Biomedical subjects

S Skulstad

Publications and source records attributed to S Skulstad.

4 recordsLinked to original sources

PubMed2001

[Acute infectious myelitis].

BACKGROUND: Acute myelitis is a clinical condition affecting the motor, sensor or autonomic function of the spinal cord. The etiology is often unknown, although a diversity of pathogens have been associated with acute myelitis. MATERIALS AND METHODS: Based on relevant literature we present an overview of the most important pathogens responsible for infectious acute myelitis in northern Europe, as well as recommendations regarding diagnostic guidelines. RESULTS: The pathogenic mechanisms are only partly known. Both replication of the pathogen, cellular defence mechanisms after invasion of the central nervous system, and the immune system seem to be important for the neurological damage. INTERPRETATION: Identification of a causative agent is important for the etiologic diagnosis and offers the possibility of specific treatment.

Acute Disease↗

PubMed2000

Blood flow and the degree of shunting through the ductus venosus in the human fetus.

OBJECTIVES: Our goal was to determine the degree of shunting through the ductus venosus in the human fetus and its possible association with fetal growth. STUDY DESIGN: Blood flow in the umbilical vein and the fetal ductus venosus was measured in 197 low-risk pregnancies in a cross-sectional ultrasonographic study at a gestational age of 18 to 41 weeks. The degree of shunting was compared to birth weight and ponderal index. RESULTS: The average fraction shunted through the ductus venosus was 28% to 32% at 18 to 20 weeks, decreased to 22% at 25 weeks, and reached 18% at 31 weeks (with wide ranges expressed in the 10th and 90th percentiles). Fetuses <10th percentile for birth weight had significantly more shunting (1.4%) than those >90th percentile (95% confidence interval, 0.1%-2.7%; P =.04). CONCLUSIONS: In the human fetus a higher proportion of umbilical blood is directed to the liver and less is shunted through the ductus venosus, in comparison with what has previously been shown in animal experiments.

Blood Circulation↗

PubMed1995

Labeling of surface proteins of herpes simplex virus type 1 using a modified biotin-streptavidin system.

Methods of labeling surface proteins on herpes simplex virus (HSV) which have minimal effect on the biological activity of the virus are useful for the study of both the localization and function(s) of surface proteins. The present work describes a procedure using a water-soluble biotin compound, sulfo-NHS-biotin, which is unable to penetrate biological membranes and reacts with primary amines in proteins. Labeled proteins were detected by binding of [125I]streptavidin. Specific reaction with surface proteins was shown in Western blots using antibodies against selected proteins in the envelope or in the tegument. Proteins susceptible to iodination were also biotinylated, but the efficiency of labeling varied from one protein to another. As a result of freezing and thawing of the virus, as well as the manipulations involved in Ficoll gradient purification, internal proteins were labeled. The infectivity of the virus was reduced by approximately 40% after biotinylation. Labeled viruses were visualized by fluorescein isothiocyanate-conjugated streptavidin, and seen as distinct spots on the surface of the cells.

Animals↗

PubMed1994

The herpes simplex virus type 1 particle: structure and molecular functions. Review article.

This review is a summary of our present knowledge with respect to the structure of the virion of herpes simplex virus type 1. The virion consists of a capsid into which the DNA is packaged, a tegument and an external envelope. The protein compositions of the structures outside the genome are described as well as the functions of individual proteins. Seven capsid proteins are identified, and two of them are mainly present in precursors of mature DNA-containing capsids. The protein components of the 150 hexamers and 12 pentamers in the icosahedral capsid are known. These capsomers all have a central channel and are connected by Y-shaped triplexes. In contrast to the capsid, the tegument has a less defined structure in which 11 proteins have been identified so far. Most of them are phosphorylated. Eleven virus-encoded glycoproteins are present in the envelope, and there may be a few more membrane proteins not yet identified. Functions of these glycoproteins include attachment to and penetration of the cellular membrane. The structural proteins, their functions, coding genes and localizations are listed in table form.

Capsid↗