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Biomedical subjects

L Josefsson

Publications and source records attributed to L Josefsson.

At least 19 recordsLinked to original sources
PubMed1997

Cellular signalling of PCH-induced pigment aggregation in the crustacean Macrobrachium potiuna erythrophores.

The cellular system responsible for the transduction of the pigment-concentrating hormone (PCH) signal was investigated in erythrophores of the freshwater shrimp, Macrobrachium potiuna. Dose-response curves to the hormone were determined in the absence and in the presence of several drugs that affect sequential steps of the Ca(2+)-dependent signalling pathway. Additionally, the ability of forskolin to induce pigment dispersion was evaluated. Neomycin sulphate (10(-4) and 10(-3) mol.l-1), trifluoperazine (10(-5) and 10(-4) mol.l-1), 1-(5-isoquinolinesulfonlyl)-2-methylpiperazine (10(-7) and 10(-5) mol.l-1) and okadaic acid (10(-7) mol.l-1) significantly (P < 0.05) decreased the responses to PCH. However, okadaic acid at low concentration (10(-9) mol.l-1) and cyclosporin A (10(-6) and 10(-5) mol.l-1) did not significantly (P > 0.05) affect PCH activity. Forskolin (10(-4) mol.l-1) was able to half-maximally reverse the hormone-induced aggregation. Our results suggest that the pigment-concentrating hormone induces pigment aggregation through a Ca(2+)-dependent pathway with a posteriori phosphatase activation, probably the serine/threonine phosphatase 1.

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
PubMed1995

Cytoskeleton and PCH-induced pigment aggregation in Macrobrachium potiuna erythrophores.

Herein we report the effects of microtubule- and actin-like filament disrupting drugs, as well as the microtubule stabilizer taxol, on PCH-induced pigment granule aggregation within erythrophores of the freshwater crustacean Macrobrachium potiuna. Dose-response curves (DRCs) to the pigment-concentrating hormone PCH were determined under control and experimental conditions to evaluate the effects elicited by the cytoskeleton-affecting drugs. Colchicine, at temperatures 22 degrees C and 4 degrees C, and vinblastine significantly inhibited the aggregating response to PCH and affected the dynamics of the process, as shown by the change in the slope of the regression curve calculated from the DRCs. Lumicolchicine, a colchicine analogue with no affinity for tubulin, also inhibited pigment migration, though no change in the slope of the regression curve was observed. The inhibitory effects of lumicolchicine demonstrate that changes in sites other than cytoskeleton, such as membrane permeability, may also cause a decrease in the PCH-induced aggregating responses and that the colchicine effects may result from its action on cellular sites additional to the cytoskeleton. Taxol, a microtubule stabilizer, did not affect the DRC to PCH, and DMSO improved the PCH-evoked responses, pointing out to the maintenance of tubulin in the polymerized state as the appropriate condition for aggregation. Cytochalasin B, an actin-like filament disrupter, diminished the aggregating responses to the hormone, with no change in the slope of the regression curve, indicating that these elements take part in the process and that cytosolic calcium rise, sol/gel transformations and endoplasmic reticulum motility may well play an important role in granule migration. It is suggested that microtubules are steadily polymerized as a requirement for pigment aggregation and that process is biphasic, the initial phase being dependent on the microtubule integrity.

Animals↗
PubMed1989

Guidelines (1988) for training in clinical laboratory management. International Federation of Clinical Chemistry (IFCC) Education Division and International Union of Pure and Applied Chemistry (IUPAC) Clinical Chemistry Division Commission on Teaching of Clinical Chemistry.

Trainees in laboratory medicine must develop skills in laboratory management. Guidelines are detailed for laboratory staff in training, directors responsible for staff development and professional bodies wishing to generate material appropriate to their needs. The syllabus delineates the knowledge base required and includes laboratory planning and organisation, control of operations, methodology and instrumentation, data management and statistics, financial management, clinical use of tests, communication, personnel management and training, and research and development. Methods for achievement of the skills required are suggested. A bibliography of IFCC publications and other material is provided to assist in training in laboratory management.

Administrative Personnel↗
PubMed1989

International Federation of Clinical Chemistry Education Division and International Union of Pure and Applied Chemistry Clinical Chemistry Division Commission on Teaching of Clinical Chemistry. Guidelines (1988) for training in clinical laboratory management.

Trainees in laboratory medicine must develop skills in laboratory management. Guidelines are detailed for laboratory staff in training, directors responsible for staff development and professional bodies wishing to generate material appropriate to their needs. The syllabus delineates the knowledge base required and includes laboratory planning and organisation, control of operations, methodology and instrumentation, data management and statistics, financial management, clinical use of tests, communication, personnel management and training, and research and development. Methods for achievement of the skills required are suggested. A bibliography of IFCC publications and other material is provided to assist in training in laboratory management.

Chemistry, Clinical↗
PubMed1989

International Federation of Clinical Chemistry (IFCC), Education Division. Guidelines (1988) for training in clinical laboratory management.

Trainees in laboratory medicine must develop skills in laboratory management. Guidelines are detailed for laboratory staff in training, directors responsible for staff development and professional bodies wishing to generate material appropriate to their needs. The syllabus delineates the knowledge base required and includes laboratory planning and organisation, control of operations, methodology and instrumentation, data management and statistics, financial management, clinical use of tests, communication, personnel management and training, and research and development. Methods for achievement of the skills required are suggested. A bibliography of IFCC publications and other material is provided to assist in training in laboratory management.

Chemistry, Clinical↗
PubMed1983

Invertebrate neuropeptide hormones.

The development of a long-term research program on the neurosecretory hormones of arthropods is described. The purification and full characterization of the first invertebrate neurohormones, the red pigment-concentrating hormone (RPCH) and the distal retinal pigment hormone (DRPH) demonstrated that they are peptides, an octapeptide and an octadecapeptide, respectively. Physiological function studies with the pure hormones and their synthetic preparations showed that the RPCH acts as a general pigment-concentrating hormone (PCH), and that the DRPH, in addition to its light-adaptive function, also constitutes a general pigment-dispersing hormone (PDH). In the regulation of the color-adaptation of the animals, the two hormones act as antagonists. The chromatophorotropic activities are widely distributed within the arthropod neuroendocrine systems. Purification of the pigment-concentrating activities from the locust corpora cardiaca lead to the isolation and characterization of the first insect neurohormones, the adipokinetic hormones (AKH I and AKH II). These two hormones, AKH I being a decapeptide and AKH II being an octapeptide, are close structural analogs to the crustacean PCH, demonstrating a common evolution of arthropod neurohormones. The hormones of this PCH-family all cross-react, but structure-function studies of the hormones show that quite different parts of their structure are involved in their binding to the various receptors.

Animals↗
PubMed1979

Structure-function studies on red pigment-concentrating hormone, II. The significance of the C-terminal tryptophan amide.

The significance of the C-terminal tryptophan residue of the red pigment-concentrating hormone (RPCH: Glu-Leu-Asn-Phe-Ser-Pro-Gly-Trp-NH2) regulating the blanching of the crustacean chromatophores has been investigated. RPCH and a number of analogues that differ only in the C-terminal part of the hormone, have been synthesized and assayed for biological activity on the shrimp Leander adspersus. It has been shown that the indole skeleton of tryptophan is an absolute requirement for the biological activity of the hormone. To provide maximum response the tryptophan must be blocked as the amide. The activity of synthetic [Tyr4]RPCH and adipokinetic hormone (AKH) purified from Schistocerca gregaria has been compared with the activity of synthetic RPCH.

Amides↗
PubMed1978

Structure-function studies on red pigment-concentrating hormone; the significance of the terminal residues.

The significance of the terminal residues of the red pigment-concentrating hormone (RPCH: Glu-Leu-Asn-Phe-Ser-Pro-Gly-Trp-NH2) for its blanching effect on crustacean chromatophores has been investigated. The chemical synthesis of the following small analogues, starting from the C-terminal amino acid are described: Ac-Trp-NH2, Boc-Gly-Trp-NH2, Ac-Gly-Trp-NH2, Gly-Trp-NH2, Ac-Pro-Gly-Trp-NH2, Glu-Trp-NH2, Glu-Pro-Gly-Trp-NH2, Ac-Pro-Gly and Glu-Pro-Gly-NH2. Assay of the biological activity of the various synthetic compounds in the shrimp Leander adspersus has established that only the C-terminal tryptophan residue is indispensable for the blanching effect of the hormone, although elongation of the chain length improves its potency.

Animals↗
PubMed1977

Intracellular hydrolysis of peptides.

Purification of the first dipeptidases, glycylleucine dipeptidase (EC 3.4.13.2) and proline dipeptidase (EC 3.4.13.9), from intestine, have shown them to be true dipeptidases, hydrolysing only dipeptides in their laevo form. Although they have quite different specificities they show great similarities in their chemical and physicochemical properties. Specific antibodies against the two dipeptidases have been raised and used in combination with the double-layer immunofluorescent staining technique to study their histological localization in the small intestine. The results conclusively demonstrated that both glycylleucine dipeptidase and proline dipeptidase are exclusively located in the cytosol of the enterocytes. This location fits well with the current idea of transport and hydrolysis of dipeptides in the intestine where the dipeptides are taken by a specific transport mechanism and are hydrolysed intracellularly. Although it is tempting to add a specific role for the dipeptidases of the enterocytes in the final digestion of exogenous proteins, studies so far have shown their identity with the corresponding dipeptidases of other tissues. It is therefore suggested that their role in the digestion process may be based entirely on their abundance in the intestine.

Animals↗
PubMed1977

Intestinal brush border peptidases.

A brush-border-specific antiserum was raised in rabbits, with Triton X-100-solubilized brush border proteins from pig intestine being used as antigens. The antiserum was used in immunoelectrophoretic studies of brush border proteins solubilized with Triton X-100. Five immunoprecipitates were obtained which corresponded to microsomal aminopeptidase (EC 3.4.11.2), asparate aminopeptidase (EC 3.4.11.7), lactase (beta-galactosidase, EC 3.2.1.23), maltase (exo-1,4-alpha-glucosidase, EC 3.2.1.3) and sucrase-isomaltase (sucrose alpha-glucohydrolase, EC 3.2.1.48). A faint immunoprecipitate was also found for the glycylprolyl dipeptidyl peptidase (EC 3.4.14.-). The brush border proteins were solubilized on a large scale from a brush border membrane preparation by the use of Triton X-100; the peptidases obtained were homogeneous in size and had hydrophobic properties. By chromatography on columns of concanavalin A-Sepharose, hydroxyapatite, Ultrogel AcA 34, DEAE-cellulose and immunosorbent, gamma-glutamyl transpeptidase (gamma-glutamyl transferase, EC 2.3.2.2) and microsomal aminopeptidase were each isolated in separate fractions. Glycylprolyl dipeptidyl peptidase and asparate aminopeptidase were obtained in another fraction. Immunoelectrophoretic, inhibitor and chromatographic studies showed that the intestinal brush border peptidases are similar to the corresponding particulate peptidases obtained from other organs.

Amino Acids↗
PubMed1977

Histological localization of two dipeptidases in the pig small intestine and liver, using immunofluorescence.

Antibodies were raised in rabbits against glycylleucine dipeptidase (EC 3.4.13.2) and proline dipeptidase (EC 3.4.13.9) purified from the pig. IgG fractions were isolated and purified by affinity chromatography on Sepharose (dipeptidase) columns and then used in histological studies on the small intestine and the liver from pig, using the double layer immunofluorescence-staining technique. In the small intestine the dipeptidases were predominantly localized in the cytoplasm of the enterocytes. A reaction was also seen in the leukocyte cytoplasm in the stroma of the small intestine. The dipeptidases were present in the villi but not in the crypts. In the liver the dipeptidases were localized in the cytoplasm of the hepatocyte, but strong fluorescence was also obtained in the epithelium of the bile ducts. Glycylleucine dipeptidase and proline dipeptidase have been isolated from liver tissue and they were shown to be immunologically identical with the purified intestinal dipeptidases.

Animals↗