Svein Kolset

Dr. Svein Kolset

orcid

Research Focus & Metrics

Academic Career Length

26Years (2001-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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27 October 2012 in Journal of Histochemistry & Cytochemistry
Verified
Journal Article
Open access
SKSvein Kolset
Svein Kolset
FRF. P. Reinholt
F. P. Reinholt
TJT. Jenssen
T. Jenssen
Diabetic nephropathy (DN) is a serious complication in diabetes. Major typical morphological changes are the result of changes in the extracellular matrix (ECM). Thus, basement membranes are thickened and the glomerular mesangial matrix and the tubulointerstitial space are expanded, due to increased amounts of ECM. One important ECM component, the proteoglycans (PGs), shows a more complex pattern of changes in DN. PGs in basement membranes are decreased but increased in the mesangium and the tubulointerstitial space. The amounts and structures of heparan sulfate chains are changed, and such changes affect levels of growth factors regulating cell proliferation and ECM synthesis, with cell attachment affecting endothelial cells and podocytes. Enzymes modulating heparan sulfate structures, such as heparanase and sulfatases, are implicated in DN. Other enzyme classes also modulate ECM proteins and PGs, such as matrix metalloproteinases (MMPs) and serine proteases, such as plasminogen activator, as well as their corresponding inhibitors. The levels of these enzymes and inhibitors are changed in plasma and in the kidneys in DN. Several growth factors, signaling pathways, and hyperglycemia per se affect ECM synthesis and turnover in DN. Whether ECM components can be used as markers for early kidney changes is an important research topic, whereas at present, the clinical use remains to be established.

8 December 2007 in Cellular and Molecular Life Sciences
Verified
Journal Article
Closed access
PDF file
SKSvein Kolset
Svein Kolset
HTH. Tveit
H. Tveit

15 November 2011 in The Journal of Immunology
Verified
Journal Article
Open access
PDF file
SKSvein Kolset
Svein Kolset
GPGunnar Pejler
Gunnar Pejler
Among the different proteoglycans expressed by mammals, serglycin is in most immune cells the dominating species. A unique property of serglycin is its ability to adopt highly divergent structures, because of glycosylation with variable types of glycosaminoglycans when expressed by different cell types. Recent studies of serglycin-deficient animals have revealed crucial functions for serglycin in a diverse array of immunological processes. However, its exact function varies to a large extent depending on the cellular context of serglycin expression. Based on these findings, serglycin is emerging as a structural and functional chameleon, with radically different properties depending on its exact cellular and immunological context.

9 January 2015 in Journal of Histochemistry & Cytochemistry
Verified
Journal Article
Open access
TVTram Thu Vuong
Tram Thu Vuong
TRTrine M. Reine
Trine M. Reine
ASAmanda Sudworth
Amanda Sudworth
TJTrond G. Jenssen
Trond G. Jenssen
SKSvein Kolset
Svein Kolset
Syndecans are important cell surface proteoglycans with many functions; yet, they have not been studied to a very large extent in primary human endothelial cells. The purpose of this study was to investigate syndecan-4 expression in cultured human umbilical vein endothelial cells (HUVECs) and assess its role in inflammatory reactions and experimental wound healing. qRT-PCR analysis revealed that syndecan-3 and syndecan-4 were highly expressed in HUVECs, whereas the expression of syndecan-1 and -2 was low. HUVECs were cultured with the inflammatory mediators lipopolysaccharide (LPS) and interleukin 1β (IL-1β). As a result, syndecan-4 expression showed a rapid and strong increase. Syndecan-1 and -2 expressions decreased, whereas syndecan-3 was unaffected. Knockdown of syndecan-4 using siRNA resulted in changes in cellular morphology and focal adhesion sites, delayed wound healing and tube formation, and increased secretion of the pro-inflammatory and angiogenic chemokine, CXCL8. These data suggest functions for syndecan-4 in inflammatory reactions, wound healing and angiogenesis in primary human endothelial cells.

1 June 2020 in The Lancet Child & Adolescent Health
Verified
Journal Article
Closed access
MNMarianne Nordstrøm
Marianne Nordstrøm
KRKjetil Retterstøl
Kjetil Retterstøl
SHSigrun Hope
Sigrun Hope
SKSvein Kolset
Svein Kolset

1 May 2015 in Matrix Biology
Verified
Journal Article
Open access
MPMona E. Pedersen
Mona E. Pedersen
TVTram T. Vuong
Tram T. Vuong
SRSissel Beate Rønning
Sissel Beate Rønning
SKSvein Kolset
Svein Kolset
Matrix metalloproteinases have important functions for tissue turnover in fish, with relevance both for the fish industry and molecular and cellular research on embryology, inflammation and tissue repair. These metalloproteinases have been studied in different fish types, subjected to both aquaculture and experimental conditions. This review highlights studies on these metalloproteinases in relation to both fish quality and health and further, the future importance of fish for basic research studies.