Biomedical subjects

S Kappeler

Publications and source records attributed to S Kappeler.

5 recordsLinked to original sources

PubMed2001

[Engine-driven preparation of curved root canals: a platform to assess physical parameters].

The number of engine-driven rotary instruments available on the market is steadily increasing. These instruments enable clinicians to prepare better shaped root canals, however, rotary instruments have a higher risk for fracture than hand instruments. Unfortunately, the stresses placed on engine-driven rotary instruments in curved canals are insufficiently studied. The aim of this study was to develop a device which could measure more accurately the physical parameters influencing rotary instruments in curved canals. For this purpose, a specially designed machine was constructed to measure the torque which develops between the rotary instrument and the motor. Apical forces and penetration depths could also be directly measured in real time. A variety of other measurements was also possible because of other special set-ups integrated into the device. In the current study torque was assessed for GT-Files, size 35 with a .12 and sizes 20 with a .12 to .06 taper. In additions to preparations in simulated canals in plastic blocks, the "ISO 3630-1 specification for fracture moment" and "number of cycles till fatigue fracture" was measured. The findings indicated that when instruments were used for preparations, torques up to 40 Nmm were present. This exceeded the static fracture load, which was less than than 13 Nmm for the size 20 with .12 taper. In contrast, the number of rotations were more than 10 times lower when shaping canals in plastic blocks with a 5 mm radius of curvature than the number of rotations to fracture in the "cyclic fatigue test". This suggests that a GT-instrument could be used in ten canals. The apical force was always greater than 1 N and occasionally, 8 N or more was recorded. Further studies on natural teeth with varying canal geometries are required using the specially developed torsional machine to reduce the incidence of instrument fracture. In this way an efficient clinical potential can be confirmed for engine-driven rotary instruments in canal preparation.

Humans↗

PubMed1999

Alternative splicing of lactophorin mRNA from lactating mammary gland of the camel (Camelus dromedarius).

The objective of this study was to determine the corrected structure of lactophorin, a major whey protein in camel milk. The protein had 60.4% amino acid sequence identity to a proteose peptone component 3 protein from bovine whey and 30.3% identity to the glycosylation-dependent cell adhesion molecule 1 in mice. The N-terminal heterogeneity of the protein was a result of alternative mRNA splicing. About 75% of the protein was expressed as a long variant A with 137 amino acid residues and a molecular mass of 15.7 kDa; about 25% was as a short variant B with 122 amino acid residues and a molecular mass of 13.8 kDa. Both proteins are probably threefold phosphorylated. In contrast to the related proteins, no glycosylation was found in camel lactophorin. Because of this difference, specific interaction with carbohydrate binding proteins, as reported for the murine protein, can be excluded, and a function of the protein other than cell recognition or rotaviral inhibition is proposed. The concentration of lactophorin in camel milk was found to be about three times higher than the concentration of the bovine homologue in bovine milk. Pronounced similarities existed between the primary and secondary structures of bovine and camel proteins. We speculated that camel lactophorin has a similar function to that of bovine protein in milk, which is supposed to be the prevention of fat globule aggregation and the inhibition of spontaneous lipolysis by lipoprotein lipase.

Alternative Splicing↗

PubMed1998

Sequence analysis of Camelus dromedarius milk caseins.

Alpha s1-, alpha s2-, beta- and kappa-caseins from Somali camels (Camelus dromedarius) were purified by acid precipitation at pH 4.4, crudely separated into an alpha-CN and a beta-CN fraction and further purified by reversed-phase HPLC. Fragments of tryptic digests were sequenced. Amino acid patterns obtained were used to screen a cDNA library constructed from mRNA from lactating udder tissue. Full length clones corresponding to the four caseins were sequenced. The numbers of residues in the sequences deduced were alpha s1-CN 207, alpha s2-CN 178, beta-CN 217, kappa-CN 162. Percentage similarity to bovine proteins was alpha s1-CN A 39, alpha s2-CN 56, beta-CN 64, kappa-CN 56. Acid-precipitated casein of pooled milk was separated by reversed-phase HPLC and monitored at 220 nm, and its composition, estimated from peak integration, was (g/kg total casein) alpha s1-CN 220, alpha s2-CN 95, beta-CN 650, kappa-CN 35. Degrees of phosphorylation and glycosylation were determined by laser ionization mass spectrometry and sequence pattern analysis. Molecular masses determined were (kDa) alpha s1-CN A, 24.755 and 24.668; alpha s1-CN B, 25.293; alpha s2-CN 21.993; beta-CN, 24.900; kappa-CN 22.294-22.987. The pH values of the most probable isoelectric points were: alpha s1-CN A 6P 4.41, alpha s1-CN B 6P 4.40, alpha s2-CN 9P 4.58, beta-CN 4P 4.66, kappa-CN 1P, with ten sialic acid residues bound, 4.10.

Amino Acid Sequence↗

PubMed1994

A light- and temperature-entrained circadian clock controls expression of transcripts encoding nuclear proteins with homology to RNA-binding proteins in meristematic tissue.

To investigate physiological processes generated by endogenous circadian rhythms on the molecular level, we have identified clock-controlled genes in the long-day plant Sinapis alba L. A cDNA library was differentially screened using cDNA probes representing transcripts expressed at either the middle of the light period or the middle of the dark period. Two closely related groups of transcripts, Sagrp1 and Sagrp2, controlled by a circadian rhythm have been isolated. RNA blot analysis verified that transcript levels oscillate in plants grown in light/dark cycles with maxima between 'Zeitgeber' time (zt)8 and zt12 (8-12 h after onset of illumination) and minima around zt20. Steady-state mRNA levels continue to oscillate in plants shifted from light/dark cycles to constant light. No synchronous mRNA oscillations are found in plants grown from seed in constant light at constant temperature, suggesting that the clock has to be entrained initially. In contrast, when plants grown in constant light are exposed to rhythmic temperature shifts oscillations of steady-state Sagrp mRNA levels are induced, indicating that temperature acts as an alternative external stimulus (zeitgeber) other than light to entrain the oscillator. In situ hybridization reveals that both transcript groups are expressed predominantly in meristematic and growing tissue. Strong expression is observed in the leaf primordia of the shoot apex, the procambial strands, cambium and in all cell layers of young leaves around zt12. In contrast, little or no signal is found on tissue sections isolated at zt20. This indicates that the oscillator(s) regulating Sagrp transcript fluctuations operate(s) synchronously in different organs. For both transcript groups cDNAs were isolated corresponding to unspliced pre-mRNAs or to transcripts generated by the use of a second 5' splice site. The cDNAs corresponding to the fully spliced transcripts contain open reading frames for polypeptides of 16 kDa, each containing a putative N-terminal RNA recognition motif and a C-terminal region rich in glycine. The predicted proteins show strong homology to an ABA-inducible glycine-rich protein from maize embryos and to the mammalian RNA-binding protein A1 of the heterogeneous nuclear ribonucleoprotein complex involved in pre-mRNA splicing. The SaGRP protein fluctuates with a very low amplitude over light/dark cycles. Immunogold labeling demonstrates the presence of the SaGRP protein within the nucleus of the investigated meristematic cells of young leaves.

Amino Acid Sequence↗

PubMed1994

The proteins encoded by two tapetum-specific transcripts, Sa tap35 and Sa tap44, from Sinapis alba L. are localized in the exine cell wall layer of developing microspores.

By differential screening of a copy DNA (cDNA) library from flowering Sinapis alba L. apices against cDNAs from vegetative apices, two cDNA clones were isolated representing transcripts that are expressed transiently at an early stage of tapetum development. The Sa tap35 cDNA encodes a polypeptide with a predicted molecular weight of 12.7 kDa and an isoelectric point of 10.4. The sa tap44 cDNA codes for a putative 12.4-kDa polypeptide with an isoelectric point of 7.5. The deduced amino-acid sequences display 76% sequence identity and contain an N-terminal stretch of hydrophobic amino acids which has characteristics of secretory signal sequences. In-vitro transcription of the cDNAs and translation of the resulting RNAs in the presence of canine pancreatic microsomes demonstrates that the two proteins are translocated into the microsomes and that the putative preproteins are proteolytically processed to the mature forms. By immunoelectron microscopy the Sa TAP35 and Sa TAP44 proteins were detected at the developing peritapetal membrane between the tapetal cytoplasm and the adjacent middle layer of the anther wall. Furthermore, labelling was observed within the locule in association with globules resembling pro-Ubisch bodies which appeared at the tetrad stage. During the early vacuolate stage of microspore development the young exine was strongly labelled. The exine and the peritapetal membrane both are composed of sporopollenin, and the pro-Ubisch bodies are thought to contain sporopollenin precursors. Thus, Sa TAP35 and Sa TAP44 might be involved in sporopollenin formation and/or deposition.

ATP-Binding Cassette Transporters↗