Cytokinesis: Filaments in the cleavage furrow

Schroeder, Thomas E.

doi:10.1016/0014-4827(68)90373-x

Cited by 230 publications

(92 citation statements)

References 11 publications

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“…Wcattempted to solve this problem by examining the ability of various kinds of reagents affecting the cytoplasmic structures and organelles to inhibit E-rosetting. In general, cytoehalasiiis have two effects on cellular events: the blocking of sugar metabolism by competition for the binding sites for sugars on the ceil membrane {18) and the blocking of act in polymerization (19). Cytoehalasin D. cytochala-sin E and dihydrocytochalasin B specifteally block the polymerization of aetin (20).…”

Section: Discussionmentioning

confidence: 99%

Participation of cytoplasmic organelles in E‐rosette formation

Ishijima

Asakura

Suzuta

1991

Immunology & Cell Biology

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Summary To elucidate the mechanism of E-roscilc formation between T cells and sheep red blood cx-lls{SRBC). the effect of variousagentsaifectingihLM'unctionorcytoplasmicstruclures(microtLibules and microtilaments) and organdies (mitocliondria and rough endoplasniic reliculum) was invcstieatcd. E-rosciie formation was greath inhibited by agents that block cither the energy producmg systcnr(KCN and NaNilur the integration ot tiiicrofilaments (cytochalasin B. dihydrocytochalasin B_ ;nui cytochalasin D). On ihe other hand, theic was little or no suppression by either inhihitors ot proici'n synthesis (cytlolieximide and puromycin). agenls that block Ihe polymeti^aiion ol microtubules (coldiicine. podophyllotoxin and vinblastinc). or chemicals disconnecting surface membrane proteins from the iniracellular strLietural proloiiis (chlnrpromazine. ^dibucaine. liydroccrtlsonc. and propranolol). The calcium ionophorc A23187. which transports Cn-' into ihe cyiosol. inhibited the F-rosette formation iiUhe presence of Ca-\ but nol in its absence. I-rum these results, we concluded thai new synthesis of ATE' and the struciural inlegration o\' niicrofilaments arc indispensable for the E-rosette formation, whieh is triggered by an interaetion between the Iigand (Tl ITS) and ils corresponding receptor (CD2). A certain levdorintraeelluIarCa-^ is also involved m the E-rosctte formalion.lMRODUCTION Thymus-derived (T) lymphocytes spontaneously form E-rosctte aggregates with sheep red blood cells (SRBC). and serve as a surface marker for the earliest stage of the expression of hLiman T-Iincage cells (1-3). E-roscttes are widely used in clinical immunology lo identify or to separate T eells (4-6). although their precise intracellular mechanism is unknown.Receni studies on E-rosette formation have shown that it is dependent upon a specilic interaction between the CD2 moleeule on T eells (7-9) and the complementary structure on SRBC termed the Tl I target structure (Tl ITS: iO.ll). The TllTS has been bioehemieally characterized and shown to be a 42 kDa glycoprotcin (10.11). CD2 binds LFA-3. a 55-70 kDa moleeule expressed on human endothelial. epithelial and connective tissue cells in most tissues, as well as human T and B lymphocytes, granuloeytes. and erythrocytes (12).On the other hand, little is known about the participation of eytopiasmie structures and organelles during E-rosette formation, although several reports suggest they probably play an important role. A study of the mechanism of capping of the surface immunoglobulins(slg) on B cells by corresponding anlibodies revealed that this phenomenon was suppressed by corticosteroids maintaining fluidity of membranes. the calcium ionophore A23187 causing Ca-**" tlux. and reagents aetingon microtilaments such as eytochalasin B (13). Another stud\ of lymphocyte adhesion to eultured Feycr's patch high endothelial venule reported that the adhesion oflymphoeytes was suppressed by NaN? and cytoehalasin L) (14). Moreover, the inhibitory effe-n of eytochalasin B and NaNi on Erosette tbrmation h...

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Section: Discussionmentioning

confidence: 99%

Participation of cytoplasmic organelles in E‐rosette formation

Ishijima

Asakura

Suzuta

1991

Immunology & Cell Biology

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“…In the division furrow, actin filaments accumulated to 1.8-fold of those in the reference cortex. Actin accumulation in the division furrow has been reported frequently including polar body formation using fluorescent phallotoxins (Strome, 1986;Yonemura and Kinoshita, 1986;Cao and Wang, 1990;Shimizu, 1990;Mabuchi, 1994;Li et al, 1997;Crawford et al, 1998;Satoh and Hamaguchi, 2000;Pielak et al, 2004Pielak et al, , 2005 after the contractile ring was described in the division furrow by Schroeder (1968Schroeder ( , 1970Schroeder ( , 1972. Therefore, actin distribution from the animal pole to the equatorial region of the oocyte is minimal at the pole, increases to maximal at the base of the bulge, and then decreases gradually to a constant value.…”

Section: Cortical Actin Distributionmentioning

confidence: 97%

Quantitative Analysis of Cortical Actin Filaments during Polar Body Formation in Starfish Oocytes

Hamaguchi

Numata

Satoh

2007

Cell Struct. Funct.

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ABSTRACT. Polar body formation is an extremely unequal cell division. In order to understand the mechanism of polar body formation, morphological changes at the animal pole were investigated in living oocytes of the starfish, Asterina pectinifera, and the amounts of cortical actin filaments were quantitatively estimated after staining the maturing oocytes with fluorescently-labeled phallotoxins using a computer and image-processing software. Formation of a bulge, which is presumed to become a polar body, and the anaphase separation of chromosomes occurred simultaneously. When the bulge became large, one group of chromatids moved into the bulge. The dividing furrow then formed and finally a polar body formed. Just at the time of bulge formation, the intensity of the fluorescence produced by the actin filaments at the top of the animal pole began to decrease, and subsequently the intensity at the top fell to half of the original value. On the other hand, the fluorescence intensity at the base of the bulge increased gradually. This actin accumulation at the base created a dividing furrow around the top of the animal pole as the bulge grew. Even when the polar body formation was inhibited mechanically, a similar pattern of actin deficiency and accumulation in the cortex near the animal pole was observed. This indicates that such regulation of filamentous actin can take place without bulging. Therefore, polar body formation is initiated by the bulging of the cortex weakened by actin deficiency and followed by contraction of the base of the bulge reinforced by actin accumulation.

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“…These preparative methods gave no information concerning the localization of the actin within the egg, but there is good evidence lor its presence in the cleavage furrow during cytokinesis, where it was seen first in the electron microscope as bundles of microfilaments (28,30,37). Actin has been localized in the cleavage furrow in a variety of other cell types ( 1,21,27,29,34) and this actin has been specifically labeled with heavy meromyosin (31). The investigations reported here were begun with the aim of determining whether the methods developed for the polymerization of tubulin to microtubules in mammalian brain (2, 39) could be used to prepare tubulin from the sea urchin egg.…”

Section: Introductionmentioning

confidence: 99%

Preparation and purification of polymerized actin from sea urchin egg extracts.

Kane¹

1975

The Journal of Cell Biology

219

145

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Isotonic extracts of the soluble cytoplasmic proteins of sea urchin eggs, containing sufficient EGTA to reduce the calcium concentration to low levels, form a dense gel on warming to 35 40~ Although this procedure is similar to that used to polymerize tubulin from mammalian brain, sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows this gel to have actin as a major component and to contain no tubulin. If such extracts are dialyzed against dilute salt solution, they no longer respond to warming, but gelation will occur if they are supplemented with 1 mM ATP and 0.020 M KC1 before heating. Gelation is not temperature reversible, but the gelled material can be dissolved in 0.6-1 M J~C1 and these solutions contain F-actin filaments. These filaments slowly aggregate to microscopic, birefringent fibrils when l mM ATP is added to the solution, and this procedure provides a simple method for preparing purified actin. The supernate remaining after actin removal contains the other two components of the gel, proteins of approximately 58,000 and 220,000 mol wt. These two proteins plus actin recombine to form the original gel material when the ionic strength is reduced. This reaction is reversible at 0~ and no heating is required.Following the demonstration of an actin-like protein, similar in properties to muscle actin, in myxomycete plasmodium (9, 10), similar methods revealed the presence of a cytoplasmic actin in unfertilized sea urchin eggs. This sea urchin egg actin was first identified and separated through its combination with rabbit muscle myosin (8,18,19), and the protein was later prepared directly from egg extracts by salting out with ammonium sulfate (17). These preparative methods gave no information concerning the localization of the actin within the egg, but there is good evidence lor its presence in the cleavage furrow during cytokinesis, where it was seen first in the electron microscope as bundles of microfilaments (28,30,37). Actin has been localized in the cleavage furrow in a variety of other cell types ( 1,21,27,29,34) and this actin has been specifically labeled with heavy meromyosin (31). The investigations reported here were begun with the aim of determining whether the methods developed for the polymerization of tubulin to microtubules in mammalian brain (2, 39) could be used to prepare tubulin from the sea urchin egg. Marine eggs are an excellent source of isolated mitotic apparatuses for the investigation of the role of microtubules in chromosome movement, but up to this time only the interaction of mammalian brain tuhulin with such isolated mitotic apparatuses has been reported (12, 25). Our attempts to prepare tubulin from extracts of sea urchin eggs with the methods developed for mammalian material were unsuccessful, and a number of modifications of this method were made to adapt it to the

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Cytokinesis: Filaments in the cleavage furrow

Cited by 230 publications

References 11 publications

Participation of cytoplasmic organelles in E‐rosette formation

Participation of cytoplasmic organelles in E‐rosette formation

Quantitative Analysis of Cortical Actin Filaments during Polar Body Formation in Starfish Oocytes

Preparation and purification of polymerized actin from sea urchin egg extracts.

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