| 1. |
- Albabtain, Reham, et al.
(författare)
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Investigations of a Possible Chemical Effect of Salvadora persica Chewing Sticks
- 2017
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Ingår i: Evidence-based Complementary and Alternative Medicine. - : Hindawi Publishing Corporation. - 1741-427X .- 1741-4288.
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Tidskriftsartikel (refereegranskat)abstract
- Salvadora persica is commonly used chewing sticks in many parts of the world as an oral hygiene tool. This study measured the amount of benzyl isothiocyanate (BITC) released into the mouth and assessed its retention time in saliva. The study also tested if the released amount of BITC could potentially be antibacterial or cytotoxic. Twelve subjects brushed their teeth with fresh Miswak once, twice, and four times. The amount of BITC in the saliva and in the used brushes was quantified using gas chromatography-mass spectrometry. The antibacterial effect of BITC and Miswak essential oil (MEO) was tested against Haemophilus influenzae, Aggregatibacter actinomycetemcomitans, and Porphyromonas gingivalis. The cytotoxic effect on gingival fibroblasts and keratinocytes was tested using MTT. The highest amount of the active compounds was detected in saliva after using the Miswak tip for once and immediately. It significantly decreased when the Miswak tip was used more than once and thus after 10 min. The growth of the tested bacteria was inhibited by MEO and BITC in a dose dependent manner, P. gingivalis being the most sensitive. MTT assay showed that BITC and MEO were cytotoxic towards gingival fibroblasts while oral keratinocytes showed resistance. This study suggests that the Miswak tip should be cut before each use to ensure the maximum effect.
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| 2. |
- Petäjäniemi, Noora, et al.
(författare)
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Localization of laminin alpha4-chain in developing and adult human tissues
- 2002
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Ingår i: Journal of Histochemistry and Cytochemistry. - : SAGE Publications. - 0022-1554 .- 1551-5044. ; 50:8, s. 1113-1130
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Tidskriftsartikel (refereegranskat)abstract
- Recent studies suggest important functions for laminin-8 (Ln-8; alpha4beta1gamma1) in vascular and blood cell biology, but its distribution in human tissues has remained elusive. We have raised a monoclonal antibody (MAb) FC10, and by enzyme-linked immunoassay (EIA) and Western blotting techniques we show that it recognizes the human Ln alpha4-chain. Immunoreactivity for the Ln alpha4-chain was localized in tissues of mesodermal origin, such as basement membranes (BMs) of endothelia, adipocytes, and skeletal, smooth, and cardiac muscle cells. In addition, the Ln alpha4-chain was found in regions of some epithelial BMs, including epidermis, salivary glands, pancreas, esophageal and gastric glands, intestinal crypts, and some renal medullary tubules. Developmental differences in the distribution of Ln alpha4-chain were detected in skeletal muscle, walls of vessels, and intestinal crypts. Ln alpha4- and Ln alpha2-chains co-localized in BMs of fetal skeletal muscle cells and in some epithelial BMs, e.g., in gastric glands and acini of pancreas. Cultured human pulmonary artery endothelial (HPAE) cells produced Ln alpha4-chain as M(r) 180,000 and 200,000 doublet and rapidly deposited it to the growth substratum. In cell-free extracellular matrices of human kidney and lung, Ln alpha4-chain was found as M(r) 180,000 protein.
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| 3. |
- Wondimu, Zenebech
(författare)
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Expression, recognition and usage of laminin-8 (a4b1g1, Lm-411) by monocytes and neutrophils
- 2004
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Laminins (LNs) are a family of large alphabetagamma heterotrimeric glycoproteins found in all basement membranes (BMs). They are expressed in a tissue- and developmental stagespecific manner and implicated in vital cellular functions, including cell adhesion, migration and signaling. So far, eleven laminin chains (5alpha, 3beta and 3gamma) that assemble into 15 isoforms (LN-1 to 15, Lm-111 to Lm-523) have been identified. LN-8 (alpha4beta1gamma1, Lm-411) is a major LN isoform of vascular endothelial BM. Its expression and functional importance in blood platelets and lymphocytes have been documented. However, expression, recognition and utilization of LNs by blood monocytes and neutrophils are poorly understood. Monocytes and neutrophils originate from a common myeloid progenitor cell and are crucial cellular elements in both innate and adaptive immunity. In response to inflammatory signals, these leukocytes extravasate and migrate to the affected tissue. Leukocyte extravasation is a multi-step process involving sequential participation of various adhesion molecules. While the initial steps, such as leukocyte interaction with endothelium, are well characterized, the subsequent steps of leukocyte extravasation, such as migration through the vascular BM, are not well defined. In this thesis, efforts have been made to detect, isolate and functionally characterize LN-8 in monocytes and neutrophils, and to define the role of alpha4 LNs in leukocyte migration and extravasation. First, we determined the chain specificity of 16 commonly used monoclonal antibodies (mAbs) to human LN by ELISA, Western blotting, and immunoprecipitation using recombinant (r) LNbeta1 and LNgamma1 chains. In addition, eight novel mAbs to LNalpha4 chain were generated and characterized. By immunohistochemistry, differential distribution of LNalpha4 chain in developing and adult human tissues was found. LNalpha4 was mainly localized in tissues of mesodermal origin, such as endothelial BM. By indirect immunofluorescence, LN-8 chains were detected in permeabilized monocytes and neutrophils, and intact LN-8 was isolated from these cells. This LN isoform was synthesized by monoblastoid cells and secreted by stimulated neutrophils. mAbs to LNalpha4 chain inhibited neutrophil migration through human serum albumin coated inserts, suggesting participation of the endogenous LN-8 in the cell migration. Monoblastoid JOSK-I cells adhered constitutively to rhLN-8 via alpha6beta1 and, to a lower extent, beta2 integrins, whereas stimulated neutrophils adhered to rhLN-8, rhLN-10 (alpha5beta1gamma1, Lm-511), and mouse LN-1 (alpha1beta1gamma1, Lm-111) via alphaMbeta2 integrin. rhLN-8 strongly promoted monocyte and neutrophil migration both in the absence and presence of chemoattractants, and the migration-promoting activity on neutrophils was mediated via alphaMbeta2 and, to a lower extent, 01 integrins. Compared to rhLN-8, several commercial LN preparations isolated from human placenta displayed in general lower migration-promoting activity on neutrophils. These preparations contained fragmented LN chains, a mixture of LN isoforms, and/or containing fibronectin. In LNalpha4 deficient mice, neutrophil recruitment to inflamed tissue was significantly impaired. rhLN-8 also protected neutrophils against spontaneous apoptosis. Altogether, the results from these studies indicate that both monocytes and neutrophils express LN-8, and that this laminin isoform can be secreted by the cells. In addition, LN-8 plays a major role in the physiology of myeloid cells, including their adhesion, migration, extravasation and survival. The results also indicate that alphaMbeta2 integrin may constitute a novel receptor for LN-8 and other LN isoforms.
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