integrin ligand, is primarily synthesized by cells distant to the muscle attachment sites, yet it accumulates specifically at these sites. Previous work has shown that the PS integrins are not required for tiggrin localization, suggesting that there is redundancy among tiggrin receptors. We have examined this by testing whether the PS2 integrin can recruit tiggrin to ectopic locations within the Drosophila embryo. We found that neither the wild type nor modified forms of the PS2 integrin, which have higher affinity for tiggrin, can recruit tiggrin to new cellular contexts. Next, we genetically manipulated the fate of the muscles and the epidermal muscle attachment cells, which demonstrated that muscles have the primary role in recruiting tiggrin to the tendon matrix and that cell-cell contact is necessary for this recruitment. Thus we propose that the inherent polarity of the muscle cells leads to a molecular specialization of their ends, and interactions between the ends produces an integrin-independent tiggrin receptor. Thus, interaction between cells generates an extracellular environment capable of nucleating extracellular matrix assembly.

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