The Effect of Basic Microshapes on hNT Astrocytes Cytoplasmic Process Outgrowth

2020 ◽  
Author(s):  
Si Li ◽  
E. Scott Graham ◽  
Charles P. Unsworth
Keyword(s):  
Cytoplasmic Process ◽  
Process Outgrowth

Ultrastructural observations on the in vitro cytoadherence of Plasmodium falciparum infected red blood cells

1990 ◽  
Vol 48 (3) ◽  
pp. 914-915
Author(s):  
D.J.P. Ferguson ◽  
A.R. Berendt ◽  
J. Tansey ◽  
K. Marsh ◽  
C.I. Newbold
Keyword(s):  
Plasmodium Falciparum ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Umbilical Vein ◽  
Cell Types ◽  
Amelanotic Melanoma ◽  
Cytoplasmic Process ◽  
Umbilical Vein Endothelial Cells

In human malaria, the most serious clinical manifestation is cerebral malaria (CM) due to infection with Plasmodium falciparum. The pathology of CM is thought to relate to the fact that red blood cells containing mature forms of the parasite (PRBC) cytoadhere or sequester to post capillary venules of various tissues including the brain. This in vivo phenomenon has been studied in vitro by examining the cytoadherence of PRBCs to various cell types and purified proteins. To date, three Ijiost receptor molecules have been identified; CD36, ICAM-1 and thrombospondin. The specific changes in the PRBC membrane which mediate cytoadherence are less well understood, but they include the sub-membranous deposition of electron-dense material resulting in surface deformations called knobs. Knobs were thought to be essential for cytoadherence, lput recent work has shown that certain knob-negative (K-) lines can cytoadhere. In the present study, we have used electron microscopy to re-examine the interactions between K+ PRBCs and both C32 amelanotic melanoma cells and human umbilical vein endothelial cells (HUVEC).We confirm previous data demonstrating that C32 cells possess numerous microvilli which adhere to the PRBC, mainly via the knobs (Fig. 1). In contrast, the HUVEC were relatively smooth and the PRBCs appeared partially flattened onto the cell surface (Fig. 2). Furthermore, many of the PRBCs exhibited an invagination of the limiting membrane in the attachment zone, often containing a cytoplasmic process from the endothelial cell (Fig. 2).

Cocaine‐induced inhibition of process outgrowth in locus coeruleus neurons: role of gestational exposure period and offspring sex

2004 ◽  
Vol 22 (5-6) ◽  
pp. 297-308 ◽  
Author(s):  
Diane M. Snow ◽  
Heidi M. Carman ◽  
Jeffrey D. Smith ◽  
Rosemarie M. Booze ◽  
Marian A. Welch ◽  
...  
Keyword(s):  
Locus Coeruleus ◽  
Exposure Period ◽  
Gestational Exposure ◽  
Offspring Sex ◽  
Process Outgrowth

scholarly journals Disease-associated Mutations in the Prion Protein Impair Laminin-induced Process Outgrowth and Survival

2012 ◽  
Vol 287 (52) ◽  
pp. 43777-43788 ◽  
Author(s):  
Cleiton F. Machado ◽  
Flavio H. Beraldo ◽  
Tiago G. Santos ◽  
Dominique Bourgeon ◽  
Michele C. Landemberger ◽  
...  
Keyword(s):  
Prion Protein ◽  
Process Outgrowth

Sequence analysis of MAP2 function in living cells

1994 ◽  
Vol 107 (11) ◽  
pp. 3115-3125 ◽  
Author(s):  
J. Ferralli ◽  
T. Doll ◽  
A. Matus
Keyword(s):  
Neuronal Cells ◽  
Specific Protein ◽  
Direct Result ◽  
Microtubule Binding ◽  
Amino Terminal ◽  
Rich Domain ◽  
Weak Binding ◽  
Repeat Domain ◽  
Combined Action ◽  
Process Outgrowth

Microtubule-associated protein 2 (MAP2) is an abundant neuron-specific protein that binds to microtubules through a domain near its carboxyl terminus that contains either three or four similar repeats of a 31 amino acid motif. When expressed in non-neuronal cells by transfection MAP2 stabilises microtubules and induces their rearrangement into long bundles that are capable of supporting process outgrowth. To investigate which elements in the MAP2 sequence are involved in these functions we have constructed a series of deletion mutants of the short embryonic form of MAP2, MAP2c, and transfected them into non-neuronal cells. This showed that the strength of binding to microtubules increased with the number of repeats present in the construct. However, the repeat domain itself was insufficient for microtubule binding, which required in addition contiguous sequences either amino-terminal or carboxyl-terminal to the repeats themselves. Particularly on the amino-terminal side of the repeats, where there is a proline-rich domain, step-wise increases in the length of neighbouring sequence produced a gradual increase in microtubule binding. The apparent strength of binding to microtubules produced by mutant MAP2 forms was further correlated with the degree of bundling they induced as well as with the ability of the resulting microtubules to support process outgrowth. These results indicate that the interaction of MAP2 with microtubules is mediated by the combined action of several weak binding sites, including each of the repeat motifs and elements in the sequences on either side of them, whose additive effect produces the strong binding of the native MAP2 molecule. The results further indicate that both the bundling and stiffening of microtubules by MAP2 are correlated with the strength of its binding to them and suggest that these properties are a direct result of microtubule stabilisation.

Nicotinic antagonists enhance process outgrowth by rat retinal ganglion cells in culture

Science ◽  
1988 ◽  
Vol 239 (4845) ◽  
pp. 1293-1296 ◽  
Author(s):  
S. Lipton ◽  
M. Frosch ◽  
M. Phillips ◽  
D. Tauck ◽  
E Aizenman
Keyword(s):  
Retinal Ganglion Cells ◽  
Ganglion Cells ◽  
Retinal Ganglion ◽  
Cells In Culture ◽  
Process Outgrowth

Peripheral nerve induces macrophage neurotrophic activities: regulation of neuronal process outgrowth, intracellular signaling and synaptic function

2003 ◽  
Vol 142 (1-2) ◽  
pp. 112-129 ◽  
Author(s):  
Annemarie Shibata ◽  
Marina Zelivyanskaya ◽  
Jenae Limoges ◽  
Kimberly A Carlson ◽  
Santhi Gorantla ◽  
...  
Keyword(s):  
Peripheral Nerve ◽  
Intracellular Signaling ◽  
Synaptic Function ◽  
Neuronal Process ◽  
Process Outgrowth

scholarly journals Juvenile and mature MAP2 isoforms induce distinct patterns of process outgrowth.

1996 ◽  
Vol 7 (3) ◽  
pp. 443-455 ◽  
Author(s):  
N Leclerc ◽  
P W Baas ◽  
C C Garner ◽  
K S Kosik
Keyword(s):  
Alternative Splicing ◽  
Spodoptera Frugiperda ◽  
Morphological Features ◽  
Developmentally Regulated ◽  
Architectural Elements ◽  
Molecular Masses ◽  
Process Outgrowth ◽  
Cell Expression

Microtubule-associated protein-2 (MAP2) is the most abundant MAP in neurons, where its distribution is restricted to the somatodendritic compartment. This molecule undergoes developmentally regulated alternative splicing, resulting in at least two isoforms, a juvenile isoform (termed MAP2c) and a mature isoform (MAP2), with greatly different molecular masses. Spodoptera frugiperda (Sf9) cell expression of the juvenile versus the mature MAP2 isoform generates two distinct patterns of process outgrowth. The smaller juvenile isoform induces multiple short thin processes. Mature MAP2 tends to induce single processes that are considerably thicker than those processes induced by juvenile MAP2. We found important differences in the variability of spacing between microtubules and the number of microtubules along the processes induced by MAP2c and mature MAP2. MAP2c showed variability with most microtubules spaced as closely as with tau, but some spaced as far apart as with mature MAP2. Over their length, the mature MAP2 processes demonstrate proximo-distal taper, which corresponds to a narrowing of the spacing between microtubules from 90 nm to 40 nm. Moreover, there is a decreased number of microtubules in mature MAP2-induced processes whereas in tau and MAP2-induced processes, the number of microtubules is constant along the length. Based on these observations, we conclude that MAP2 isoforms can serve as architectural elements by establishing specific morphological features of processes and specific arrangements of their microtubules.

scholarly journals Interactions of a neuronal cell line (PC12) with laminin, collagen IV, and fibronectin: identification of integrin-related glycoproteins involved in attachment and process outgrowth.

1987 ◽  
Vol 105 (5) ◽  
pp. 2347-2358 ◽  
Author(s):  
K J Tomaselli ◽  
C H Damsky ◽  
L F Reichardt
Keyword(s):  
Cell Surface ◽  
Cell Line ◽  
Pc12 Cells ◽  
Pc12 Cell ◽  
Mammalian Cells ◽  
Chinese Hamster ◽  
Neuronal Cell ◽  
Collagen Iv ◽  
Nervous System Development ◽  
Process Outgrowth

Neuronal responses to extracellular matrix (ECM) constituents are likely to play an important role in nervous system development and regeneration. We have studied the interactions of a neuron-like rat pheochromocytoma cell line, PC12, with ECM protein-coated substrates. Using a quantitative cell attachment assay, PC12 cells were shown to adhere readily to laminin (LN) or collagen IV (Col IV) but poorly to fibronectin (FN). The specificity of attachment to these ECM proteins was demonstrated using ligand-specific antibodies and synthetic peptides. To identify PC12 cell surface proteins that mediate interactions with LN, Col IV, and FN, two different antisera to putative ECM receptors purified from mammalian cells were tested for their effects on PC12 cell adhesion and neuritic process outgrowth. Antibodies to a 140-kD FN receptor heterodimer purified from Chinese hamster ovarian cells (anti-FNR; Brown, P. J., and R. L. Juliano, 1986, J. Cell Biol., 103:1595-1603) inhibited attachment to LN and FN but not to Col IV. Antibodies to an ECM receptor preparation purified from baby hamster kidney fibroblastic cells (anti-ECMR; Knudsen, K. A., P. E. Rao, C. H. Damsky, and C. A. Buck, 1981, Proc. Natl. Acad. Sci. USA., 78:6071-6075) inhibited attachment to LN, FN, and Col IV, but did not prevent attachment to other adhesive substrates. In addition to its effects on adhesion, the anti-ECMR serum inhibited both PC12 cell and sympathetic neuronal process outgrowth on LN substrates. Immunoprecipitation of surface-iodinated or [3H]glucosamine-labeled PC12 cells with either the anti-FNR or anti-ECMR serum identified three prominent cell surface glycoproteins of 120, 140, and 180 kD under nonreducing conditions. The 120-kD glycoprotein, which could be labeled with 32P-orthophosphate and appeared to be noncovalently associated with the 140- and 180-kD proteins, cross reacted with antibodies to the beta-subunit (band 3) of the avian integrin complex, itself a receptor or receptors for the ECM constituents LN, FN, and some collagens.

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