Regulative capacity of the archenteron during gastrulation in the sea urchin

Development ◽  
1996 ◽  
Vol 122 (2) ◽  
pp. 607-616 ◽  
Author(s):  
D.R. McClay ◽  
C.Y. Logan
Keyword(s):  
Sea Urchin ◽  
Short Range ◽  
Endodermal Cells ◽  
Regulative Capacity

Gastrulation in the sea urchin involves an extensive rearrangement of cells of the archenteron giving rise to secondary mesenchyme at the archenteron tip followed by the foregut, midgut and hindgut. To examine the regulative capacity of this structure, pieces of the archenteron were removed or transplanted at different stages of gastrulation. After removal of any or all parts of the archenteron, the remaining veg 1 and /or veg 2 tissue regulated to replace the missing parts. Endoderm transplanted to ectopic positions also regulated to that new position in the archenteron. This ability to replace or regulate endoderm did not decline until after full elongation of the archenteron was completed. When replacement occurred, the new gut was smaller relative to the remaining embryo but the recognizable morphology of the archenteron was re-established. Long after the archenteron reveals territorial specification through expression of specific markers, the endodermal cells remain capable of being respecified to other gut regions. Thus, for much of gastrulation, the gut is conditionally specified. We propose that this regulative ability requires extensive and continuous short-range communication between cells of the archenteron in order to reorganize the tissues and position the boundaries of this structure even after experimental alterations.

Endo16, a Large Multidomain Protein Found on the Surface and ECM of Endodermal Cells during Sea Urchin Gastrulation, Binds Calcium

1994 ◽  
Vol 165 (1) ◽  
pp. 73-85 ◽  
Author(s):  
Margaret Soltysik-Española ◽  
David C. Klinzing ◽  
Kenneth Pfarr ◽  
Robert D. Burke ◽  
Susan G. Ernst
Keyword(s):  
Sea Urchin ◽  
Multidomain Protein ◽  
Endodermal Cells

scholarly journals Short-range Wnt5 signaling initiates specification of sea urchin posterior ectoderm

Development ◽  
2013 ◽  
Vol 140 (24) ◽  
pp. 4881-4889 ◽  
Author(s):  
D. C. McIntyre ◽  
N. W. Seay ◽  
J. C. Croce ◽  
D. R. McClay
Keyword(s):  
Sea Urchin ◽  
Short Range

Immunogold and immunoblot studies on a cell surface protein found in primary mesenchyme cells and in the cortical secretory vesicles of the sea urchin egg

1987 ◽  
Vol 45 ◽  
pp. 832-833
Author(s):  
G.L. Decker ◽  
M.C. Valdizan
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Protein ◽  
Egg Cell ◽  
Secretory Vesicles ◽  
Cell Surface Protein ◽  
Surface Complexes ◽  
Mesenchyme Cells ◽  
Lowicryl K4m ◽  
Primary Mesenchyme Cells

A monoclonal antibody designated MAb 1223 has been used to show that primary mesenchyme cells of the sea urchin embryo express a 130-kDa cell surface protein that may be directly involved in Ca2+ uptake required for growth of skeletal spicules. Other studies from this laboratory have shown that the 1223 antigen, although in relatively low abundance, is also expressed on the cell surfaces of unfertilized eggs and on the majority of blastomeres formed prior to differentiation of the primary mesenchyme cells.We have studied the distribution of 1223 antigen in S. purpuratus eggs and embryos and in isolated egg cell surface complexes that contain the cortical secretory vesicles. Specimens were fixed in 1.0% paraformaldehyde and 1.0% glutaraldehyde and embedded in Lowicryl K4M as previously reported. Colloidal gold (8nm diameter) was prepared by the method of Mulpfordt.

Domain coarsening by grain boundary migration in ordered Ni4Mo

1986 ◽  
Vol 44 ◽  
pp. 560-561
Author(s):  
K. Vasudevan ◽  
H. P. Kao ◽  
C. R. Brooks ◽  
E. E. Stansbury
Keyword(s):  
Grain Boundary ◽  
Grain Boundaries ◽  
Short Range ◽  
Boundary Migration ◽  
Grain Boundary Migration ◽  
Rapid Cooling ◽  
Temperature Range ◽  
Fee Structure ◽  
Domain Coarsening ◽  
Boundary Reaction

The Ni4Mo alloy has a short-range ordered fee structure (α) above 868°C, but transforms below this temperature to an ordered bet structure (β) by rearrangement of atoms on the fee lattice. The disordered α, retained by rapid cooling, can be ordered by appropriate aging below 868°C. Initially, very fine β domains in six different but crystallographically related variants form and grow in size on further aging. However, in the temperature range 600-775°C, a coarsening reaction begins at the former α grain boundaries and the alloy also coarsens by this mechanism. The purpose of this paper is to report on TEM observations showing the characteristics of this grain boundary reaction.

Ordering in Ni4Mo by TEM and APFIM

1987 ◽  
Vol 45 ◽  
pp. 214-215
Author(s):  
E.A. Kenik ◽  
T.A. Zagula ◽  
M.K. Miller ◽  
J. Bentley
Keyword(s):  
Electron Irradiation ◽  
Low Temperatures ◽  
Short Range ◽  
Atom Probe ◽  
Range Order ◽  
Considerable Time ◽  
Probe Field ◽  
Disordered Phase ◽  
Transmission Electron ◽  
Diffraction Patterns

The state of long-range order (LRO) and short-range order (SRO) in Ni4Mo has been a topic of interest for a considerable time (see Brooks et al.). The SRO is often referred to as 1½0 order from the apparent position of the diffuse maxima in diffraction patterns, which differs from the positions of the LRO (D1a) structure. Various studies have shown that a fully disordered state cannot be retained by quenching, as the atomic arrangements responsible for the 1½0 maxima are present at temperatures above the critical ordering temperature for LRO. Over 20 studies have attempted to identify the atomic arrangements associated with this state of order. A variety of models have been proposed, but no consensus has been reached. It has also been shown that 1 MeV electron irradiation at low temperatures (∼100 K) can produce the disordered phase in Ni4Mo. Transmission electron microscopy (TEM), atom probe field ion microscopy (APFIM), and electron irradiation disordering have been applied in the current study to further the understanding of the ordering processes in Ni4Mo.

The extracellular matrix of echinoderm and amphibian eggs: Visualization in quick-frozen, deep-etched, and rotary-shadowed specimens

1990 ◽  
Vol 48 (3) ◽  
pp. 60-61
Author(s):  
Barry Bonnell ◽  
Carolyn Larabell ◽  
Douglas Chandler
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Sea Urchin ◽  
Crystalline Structure ◽  
Cortical Granule ◽  
Two Dimensional ◽  
Small Peptides ◽  
Deep Etching ◽  
Quick Freezing ◽  
Acrosomal Reaction

Eggs of many species including those of echinoderms, amphibians and mammals exhibit an extensive extracellular matrix (ECM) that is important both in the reception of sperm and in providing a block to polyspermy after fertilization.In sea urchin eggs there are two distinctive coats, the vitelline layer which contains glycoprotein sperm receptors and the jelly layer that contains fucose sulfate glycoconjugates which trigger the acrosomal reaction and small peptides which act as chemoattractants for sperm. The vitelline layer (VL), as visualized by quick-freezing, deep-etching, and rotary-shadowing (QFDE-RS), is a fishnet-like structure, anchored to the plasma membrane by short posts. Orbiting above the VL are horizontal filaments which are thought to anchor the thicker jelly layer to the egg. Upon fertilization, the VL elevates and is transformed by cortical granule secretions into the fertilization envelope (FE). The rounded casts of microvilli in the VL are transformed into angular peaks and the envelope becomes coated inside and out with sheets of paracrystalline protein having a quasi-two dimensional crystalline structure.

Introductory Remarks

1980 ◽  
Vol 38 ◽  
pp. 598-599
Author(s):  
H. Mohri
Keyword(s):  
Muscle Contraction ◽  
Experimental Evidence ◽  
Sea Urchin ◽  
Constant Length ◽  
Thin Filaments ◽  
Bridge Formation ◽  
Thick Filaments ◽  
Sliding Mechanism ◽  
Radial Spokes ◽  
Cilia And Flagella

In 1959, Afzelius observed the presence of two rows of arms projecting from each outer doublet microtubule of the so-called 9 + 2 pattern of cilia and flagella, and suggested a possibility that the outer doublet microtubules slide with respect to each other with the aid of these arms during ciliary and flagellar movement. The identification of the arms as an ATPase, dynein, by Gibbons (1963)strengthened this hypothesis, since the ATPase-bearing heads of myosin molecules projecting from the thick filaments pull the thin filaments by cross-bridge formation during muscle contraction. The first experimental evidence for the sliding mechanism in cilia and flagella was obtained by examining the tip patterns of molluscan gill cilia by Satir (1965) who observed constant length of the microtubules during ciliary bending. Further evidence for the sliding-tubule mechanism was given by Summers and Gibbons (1971), using trypsin-treated axonemal fragments of sea urchin spermatozoa. Upon the addition of ATP, the outer doublets telescoped out from these fragments and the total length reached up to seven or more times that of the original fragment. Thus, the arms on a certain doublet microtubule can walk along the adjacent doublet when the doublet microtubules are disconnected by digestion of the interdoublet links which connect them with each other, or the radial spokes which connect them with the central pair-central sheath complex as illustrated in Fig. 1. On the basis of these pioneer works, the sliding-tubule mechanism has been established as one of the basic mechanisms for ciliary and flagellar movement.

The Organization of Actin Filaments in the Stereocilia of the Bird Cochlea

1980 ◽  
Vol 38 ◽  
pp. 554-555
Author(s):  
E.J. Battles ◽  
D. DeRosier ◽  
J.C. Saunders ◽  
L.G. Tilney
Keyword(s):  
Hair Cell ◽  
Diffraction Pattern ◽  
Sea Urchin ◽  
Actin Filaments ◽  
Optical Diffraction ◽  
Dense Material ◽  
Apical Surface ◽  
Structural Rigidity ◽  
High Degree ◽  
Degree Of Order

Extending from the apical surface of each hair cell of the chick cochlea are from 75 to 200 microvilli or stereocllia and one true cllium, the kinocilium. The stereocllia are arranged in rows of progressively increasing length (Fig. 1). Within each tapering sterocilium is a bundle of actin filaments with over 900 filaments near the tip yet only approximately 25 at the base where filaments are enmeshed in a dense material (Fig. 1); from here some of the filaments enter the apical surface of the cell (cuticular plate) as a rootlet. Examination of longitudinal sections of the stereocilia (Fig. 2) show that the filaments are aligned parallel to each other and show considerable order. Examination of an optical diffraction pattern of this bundle (Fig. 4) reveal that the actin filaments are packed such that the crossover points of adjacent actin filaments are inregister. A prominent reflection at 125Å−1 demonstrates that the filaments are cjossbridged by a macromolecular bridge situated at an average of 125Å−1 intervals (Fig. 4) in transverse sections the filaments appear hexagonally packed although there are regions where the filaments are less ordered (Fig. 3). In images processed in the computer to remove, noise and enhance detail periodic nature of the bridge can be clearly seen (see arrows Fig. 5). This image resembles that of an actin paracrystal formed from sea urchin extract composed of bundles of actin filaments crossbridged by a second protein. Thus the actin filaments in the bird stereocilia by being cross-bridged and packed with a high degree of order and produces a structure with considerable structural rigidity. Embryos were studied at various stages in development in an attempt to determine how the stereocilia form and how does the actin packing develops. These stages will be discussed.

Early Education in Short-Range Historical Perspective

1969 ◽  
Vol 14 (8) ◽  
pp. 437-438
Author(s):  
CELIA STENDLER LAVATELLI
Keyword(s):  
Short Range ◽  
Historical Perspective ◽  
Early Education
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