PubMed HealthSearch

Biomedical subjects

M Locke

Publications and source records attributed to M Locke.

8 recordsLinked to original sources

Apolysis and the turnover of plasma membrane plaques during cuticle formation in an insect.

The apical plasma membranes of Calpodes epidermal cells have small fattened areas or plaques with an extra density upon their cytoplasmic face. The plaques are typically at the tips of microvilli. The are present during the deposition of fibrous cuticle and the cuticulin layer. Since the plaques are close (less than 15nm) to the sites where these kinds of cuticle first appear, they are presumed to have a role in their synthesis and/or deposition and orientation. When fifth stage larval cuticle deposition ceases prior to pupation, the plaques are lost as the area of the apical plasma membrane is reduced. The plaques pass from the surface into pinocytosis vesicles and multivesicular bodies where they are presumably digested. The loss of plaques occurs as the blood level of moulting hormone reaches a peak at the critical period after which the prothoracic glands are no longer needed for pupation. Apolysis or separation of the epidermis from the old cuticle is the stage when plaques are absent, the old ones have been lost but the new ones have yet to form. After the critical period, the epidermis prepared for pupation with a phase of elevated RNA synthesis at the end of which plaques and microvilli reform in time to secrete the new cuticulin layer and later the fibrous cuticle of the pharate pupa. There is a new generation of plaques for each moult and succeeding intermoult and each generation is involved in two kinds of cuticle deposition before involution and redifferentiation.

Animals

Nucleoprotein localization by bismuth staining.

Experiments on isolated mouse liver muclei involving enzyme digestion, the crosslinking of amino groups and alkaline hydrolysis demonstrate that bismuth binds to nucleoproteins through amino and phosphate groups. Analysis of the nucleoproteins extracted with salt and acid solutions in conjunction with bismuth staining after these treatments suggests that: (1) a bismuth amino group interaction occurs on ribonucleo-protein particles, histones and perhaps some non-histone chromosomal proteins, and (2) bismuth phosphate binding is specific for one, or all, of three distinct species of non-histone proteins. These results suggest that histones not tightly bound to DNA through their amino groups are present on interchromatin granules, the presumed transcriptionally active regions of chromatin. Phosphorylated non-histone proteins are also localized at these sites. Staining with heavy metals such as bismuth may be the best method for high resolution localization of nucleoproteins involved with regulating gene activity and maintaining chromatin structure.

Animals

Vertebrate Golgi complexes have beads in a similar position to those found in arthropods.

Insects and other arthropods have bead-like structures in Golgi complexes from all cell types. They are arranged in rings at the base of transition vesicles located near the smooth surface of the rough endoplasmic reticulum making the forming face of the Golgi complex and are only seen easily after staining in bismuth salts. Procedures used to demonstrate the beads in arthropod Golgi complexes do not selectively stain any structures where they would be expected to occur in several mouse and tadpole tissues. However, a faint pattern similar to the arthropod GC beads can be made out in the large GCs concerned in the formation of acrosomes during mouse spermatogenesis. Uranyl staining shows particles of about the same size and spacing as the beads of arthropod GCs. We conclude that vertebrate GCs may have beads that differ from arthropods in their staining properties.

Acrosome

The beads in the Golgi complex-endoplasmic reticulum region.

The region between the rough endoplasmic reticulum (ER) and the Golgi complex has been studied in a variety of insect cell types in an attempt to find a marker for the exit gate or gates from the ER. We have found that the smooth surface of the rough endoplasmic reticulum near Golgi complex transitional elements has beadlike structures arranged in rings at the base of transition vesicles. They occur in all insect cell types and a variety of other organisms. The beads can be seen only after staining in bismuth salts. They are 10-12 nm in diameter and are separated from the membrane and one another by a clear halo giving them a center to center spacing of about 27 nm. The beads are not sensitive to nucleases under conditions which disrupt ribosomes or remove all Feulgen staining material from the nucleus. Under conditions similar to those used to stain tissue, bismuth does not react in vitro with nucleic acids. The component of the beads that stains preferentially with bismuth is therefore probably not nucleic acid.

Bismuth

Golgi complex--endoplasmic reticulum transition region has rings of beads.

The smooth surface of the rough endoplasmic reticulum that makes the forming face of the Golgi complex has beadlike structures arranged in rings at the base of transition vesicles. The beads can only be seen easily after staining in bismuth salts. They are 10 to 12 nanometers in diameter and occur in a variety of cell types and organisms.

Animals