scholarly journals Ca2+–Calmodulin Dependent Wound Repair in Dictyostelium Cell Membrane

Cells ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 1058
Author(s):  
Md. Shahabe Uddin Talukder ◽  
Mst. Shaela Pervin ◽  
Md. Istiaq Obaidi Tanvir ◽  
Koushiro Fujimoto ◽  
Masahito Tanaka ◽  
...  

Wound repair of cell membrane is a vital physiological phenomenon. We examined wound repair in Dictyostelium cells by using a laserporation, which we recently invented. We examined the influx of fluorescent dyes from the external medium and monitored the cytosolic Ca2+ after wounding. The influx of Ca2+ through the wound pore was essential for wound repair. Annexin and ESCRT components accumulated at the wound site upon wounding as previously described in animal cells, but these were not essential for wound repair in Dictyostelium cells. We discovered that calmodulin accumulated at the wound site upon wounding, which was essential for wound repair. The membrane accumulated at the wound site to plug the wound pore by two-steps, depending on Ca2+ influx and calmodulin. From several lines of evidence, the membrane plug was derived from de novo generated vesicles at the wound site. Actin filaments also accumulated at the wound site, depending on Ca2+ influx and calmodulin. Actin accumulation was essential for wound repair, but microtubules were not essential. A molecular mechanism of wound repair will be discussed.

Author(s):  
M. Shlepr ◽  
R. L. Turner

Calcification in the echinoderms occurs within a limited-volume cavity enclosed by cytoplasmic extensions of the mineral depositing cells, the sclerocytes. The current model of this process maintains that the sheath formed from these cytoplasmic extensions is syncytial. Prior studies indicate that syncytium formation might be dependent on sclerocyte density and not required for calcification. This model further envisions that ossicles formed de novo nucleate and grow intracellularly until the ossicle effectively outgrows the vacuole. Continued ossicle growth occurs within the sheath but external to the cell membrane. The initial intracellular location has been confirmed only for elements of the echinoid tooth.The regenerating aboral disc integument of ophiophragmus filograneus was used to test the current echinoderm calcification model. This tissue is free of calcite fragments, thus avoiding questions of cellular engulfment, and ossicles are formed de novo. The tissue calcification pattern was followed by light microscopy in both living and fixed preparations.


2001 ◽  
Vol 81 (4) ◽  
pp. 1791-1826 ◽  
Author(s):  
Helfried Günther Glitsch

Like several other ion transporters, the Na+-K+ pump of animal cells is electrogenic. The pump generates the pump current I p. Under physiological conditions, I p is an outward current. It can be measured by electrophysiological methods. These methods permit the study of characteristics of the Na+-K+ pump in its physiological environment, i.e., in the cell membrane. The cell membrane, across which a potential gradient exists, separates the cytosol and extracellular medium, which have distinctly different ionic compositions. The introduction of the patch-clamp techniques and the enzymatic isolation of cells have facilitated the investigation of I p in single cardiac myocytes. This review summarizes and discusses the results obtained from I p measurements in isolated cardiac cells. These results offer new exciting insights into the voltage and ionic dependence of the Na+-K+ pump activity, its effect on membrane potential, and its modulation by hormones, transmitters, and drugs. They are fundamental for our current understanding of Na+-K+ pumping in electrically excitable cells.


Cytometry ◽  
1995 ◽  
Vol 21 (2) ◽  
pp. 160-169 ◽  
Author(s):  
Ludwig Spötl ◽  
Alessandra Sarti ◽  
Manfred P. Dierich ◽  
Johannes Möst

2020 ◽  
Vol 133 (14) ◽  
pp. jcs239814 ◽  
Author(s):  
Laura M. Westrate ◽  
Melissa J. Hoyer ◽  
Michael J. Nash ◽  
Gia K. Voeltz

ABSTRACTSecretory cargo is recognized, concentrated and trafficked from endoplasmic reticulum (ER) exit sites (ERES) to the Golgi. Cargo export from the ER begins when a series of highly conserved COPII coat proteins accumulate at the ER and regulate the formation of cargo-loaded COPII vesicles. In animal cells, capturing live de novo cargo trafficking past this point is challenging; it has been difficult to discriminate whether cargo is trafficked to the Golgi in a COPII-coated vesicle. Here, we describe a recently developed live-cell cargo export system that can be synchronously released from ERES to illustrate de novo trafficking in animal cells. We found that components of the COPII coat remain associated with the ERES while cargo is extruded into COPII-uncoated, non-ER associated, Rab1 (herein referring to Rab1a or Rab1b)-dependent carriers. Our data suggest that, in animal cells, COPII coat components remain stably associated with the ER at exit sites to generate a specialized compartment, but once cargo is sorted and organized, Rab1 labels these export carriers and facilitates efficient forward trafficking.This article has an associated First Person interview with the first author of the paper.


Blood ◽  
1976 ◽  
Vol 47 (2) ◽  
pp. 189-195 ◽  
Author(s):  
TA Lane ◽  
SK Ballas ◽  
ER Burka

Abstract Human reticulocytes are capable of synthesizing membrane lipids from 14C-glycerol de novo. In both sickle and nonsickle reticulocytes the majority of 14C-glycerol was incorporated into phospholipids, primarily phosphatidylserine and phosphatidylcholine. Incorporation into sphingomyelin was minimal. The most abundant neutral lipid synthesized was triglyceride. In the absence of sickling, the rate of lipid synthesis in sickle reticulocytes was similar to that of nonsickle reticulocytes. With the induction of sickling under anoxic conditions sickle reticulocytes showed a prompt increase in the rate of lipid synthesis to an average of 69% above control values, while nonsickle reticulocytes under similar conditions decreased the rate of lipid synthesis. An increase in the rate of membrane lipid synthesis is associated in the mammalian erythroid cell with cell membrane damage. The findings further confirm that lesions of the erythroid cell membrane in sickle cell anemia are secondary to the sickling process itself.


1977 ◽  
Vol 55 (7) ◽  
pp. 1158-1165 ◽  
Author(s):  
Charles R. Bursey

Observations are presented on the wound repair process of the horseshoe crab, Limulus polyphemus. A cut, 1 × 40 × 3 mm, was made through the dorsal abdominal carapace and observations of the tissue at the wound site were made at 6, 24, 48, 96 h and 5, 10, 15, 30, 60, 90, 120, and 180 days. The wound was immediately plugged by a hemolymph coagulum and there was heavy infiltration of hemocytes into the area. Infiltrating hemocytes undergo a series of changes. The outermost cells hyalinize and form a thick layer between the cut ends of the exoskeleton. Pigmented epithelial cells migrate into the scar and produce a layer of cuticle under the cut exoskeleton. During the remaining period of observation, the cuticular scab enlarged and the cellular mass that filled the wound channel was lost through a series of changes that eventually restored the original tissue structure.


2018 ◽  
Vol 50 (2) ◽  
pp. 77-97 ◽  
Author(s):  
Qin M. Chen ◽  
Anthony J. Maltagliati

The NFE2L2 gene encodes the transcription factor Nrf2 best known for regulating the expression of antioxidant and detoxification genes. Gene knockout approaches have demonstrated its universal cytoprotective features. While Nrf2 has been the topic of intensive research in cancer biology since its discovery in 1994, understanding the role of Nrf2 in cardiovascular disease has just begun. The literature concerning Nrf2 in experimental models of atherosclerosis, ischemia, reperfusion, cardiac hypertrophy, heart failure, and diabetes supports its cardiac protective character. In addition to antioxidant and detoxification genes, Nrf2 has been found to regulate genes participating in cell signaling, transcription, anabolic metabolism, autophagy, cell proliferation, extracellular matrix remodeling, and organ development, suggesting that Nrf2 governs damage resistance as well as wound repair and tissue remodeling. A long list of small molecules, most derived from natural products, have been characterized as Nrf2 inducers. These compounds disrupt Keap1-mediated Nrf2 ubquitination, thereby prohibiting proteasomal degradation and allowing Nrf2 protein to accumulate and translocate to the nucleus, where Nrf2 interacts with sMaf to bind to ARE in the promoter of genes. Recently alternative mechanisms driving Nrf2 protein increase have been revealed, including removal of Keap1 by autophagy due to p62/SQSTM1 binding, inhibition of βTrCP or Synoviolin/Hrd1-mediated ubiquitination of Nrf2, and de novo Nrf2 protein translation. We review here a large volume of literature reporting historical and recent discoveries about the function and regulation of Nrf2 gene. Multiple lines of evidence presented here support the potential of dialing up the Nrf2 pathway for cardiac protection in the clinic.


2003 ◽  
Vol 33 (12) ◽  
pp. 2331-2339 ◽  
Author(s):  
Alieta Eyles ◽  
Noel W Davies ◽  
Caroline Mohammed

The wound-associated wood that developed 17 months following artificial xylem injury in Eucalyptus globulus (Labill) and Eucalyptus nitens (Maiden) was examined anatomically and chemically. This new tissue located immediately adjacent to the wound site and termed "wound wood" was highly variable consisting of callus, altered wood of increased parenchyma density, and dark extractives, visible to the naked eye. Subsequent chemical analysis of crude wound wood extracts by HPLC coupled to negative ion electrospray mass spectrometry revealed the presence of a diverse range of polyphenolic compounds including hydrolysable tannins, proanthocyanidins, flavanone glycosides, and formylated phloroglucinol compounds. A number of polyphenols were unequivocally identified including engelitin, pedunculagin, and tellimagrandin I. Other compounds present in wound wood include various hydroxystilbene glycosides and volatile terpenes. The importance of the diverse range of secondary metabolites detected in wound wood is discussed in relation to tree wound repair responses.


1986 ◽  
Vol 103 (1) ◽  
pp. 265-275 ◽  
Author(s):  
M D Snider ◽  
O C Rogers

The recycling of cellular glycoproteins to the site of Golgi mannosidase I, an enzyme of asparagine-linked oligosaccharide synthesis, was studied in K562 human erythroleukemia cells. Cells were metabolically labeled in the presence of deoxymannojirimycin, a reversible inhibitor of Golgi mannosidase I. This generates glycoproteins with immature oligosaccharides in their normal locations. Transport to the mannosidase I compartment was then assessed by testing for the conversion of oligosaccharides into mature forms during reculture without deoxymannojirimycin. Transferrin receptor (TfR) was acted on by mannosidase I during reculture, suggesting that it returned to the region of the Golgi complex where this enzyme resides. The slow rate of this transport (t1/2 greater than 6 h) implies that it is probably different than TfR movement during transferrin internalization (t1/2 = 10-20 min) and TfR transport to the sialyltransferase compartment in the Golgi complex (t1/2 = 2-3 h) (Snider, M. D., and O. C. Rogers, 1985, J. Cell Biol., 100:826-834). The total cell glycoprotein pool was also transported to the mannosidase I compartment with a half-time of 4 h. Because this transport is 5-10 times faster than the rate of de novo glycoprotein synthesis in these cells, it is likely that most of the glycoprotein traffic through the Golgi complex is composed of recycling molecules.


2014 ◽  
Vol 25 (12) ◽  
pp. 1867-1876 ◽  
Author(s):  
Emily M. Vaughan ◽  
Jae-Sung You ◽  
Hoi-Ying Elsie Yu ◽  
Amber Lasek ◽  
Nicolas Vitale ◽  
...  

After damage, cells reseal their plasma membrane and repair the underlying cortical cytoskeleton. Although many different proteins have been implicated in cell repair, the potential role of specific lipids has not been explored. Here we report that cell damage elicits rapid formation of spatially organized lipid domains around the damage site, with different lipids concentrated in different domains as a result of both de novo synthesis and transport. One of these lipids—diacylglycerol (DAG)—rapidly accumulates in a broad domain that overlaps the zones of active Rho and Cdc42, GTPases that regulate repair of the cortical cytoskeleton. Formation of the DAG domain is required for Cdc42 and Rho activation and healing. Two DAG targets, protein kinase C (PKC) β and η, are recruited to cell wounds and play mutually antagonistic roles in the healing process: PKCβ participates in Rho and Cdc42 activation, whereas PKCη inhibits Rho and Cdc42 activation. The results reveal an unexpected diversity in subcellular lipid domains and the importance of such domains for a basic cellular process.


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