Morphological and functional characteristics of arpa (receptor potential absent) visual mutant of the blowfly (Calliphora erythrocephala)

1989 ◽  
Vol 165 (3) ◽  
pp. 333-341 ◽  
Author(s):  
P. Torkkeli ◽  
M. Weckstr�m ◽  
E. Kouvalainen ◽  
M. J�rvilehto
Keyword(s):  
Receptor Potential ◽  
Functional Characteristics ◽  
Calliphora Erythrocephala ◽  
Visual Mutant

TheRpa(Receptor Potential Absent) Visual Mutant of the Blowfly (Calliphora Erythrocephala) is Deficient in Phospholipase C in the Eye

1994 ◽  
Vol 9 (3) ◽  
pp. 177-187 ◽  
Author(s):  
Richard R. McKay ◽  
Karen Miller ◽  
Matti Weckström ◽  
Päivi Torkkeli ◽  
Matti Järvilehto ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Receptor Potential ◽  
Calliphora Erythrocephala ◽  
Visual Mutant

Fine Structure of the Malpighian Tubules of the Mosquito, Culex pipiens

1971 ◽  
Vol 29 ◽  
pp. 402-403
Author(s):  
Brendan Clifford
Keyword(s):  
Fine Structure ◽  
Culex Pipiens ◽  
Stellate Cell ◽  
Malpighian Tubule ◽  
Cell Types ◽  
Instar Larva ◽  
Malpighian Tubules ◽  
Calliphora Erythrocephala ◽  
Distinct Cell ◽  
Basal Plasma

An ultrastructural investigation of the Malpighian tubules of the fourth instar larva of Culex pipiens was undertaken as part of a continuing study of the fine structure of transport epithelia.Each of the five Malpighian tubules was found to be morphologically identical and regionally undifferentiated. Two distinct cell types, the primary and stellate, were found intermingled along the length of each tubule. The ultrastructure of the stellate cell was previously described in the Malpighian tubule of the blowfly, Calliphora erythrocephala by Berridge and Oschman.The basal plasma membrane of the primary cell is extremely irregular, giving rise to a complex interconnecting network of basal channels. The compartments of cytoplasm entrapped within this system of basal infoldings contain mitochondria, free ribosomes, and small amounts of rough endoplasmic reticulum. The mitochondria are distinctive in that the cristae run parallel to the long axis of the organelle.

Actin and α-tubulin immuno-EM labelings reveal differences in intra versus interphotoreceptor matrix

1990 ◽  
Vol 48 (3) ◽  
pp. 466-467
Author(s):  
Matti Järvilehto ◽  
Riitta Harjula
Keyword(s):  
Compound Eye ◽  
Frozen Section ◽  
Smooth Muscle Actin ◽  
Photoreceptor Cells ◽  
Immune Serum ◽  
Cell Organelles ◽  
Calliphora Erythrocephala ◽  
Optical Axes ◽  
Interphotoreceptor Matrix ◽  
Similar Kind

The photoreceptor cells in the compound eyes of higher diptera are clustered in groups (ommatidia) of eight receptor cells. The cells from six adjacent ommatidia are organized into optical units, neuro-ommatia sharing the same visual field. In those ommatidia the optical axes of the photopigment containing structures (rhabdomeres) are parallel. The rhabdomeres of the photoreceptor cells are separated from each other by an interstitial i.e innerommatidial space (IOS). In the photoreceptor cell body, besides of the normal cell organelles, a cellular matrix is a structurally apparent component. Similar kind of reticular formation is also found in the IOS containing some unidentified filamentary substance, of which composition and functional significance for optical properties of vision is the aim of this report.The prefixed (2% PA + 0.2% GA in 0.1-n phosphate buffer, pH 7.4, for 1h), frozen section blocks of the compound eye of the blowfly (Calliphora erythrocephala) were prepared by immuno-cryo-techniques. The ultrathin cryosections were incubated with antibodies of monoclonal α-tubulin and polyclonal smooth muscle actin. Control labelings of excess of antigen, non-immune serum and non-present antibody were perforated.

Inositol lipids and TRPC channel activation

2007 ◽  
Vol 74 ◽  
pp. 37-45 ◽  
Author(s):  
James W. Putney
Keyword(s):  
Plasma Membrane ◽  
Phospholipase C ◽  
Transient Receptor Potential ◽  
Calcium Signalling ◽  
Receptor Potential ◽  
Breakdown Product ◽  
Channel Activation ◽  
Inositol Lipids ◽  
Transient Receptor ◽  
Secondary Mechanism

The original hypothesis put forth by Bob Michell in his seminal 1975 review held that inositol lipid breakdown was involved in the activation of plasma membrane calcium channels or ‘gates’. Subsequently, it was demonstrated that while the interposition of inositol lipid breakdown upstream of calcium signalling was correct, it was predominantly the release of Ca2+ that was activated, through the formation of Ins(1,4,5)P3. Ca2+ entry across the plasma membrane involved a secondary mechanism signalled in an unknown manner by depletion of intracellular Ca2+ stores. In recent years, however, additional non-store-operated mechanisms for Ca2+ entry have emerged. In many instances, these pathways involve homologues of the Drosophila trp (transient receptor potential) gene. In mammalian systems there are seven members of the TRP superfamily, designated TRPC1–TRPC7, which appear to be reasonably close structural and functional homologues of Drosophila TRP. Although these channels can sometimes function as store-operated channels, in the majority of instances they function as channels more directly linked to phospholipase C activity. Three members of this family, TRPC3, 6 and 7, are activated by the phosphoinositide breakdown product, diacylglycerol. Two others, TRPC4 and 5, are also activated as a consequence of phospholipase C activity, although the precise substrate or product molecules involved are still unclear. Thus the TRPCs represent a family of ion channels that are directly activated by inositol lipid breakdown, confirming Bob Michell's original prediction 30 years ago.

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