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B Rozell

Publications and source records attributed to B Rozell.

35 records · Page 2Linked to original sources

Differing expression of insulin-like growth factor I in the developing and in the adult rat cerebellum.

Insulin-like growth factor I (IGF-I; somatomedin C) is a trophic peptide of importance for the development of several tissues and organs. In the present study we have mapped the cellular distribution and dynamic changes of IGF-I immunoreactivity in the rat cerebellum from its postnatal development to maturity. In vitro hybridization of IGF-I mRNA was used to demonstrate that the IGF-I immunoreactive material was synthesized in the cerebellum during a limited time period of cerebellar differentiation. IGF-I immunoreactivity was absent in primordial nerve cells but was present in neuroglial cells during the first two days after birth and then rapidly increased in intensity in the latter during the next few days. Proliferative nerve cells in the external granular layer did not express IGF-I immunoreactivity, while migrating and differentiating nerve cells as well as neuroglial cells showed intense labelling. Starting about 2 weeks postnatally, the IGF-I immunoreactivity declined, first in the neuroglial cells and eventually in the nerve cells. No IGF-I immunoreactivity could be demonstrated in the normal adult cerebellum. Colchicine pretreatment did, however, enable demonstration of IGF-I immunoreactivity in adult cerebellar nerve cells but not in neuroglial cells. In vitro hybridization revealed IGF-I mRNA in the developing cerebellum but only at very low levels in the adult cerebellum. It is concluded that IGF-I is likely to be a factor of importance for the development and maturation of nerve cells and neuroglial cells in the brain.(ABSTRACT TRUNCATED AT 250 WORDS)

Age Factors↗

Thioredoxin and thioredoxin reductase show function-related changes in the gastric mucosa: immunohistochemical evidence.

Low levels of thioredoxin and thioredoxin reductase immunoreactivity were demonstrated immunohistochemically in rat gastric epithelial cells. The intensity was influenced by feeding and fasting, the former resulting in diminished reactions. Acute vagotomy, which abolishes basal acid secretion, resulted in a strongly increased thioredoxin immunoreactivity in all gastric epithelial cells. Stimulation of vagotomized rats with pentagastrin and carbachol reduced the levels of thioredoxin and thioredoxin reductase. Atropine and omeprazole (in stimulated, vagotomized rats) completely inhibited acid secretion, but caused different effects on the thioredoxin levels of gastric cells. Atropine restored the thioredoxin immunoreactivity in most gastric epithelial cells to that of the unstimulated, vagotomized controls. Omeprazole, however, did not reverse the effects of stimulation, and, except in the parietal cells, weaker fluorescence was observed. Similar reaction patterns were seen for thioredoxin reductase, although at lower staining intensities. The results demonstrate that thioredoxin and thioredoxin reductase are expressed in resting cells, and to a lower extent in cells with ongoing secretion.

Animals↗

Ultrastructural demonstration of thioredoxin and thioredoxin reductase in rat hepatocytes.

Electron microscopic immunocytochemistry, in conjunction with the immunogold technique, was used to demonstrate the ultrastructural localization of thioredoxin and thioredoxin reductase in rat liver hepatocytes. Gold particles representing thioredoxin and thioredoxin reductase antigenic sites were found throughout the cell, but particularly densely associated with the granular endoplasmic reticulum and the cisternae of the Golgi complex. Label was also distributed over the cytosol and in the chromatin of the nucleus. We conclude that thioredoxin and thioredoxin reductase are present in several different cellular compartments including the nucleus. In particular, the enrichment of thioredoxin and thioredoxin reductase to the endoplasmic reticulum is consistent with functions in protein processing, secretion and the formation of nascent protein disulfides.

Animals↗

Rapid axoplasmic transport of insulin-like growth factor I in the sciatic nerve of adult rats.

Somatomedin C (Sm-C; insulin-like growth factor I; IGF-I) is a polypeptide (Mr 7649), often dependent on growth hormone (GH), with trophic effects on several different tissues. Monospecific IGF-I antisera were used to investigate its localization in the sciatic nerve and corresponding nerve cells, as well as its possible axoplasmic transport in the adult rat. IGF-I-like immunoreactivity was demonstrated in anterior horn motor nerve cells in the spinal cord and in spinal- and autonomic ganglion nerve cells. Faint IGF-I immunoreactivity was under normal conditions observed in axons of the sciatic nerve and in the Schwann cells. Using crush technique, accumulation of IGF-I immunoreactivity was seen in dilated axons within 2 h, both proximal and distal to the crush. However, only a small fraction of the anterogradely transported IGF-I immunoreactive material could be demonstrated to be transported in retrograde direction. Colchicine injected proximal to a crush prevented accumulation of IGF-I immunoreactivity proximal to the crush, but not distal to it. IGF-I-immunoreactive material is synthesized in the cell bodies of peripheral sensory and motor nerve cells. It is transported at rapid rates in the axoplasm of the sciatic nerve of adult rats both in anterograde and retrograde directions. We propose that axonally transported IGF-I may be released and exert trophic influence on innervated cells, tissues and organs.

Animals↗

Immunohistochemical localization of thioredoxin and thioredoxin reductase in mouse exocrine and endocrine pancreas.

Thioredoxin and thioredoxin reductase (NADPH-oxidized thioredoxin oxidoreductase, E.C. 1.6.4.5) have been proposed to be involved in several thiol-dependent reduction-oxidation reactions in cells. Both proteins have been immunohistochemically demonstrated in the periphery of the cytoplasm and in cytoplasmic granules of acinar and islet cells in mouse pancreas. In animals fed ad libitum, the staining for thioredoxin was more intense in the exocrine acinar cells than in the islet cells, whereas that for thioredoxin reductase was more intense in the endocrine than in the exocrine pancreas. In the islets of fed mice all endocrine cell types showed about the same staining intensity for thioredoxin, while thioredoxin reductase was greatly enriched in the somatostatin-containing D cells. Starvation overnight caused an increased staining for both proteins in the acinar cells as well as in the islets. Under conditions of starvation, thioredoxin reductase, in contrast to thioredoxin, appeared to increase preferentially in the islet B cells, as compared with the D cells. Cysteamine treatment reduced the staining for somatostatin and for thioredoxin reductase in the D cells without any obvious effect on the other pancreatic cells. The results are compatible with a role for thioredoxin and thioredoxin reductase in secretion.

Aging↗

Different cellular distribution of thioredoxin and subunit M1 of ribonucleotide reductase in rat tissues.

The cellular distribution of thioredoxin and protein M1 of ribonucleotide reductase in adult rat tissues was investigated with immunohistochemical techniques using specific antisera. Tissues with high or low frequency of either mitotic or meiotic cell divisions were compared. Thioredoxin was demonstrated in many cells types that showed no detectable protein M1 of ribonucleotide reductase. A few cell types with protein M1 immunoreactivity also contained immunoreactive thioredoxin. However, in most cells no such co-localization could be demonstrated. This lack of correlation between cells containing subunit M1 of ribonucleotide reductase and the thioredoxin indicates that thioredoxin is not the physiologist hydrogen donor for ribonucleotide reductase in rat tissues and that the expression of two enzymes is differently regulated.

Animals↗

Disturbed expression of ribonucleotide reductase and cytokeratin polypeptides in focal epithelial hyperplasia. An immunohistochemical study using monoclonal antibodies.

Four cases of focal epithelial hyperplasia (FEH) were studied immunohistochemically, using monoclonal antibodies against the M1 subunit of ribonucleotide reductase and different cytokeratin polypeptides. The FEH lesions showed, compared to normal oral mucosa, extensive alterations in their staining patterns. This included ectopic suprabasal M1 staining and the novel expression of cytokeratin polypeptides differing from those previously reported for other HPV infections. The results are discussed in relation to the causative agent, human papillomavirus, and its expression in focal epithelial hyperplasia.

Epithelium↗

Evidence indicating trophic importance of IGF-I in regenerating peripheral nerves.

The mechanisms influencing regeneration of peripheral nerves are incompletely known, but growth factors are supposed to play a key role. In the present study, we demonstrate, with the aid of immunohistochemical methods, that somatomedin C (Sm-C/insulin-like growth factor I/IGF-I) rapidly increased from low to high concentrations, reaching peak values in 2 weeks, in regenerating sciatic nerves of adult rats. In addition, IGF-I was demonstrated extracellularly, never observed in the control nerves. Reactive Schwann cells appeared to be the major source for IGF-synthesis. Higher concentrations were seen in tubulated nerves as compared to sutured ones. It is proposed that IGF-I exerts important growth supporting effects on regenerating peripheral nerves.

Animals↗

Axoplasmic transport of thioredoxin and thioredoxin reductase in rat sciatic nerve.

Thioredoxin and thioredoxin reductase were localized immunohistochemically in the rat sciatic nerve by immunofluorescence using specific rabbit antisera. Both proteins showed strong immunoreactivity in the cytoplasm of Schwann cells and at the nodes of Ranvier. The axoplasm of myelinated axons also showed a low, evenly distributed immunoreactivity for both proteins. A single or double crush of the nerve caused accumulation of immunoreactivity in dilatated axons both proximally and distally to the crush for up to 8 h. Local cooling of the nerve or subepineural injection of either colchicine or vinblastine prevented the accumulation indicating a role of microtubules. The results showed that thioredoxin and thioredoxin reductase are synthesized in nerve cell bodies and rapidly transported in axons both in anterograde and retrograde directions.

Animals↗

Intermediate filaments in cultured human pleomorphic adenomas. An immunohistochemical study.

Primary cultures of 9 benign human pleomorphic adenomas were analyzed by immunofluorescence and antibodies against the different intermediate filaments and microfilaments. The cultured cells were also cytogenetically characterized by G- and C-banding techniques. The adenoma cells expressed at least three different classes of intermediate filaments, viz. prekeratin, vimentin and glial fibrillary acidic protein (GFA). No correlation between chromosomal pattern and intermediate filament expression was found. The frequency of cells stained for each of the different antibodies varied considerably among the tumours. Prolonged culturing appeared to induce a reduction of cells positive for prekeratin. This was probably a true loss of antigens and not an effect of overgrowth of stromal cells. It is concluded that the cells studied, on the basis of several criteria, are of neoplastic origin. This in vitro system appears to be well suited for further histogenetic studies on pleomorphic adenomas.

Actin Cytoskeleton↗

Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats.

Rabbit antisera against homogeneous rat liver thioredoxin and thioredoxin reductase (NADPH-oxidized thioredoxin oxidoreductase, E.C. 1.6.4.5) were prepared and used for immunohistochemical analysis in adult rats. Immunoreactive thioredoxin and thioredoxin reductase were widely distributed in tissues and organs, but varied a lot between cell types. Generally, epithelial cells, neuronal cells and secretory cells, both exocrine and endocrine, showed high immunoreactivity whereas mesenchymal cells with exceptions showed low activity. Surface lining epithelial and keratinizing cells showed high activity. The immunofluorescence was localized in the cytoplasm of cells with enrichments at secretory granules, at the plasma membrane or in the subplasma membrane zone. Variations in secretory cells were seen related to feeding and starvation and to metabolic activity. The distribution of thioredoxin and thioredoxin reductase is compatible with function in thiol-disulfide interchange reaction related to protein synthesis, intracellular transport and different forms of secretion.

Animals↗

Localization of ribonucleotide reductase in mammalian cells.

The results of immunocytochemical studies using two different monoclonal antibodies against the M1 subunit of ribonucleotide reductase show an exclusively cytoplasmic localization of this subunit both in cultured MDBK and mouse 3T6 cells, and in cells from various rat tissues. By fluorescent light microscopy, there is a diffuse staining of the cytoplasm, while by electron microscopy the immunoreactive material appears to be associated with ribosomes. In the rat tissues, only actively dividing cells show M1-specific immunofluorescence revealing a strong correlation between the presence of protein M1 and DNA synthesis. Therefore M1 immunofluorescence could be used to study cell proliferation in normal, inflammatory or neoplastic tissue. A lesser variation in M1 staining is observed between individual cells in tissue culture, where most cells are positive, but neither here nor in the tissues examined are any cells with nuclear staining detected. We interpret our results to mean that in mammalian cells ribonucleotide reduction takes place in the cytoplasm and from there the deoxyribonucleotides are transported into the nucleus to serve in DNA synthesis.

Animals↗

Cytoskeletal disarrangement in rat intestinal epithelium after in vivo exposure to secretagogues.

Cholera toxin (CT) and E. coli heat-labile enterotoxin (LT) induced hypersecretion in the small intestine, as did cytochalasin B and dibutyryl-cyclic AMP (DB-cAMP). The cytoskeleton in the apical part of the intestinal epithelial cells was disorganized after challenge with either of the four secretagogues, but not cholera B-subunit toxoid, as revealed by immunofluorescence microscopy using actin and the intermediate filament keratin as markers. Electron microscopic analysis confirmed the re-engagement of the terminal web and the appearance of short microvilli lacking most of their normally observed central core of actin filaments. Pretreatment with chloroquine prevented cytoskeletal disorganization as well as hypersecretion by CT, but not by cytochalasin B. A similar effect was achieved with chloroquine on CT-induced fluid secretion, while chlorpromazine inhibited the fluid response to cytochalasin B as well as to CT. The observed cytoskeletal re-engagement might be one of the reactions behind enterotoxic diarrhoea.

Animals↗

Expression of E-cadherin during craniofacial development.

The cell adhesion molecule E-cadherin is assumed to play an important role in organogenesis and histogenesis. We have analyzed the presence of E-cadherin during normal and disturbed craniofacial development with respect to palate and tooth formation by immunohistochemistry using a rat monoclonal antibody (DECMA-1) and by in situ hybridization using an oligonucleotide probe. Cleft palate was induced by retinoic acid (RA) treatment of pregnant dams. Normal and RA-treated fetuses of gestational days 14-18 were examined. E-cadherin was present in epithelia of both ectodermal and endodermal origin, including developing teeth and epithelia of the palate as well as respiratory and oral epithelia. The expression level of E-cadherin increased with age and differentiation. In normal fetuses, at day 18, the expression was higher in the epithelia of the oral cavity than in the forming nasal cavity. The expression pattern of E-cadherin implies that this molecule has a role during normal development of the epithelia of the craniofacial complex.

Animals↗