scholarly journals The Role of Myosin II Motor Activity in Distributing Myosin Asymmetrically and Coupling Protrusive Activity to Cell Translocation

2006 ◽  
Vol 17 (10) ◽  
pp. 4435-4445 ◽  
Author(s):  
John Kolega
Keyword(s):  
Motor Activity ◽  
Cell Body ◽  
Body Movement ◽  
Myosin Ii ◽  
Time Lapse ◽  
The Body ◽  
Myosin Filament ◽  
Forward Movement ◽  
Myosin Iia ◽  
And Function

Nonmuscle myosin IIA and IIB distribute preferentially toward opposite ends of migrating endothelial cells. To understand the mechanism and function of this behavior, myosin II was examined in cells treated with the motor inhibitor, blebbistatin. Blebbistatin at ≥30 μM inhibited anterior redistribution of myosin IIA, with 100 μM blebbistatin causing posterior accumulation. Posterior accumulation of myosin IIB was unaffected. Time-lapse cinemicrography showed myosin IIA entering lamellipodia shortly after their formation, but failing to move into lamellipodia in blebbistatin. Thus, myosin II requires motor activity to move forward onto F-actin in protrusions. However, this movement is inhibited by myosin filament assembly, because whole myosin was delayed relative to a tailless fragment. Inhibiting myosin's forward movement reduced coupling between protrusive activity and translocation of the cell body: In untreated cells, body movement followed advancing lamellipodia, whereas blebbistatin-treated cells extended protrusions without displacement of the body or with a longer delay before movement. Anterior cytoplasm of blebbistatin-treated cells contained disorganized bundles of parallel microfilaments, but anterior F-actin bundles in untreated cells were mostly oriented perpendicular to movement. Myosin II may ordinarily move anteriorly on actin filaments and pull crossed filaments into antiparallel bundles, with the resulting realignment pulling the cell body forward.

scholarly journals Localized Depolymerization of the Major Sperm Protein Cytoskeleton Correlates with the Forward Movement of the Cell Body in the Amoeboid Movement of Nematode Sperm

1999 ◽  
Vol 146 (5) ◽  
pp. 1087-1096 ◽  
Author(s):  
Joseph E. Italiano ◽  
Murray Stewart ◽  
Thomas M. Roberts
Keyword(s):  
Cell Body ◽  
Body Movement ◽  
Leading Edge ◽  
Amoeboid Movement ◽  
Major Sperm Protein ◽  
Membrane Protrusion ◽  
Forward Movement ◽  
Sperm Protein ◽  
Amoeboid Motility ◽  
Tightly Coupled

The major sperm protein (MSP)-based amoeboid motility of Ascaris suum sperm requires coordinated lamellipodial protrusion and cell body retraction. In these cells, protrusion and retraction are tightly coupled to the assembly and disassembly of the cytoskeleton at opposite ends of the lamellipodium. Although polymerization along the leading edge appears to drive protrusion, the behavior of sperm tethered to the substrate showed that an additional force is required to pull the cell body forward. To examine the mechanism of cell body movement, we used pH to uncouple cytoskeletal polymerization and depolymerization. In sperm treated with pH 6.75 buffer, protrusion of the leading edge slowed dramatically while both cytoskeletal disassembly at the base of the lamellipodium and cell body retraction continued. At pH 6.35, the cytoskeleton pulled away from the leading edge and receded through the lamellipodium as its disassembly at the cell body continued. The cytoskeleton disassembled rapidly and completely in cells treated at pH 5.5, but reformed when the cells were washed with physiological buffer. Cytoskeletal reassembly occurred at the lamellipodial margin and caused membrane protrusion, but the cell body did not move until the cytoskeleton was rebuilt and depolymerization resumed. These results indicate that cell body retraction is mediated by tension in the cytoskeleton, correlated with MSP depolymerization at the base of the lamellipodium.

scholarly journals Analysis of the Actin–Myosin II System in Fish Epidermal Keratocytes: Mechanism of Cell Body Translocation

1997 ◽  
Vol 139 (2) ◽  
pp. 397-415 ◽  
Author(s):  
Tatyana M. Svitkina ◽  
Alexander B. Verkhovsky ◽  
Kyle M. McQuade ◽  
Gary G. Borisy
Keyword(s):  
Cell Body ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Myosin Ii ◽  
Leading Edge ◽  
Time Lapse ◽  
Supramolecular Organization ◽  
Retrograde Flow ◽  
Body Boundary ◽  
Filament Bundles

While the protrusive event of cell locomotion is thought to be driven by actin polymerization, the mechanism of forward translocation of the cell body is unclear. To elucidate the mechanism of cell body translocation, we analyzed the supramolecular organization of the actin–myosin II system and the dynamics of myosin II in fish epidermal keratocytes. In lamellipodia, long actin filaments formed dense networks with numerous free ends in a brushlike manner near the leading edge. Shorter actin filaments often formed T junctions with longer filaments in the brushlike area, suggesting that new filaments could be nucleated at sides of preexisting filaments or linked to them immediately after nucleation. The polarity of actin filaments was almost uniform, with barbed ends forward throughout most of the lamellipodia but mixed in arc-shaped filament bundles at the lamellipodial/cell body boundary. Myosin II formed discrete clusters of bipolar minifilaments in lamellipodia that increased in size and density towards the cell body boundary and colocalized with actin in boundary bundles. Time-lapse observation demonstrated that myosin clusters appeared in the lamellipodia and remained stationary with respect to the substratum in locomoting cells, but they exhibited retrograde flow in cells tethered in epithelioid colonies. Consequently, both in locomoting and stationary cells, myosin clusters approached the cell body boundary, where they became compressed and aligned, resulting in the formation of boundary bundles. In locomoting cells, the compression was associated with forward displacement of myosin features. These data are not consistent with either sarcomeric or polarized transport mechanisms of cell body translocation. We propose that the forward translocation of the cell body and retrograde flow in the lamellipodia are both driven by contraction of an actin–myosin network in the lamellipodial/cell body transition zone.

FURTHER OBSERVATIONS ON AMOEBOID HAEMOCYTES IN BLABERUS GIGANTEUS (L.) (ORTHOPTERA: BLATTIDAE)

1961 ◽  
Vol 39 (5) ◽  
pp. 755-766 ◽  
Author(s):  
J. W. Arnold
Keyword(s):  
Cell Body ◽  
Time Lapse ◽  
Flat Surfaces ◽  
Variable Form ◽  
Form And Function ◽  
Projection Analysis ◽  
Rapid Elongation ◽  
Wing Veins ◽  
And Function

The movements of amoeboid haemocytes in vivo in wing veins of B. giganteus were studied with the aid of time-lapse cinephotomicrography and projection analysis. They are described here in detail and discussed in relation to haemocyte form and function. Haemocyte motion included non-migratory as well as migratory aspects. Non-migratory motion comprised the slow to turbulent cytoplasmic motion and intermittent probing movements of stationary cells. Active migration occurred in the more or less typical amoeboid fashion and also in the more peculiar contractile manner which involved the projection of hyaline, tactile pseudopodia of variable form and often resulted in extreme and relatively rapid elongation of the cell body. Haemocytes were thus able to move on flat surfaces, to extend themselves across spaces, and to force their way into narrow tissue interstices. These activities demonstrate the versatility of the cells and provide a means of accounting for certain of their functions.

scholarly journals Regulation of Fission Yeast Myosin-II Function and Contractile Ring Dynamics by Regulatory Light-Chain and Heavy-Chain Phosphorylation

2009 ◽  
Vol 20 (17) ◽  
pp. 3941-3952 ◽  
Author(s):  
Thomas E. Sladewski ◽  
Michael J. Previs ◽  
Matthew Lord
Keyword(s):  
Motor Activity ◽  
Heavy Chain ◽  
Light Chain ◽  
Myosin Ii ◽  
Phosphorylation Sites ◽  
Contractile Ring ◽  
In Vitro Motility ◽  
Ring Constriction ◽  
And Function

We investigated the role of regulatory light-chain (Rlc1p) and heavy-chain phosphorylation in controlling fission yeast myosin-II (Myo2p) motor activity and function during cytokinesis. Phosphorylation of Rlc1p leads to a fourfold increase in Myo2p's in vitro motility rate, which ensures effective contractile ring constriction and function. Surprisingly, unlike with smooth muscle and nonmuscle myosin-II, RLC phosphorylation does not influence the actin-activated ATPase activity of Myo2p. A truncated form of Rlc1p lacking its extended N-terminal regulatory region (including phosphorylation sites) supported maximal Myo2p in vitro motility rates and normal contractile ring function. Thus, the unphosphorylated N-terminal extension of Rlc1p can uncouple the ATPase and motility activities of Myo2p. We confirmed the identity of one out of two putative heavy-chain phosphorylation sites previously reported to control Myo2p function and cytokinesis. Although in vitro studies indicated that phosphorylation at Ser-1444 is not needed for Myo2p motor activity, phosphorylation at this site promotes the initiation of contractile ring constriction.

scholarly journals A three-component mechanism for fibroblast migration with a contractile cell body that couples a myosin II–independent propulsive anterior to a myosin II–dependent resistive tail

2012 ◽  
Vol 23 (9) ◽  
pp. 1657-1663 ◽  
Author(s):  
Wei-hui Guo ◽  
Yu-li Wang
Keyword(s):  
Cell Migration ◽  
Cell Body ◽  
Nuclear Translocation ◽  
Myosin Ii ◽  
Local Treatment ◽  
Anterior Region ◽  
Nuclear Movement ◽  
Forward Movement ◽  
Cultured Fibroblasts ◽  
Fibroblast Migration

To understand the mechanism of cell migration, we cultured fibroblasts on micropatterned tracks to induce persistent migration with a highly elongated morphology and well-defined polarity, which allows microfluidic pharmacological manipulations of regional functions. The function of myosin II was probed by applying inhibitors either globally or locally. Of interest, although global inhibition of myosin II inhibited tail retraction and caused dramatic elongation of the posterior region, localized inhibition of the cell body inhibited nuclear translocation and caused elongation of the anterior region. In addition, local application of cytochalasin D at the tip inhibited frontal extension without inhibiting forward movement of the cell nucleus, whereas local treatment posterior to the nucleus caused reversal of nuclear movement. Imaging of cortical dynamics indicated that the region around the nucleus is a distinct compression zone where activities of anterior and posterior regions converge. These observations suggest a three-component model of cell migration in which a contractile middle section is responsible for the movement of a bulky cell body and the detachment/retraction of a resistive tail, thereby allowing these regions to undergo coordinated movement with a moving anterior region that carries little load.

Deadlift Recognition and Application based on Multiple Modalities using Recurrent Neural Network

2020 ◽  
Vol 2020 (17) ◽  
pp. 2-1-2-6
Author(s):  
Shih-Wei Sun ◽  
Ting-Chen Mou ◽  
Pao-Chi Chang
Keyword(s):  
Neural Network ◽  
Recurrent Neural Network ◽  
Network Structure ◽  
Inertial Sensors ◽  
Body Movement ◽  
The Body ◽  
Body Parts ◽  
Multimodal Sensing ◽  
Multiple Devices ◽  
Neural Network Structure

To improve the workout efficiency and to provide the body movement suggestions to users in a “smart gym” environment, we propose to use a depth camera for capturing a user’s body parts and mount multiple inertial sensors on the body parts of a user to generate deadlift behavior models generated by a recurrent neural network structure. The contribution of this paper is trifold: 1) The multimodal sensing signals obtained from multiple devices are fused for generating the deadlift behavior classifiers, 2) the recurrent neural network structure can analyze the information from the synchronized skeletal and inertial sensing data, and 3) a Vaplab dataset is generated for evaluating the deadlift behaviors recognizing capability in the proposed method.

Influence of Ascorbic Acid on the Structure and Function of Alpha-2- macroglobulin: Investigations using Spectroscopic and Thermodynamic Techniques

2020 ◽  
Vol 27 (3) ◽  
pp. 201-209
Author(s):  
Syed Saqib Ali ◽  
Mohammad Khalid Zia ◽  
Tooba Siddiqui ◽  
Haseeb Ahsan ◽  
Fahim Halim Khan
Keyword(s):  
Ascorbic Acid ◽  
Conformational Changes ◽  
Structural Changes ◽  
The Body ◽  
Titration Calorimetry ◽  
Spectroscopic Techniques ◽  
Human Beings ◽  
Plasma Ascorbic Acid ◽  
Dietary Antioxidant ◽  
And Function

Background: Ascorbic acid is a classic dietary antioxidant which plays an important role in the body of human beings. It is commonly found in various foods as well as taken as dietary supplement. Objective: The plasma ascorbic acid concentration may range from low, as in chronic or acute oxidative stress to high if delivered intravenously during cancer treatment. Sheep alpha-2- macroglobulin (α2M), a human α2M homologue is a large tetrameric glycoprotein of 630 kDa with antiproteinase activity, found in sheep’s blood. Methods: In the present study, the interaction of ascorbic acid with alpha-2-macroglobulin was explored in the presence of visible light by utilizing various spectroscopic techniques and isothermal titration calorimetry (ITC). Results: UV-vis and fluorescence spectroscopy suggests the formation of a complex between ascorbic acid and α2M apparent by increased absorbance and decreased fluorescence. Secondary structural changes in the α2M were investigated by CD and FT-IR spectroscopy. Our findings suggest the induction of subtle conformational changes in α2M induced by ascorbic acid. Thermodynamics signatures of ascorbic acid and α2M interaction indicate that the binding is an enthalpy-driven process. Conclusion: It is possible that ascorbic acid binds and compromises antiproteinase activity of α2M by inducing changes in the secondary structure of the protein.

A Guide to Old Spanish

2018 ◽  
Author(s):  
Steven N. Dworkin
Keyword(s):  
The Body ◽  
Standard Language ◽  
Function Words ◽  
Sound System ◽  
Old Spanish ◽  
And Function ◽  
Linguistic Structures ◽  
Verb Tense ◽  
Modern Standard

This book describes the linguistic structures that constitute Medieval or Old Spanish as preserved in texts written prior to the beginning of the sixteenth century. It emphasizes those structures that contrast with the modern standard language. Chapter 1 presents methodological issues raised by the study of a language preserved only in written sources. Chapter 2 examines questions involved in reconstructing the sound system of Old Spanish before discussing relevant phonetic and phonological details. The chapter ends with an overview of Old Spanish spelling practices. Chapter 3 presents in some detail the nominal, verbal, and pronominal morphology of the language, with attention to regional variants. Chapter 4 describes selected syntactic structures, with emphasis on the noun phrase, verb phrase, object pronoun placement, subject-verb-object word order, verb tense, aspect, and mood. Chapter 5 begins with an extensive list of Old Spanish nouns, adjectives, verbs, and function words that have not survived into the modern standard language. It then presents examples of coexisting variants (doublets) and changes of meaning, and finishes with an overview of the creation of neologisms in the medieval language through derivational morphology (prefixation, suffixation, compounding). The book concludes with an anthology composed of three extracts from Spanish prose texts, one each from the thirteenth, fourteenth, and fifteenth centuries. The extracts contain footnotes that highlight relevant morphological, syntactic, and lexical features, with cross references to the relevant sections in the body of the book.

scholarly journals Estimation of Motion and Respiratory Characteristics during the Meditation Practice Based on Video Analysis

Sensors ◽  
2021 ◽  
Vol 21 (11) ◽  
pp. 3771
Author(s):  
Alexey Kashevnik ◽  
Walaa Othman ◽  
Igor Ryabchikov ◽  
Nikolay Shilov
Keyword(s):  
Respiratory Rate ◽  
Evaluation System ◽  
Body Movement ◽  
Absolute Error ◽  
The Body ◽  
Meditation Practice ◽  
Body Parts ◽  
Mental Health Training ◽  
Negative Thoughts ◽  
The Mean

Meditation practice is mental health training. It helps people to reduce stress and suppress negative thoughts. In this paper, we propose a camera-based meditation evaluation system, that helps meditators to improve their performance. We rely on two main criteria to measure the focus: the breathing characteristics (respiratory rate, breathing rhythmicity and stability), and the body movement. We introduce a contactless sensor to measure the respiratory rate based on a smartphone camera by detecting the chest keypoint at each frame, using an optical flow based algorithm to calculate the displacement between frames, filtering and de-noising the chest movement signal, and calculating the number of real peaks in this signal. We also present an approach to detecting the movement of different body parts (head, thorax, shoulders, elbows, wrists, stomach and knees). We have collected a non-annotated dataset for meditation practice videos consists of ninety videos and the annotated dataset consists of eight videos. The non-annotated dataset was categorized into beginner and professional meditators and was used for the development of the algorithm and for tuning the parameters. The annotated dataset was used for evaluation and showed that human activity during meditation practice could be correctly estimated by the presented approach and that the mean absolute error for the respiratory rate is around 1.75 BPM, which can be considered tolerable for the meditation application.

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