Leucine-rich repeat glycoproteins of the extracellular matrix

Hocking, Anne M.; Shinomura, Tamayuki; McQuillan, David J.

doi:10.1016/s0945-053x(98)90121-4

Cited by 414 publications

(148 citation statements)

References 114 publications

Supporting

Mentioning

146

Contrasting

Unclassified

Order By: Relevance

“…Molecules with a potential to bind TGF-b and immobilize the growth factor within the extracellular matrix are the leucine-rich repeat glycoproteins, e. g., decorin and biglycan, that are secreted by chondrocytes, fibroblasts, and other matrixproducing cell types [reviewed in ref. 21]. The possibility that TGF-b and related growth factors are sequestered within cartilage and released upon tissue damage offers an interesting hypothetical mechanism in the modulation of tissue repair activities.…”

Section: Growth Factors -Insulin-like Growth-factor-i and The Transfomentioning

confidence: 99%

Molecular aspects of pathogenesis in osteoarthritis: the role of inflammation

Hedbom¹,

Häuselmann²

2002

Cellular and Molecular Life Sciences (CMLS)

191

137

View full text Add to dashboard Cite

Arthritic diseases cause enormous burdens in terms of pain, crippling, and disability. Osteoarthritis (OA), the most common form of arthritis, is characterized by a slow progressive degeneration of articular cartilage. The exact etiology of OA is not known, but the degradation of cartilage matrix components is generally agreed to be due to an increased synthesis and activation of extracellular proteinases, mainly matrix metalloproteinases. Insufficient synthesis of new matrix macromolecules is also thought to be involved, possibly as a consequence of deficient stimulation by growth factors. Although OA is defined as a noninflammatory arthropathy, proinflammatory cytokines such as interleukin-1 have been implicated as important mediators in the disease. In response to interleukin-1, chondrocytes upregulate the production of nitric oxide and prostaglandin E2, two factors that have been shown to induce a number of the cellular changes associated with OA. The generation of these key signal molecules depends on inducible enzymes and can be suppressed by pharmacological inhibitors.

show abstract

Section: Growth Factors -Insulin-like Growth-factor-i and The Transfomentioning

confidence: 99%

Molecular aspects of pathogenesis in osteoarthritis: the role of inflammation

Hedbom¹,

Häuselmann²

2002

Cellular and Molecular Life Sciences (CMLS)

191

137

View full text Add to dashboard Cite

show abstract

“…Proteins and domains containing tandems of two or more LRRs form the continuously expanding LRR superfamily [4]. Members include intracellular, extracellular and membrane-attached proteins with such varied functions as cell adhesion and signalling [5 -7], extracellular matrix assembly [8], platelet aggregation [9], neuronal development [10,11], RNA processing [12,13], adhesion and invasion of pathogenic bacteria to host cells [14,15], disease resistance and pathogen recognition in plants [16 -18] and immune response [19 -23]. Despite their apparently unrelated functions, LRR proteins and domains share a common structural framework that makes them suitable for protein-protein interactions.…”

Section: Introductionmentioning

confidence: 99%

The leucine-rich repeat structure

Bella

Hindle

McEwan

et al. 2008

Cell. Mol. Life Sci.

407

396

View full text Add to dashboard Cite

The leucine-rich repeat is a widespread structural motif of 20-30 amino acids with a characteristic repetitive sequence pattern rich in leucines. Leucine-rich repeat domains are built from tandems of two or more repeats and form curved solenoid structures that are particularly suitable for protein-protein interactions. Thousands of protein sequences containing leucine-rich repeats have been identified by automatic annotation methods. Three-dimensional structures of leucine-rich repeat domains determined to date reveal a degree of structural variability that translates into the considerable functional versatility of this protein superfamily. As the essential structural principles become well established, the leucine-rich repeat architecture is emerging as an attractive framework for structural prediction and protein engineering. This review presents an update of the current understanding of leucine-rich repeat structure at the primary, secondary, tertiary and quaternary levels and discusses specific examples from recently determined three-dimensional structures.

show abstract

“…The protein cores of the SLRPs are defined by leucine-rich tandem repeats of about twenty-four amino acids flanked by cysteine clusters. They can interact with a variety of extracellular matrix proteins and have been implicated in the regulation of various stages of collagen fibril assembly [for review see 4, 6]. The ability of the protein core to interact with triple helical molecules may at least in part be due to their horseshoe-like tertiary structure, as being suggested from molecular modeling [7]and rotary shadowing data [8, 9].…”

Section: Introductionmentioning

confidence: 99%

Decorin Deficiency Leads to Impaired Angiogenesis in Injured Mouse Cornea

Schönherr

Sunderkötter

Schaefer³

et al. 2004

J Vasc Res

101

View full text Add to dashboard Cite

Small leucine-rich proteoglycans play important roles in the organization of the extracellular matrix as well as for the regulation of cell behavior; two biological processes that are essential for angiogenesis. We investigated consequences of the targeted ablation of decorin (DCN), biglycan (BGN) and fibromodulin (FMOD) genes on inflammation-induced angiogenesis in the cornea. In wild-type mice, DCN was localized exclusively to the corneal stroma, while FMOD and BGN were more prominently expressed in epithelial cells. Endothelial cells from limbus blood vessels expressed BGN and FMOD, but no DCN. However, after induction of angiogenesis by chemical cauterization, DCN was expressed in the newly formed capillaries, together with BGN and FMOD. Notably, in DCN-deficient mice, the growth of vessels was significantly diminished, whereas it did not significantly change in FMOD- or BGN-deficient animals. Moreover, blood vessels of DCN-deficient mice exhibited a similar expression level of BGN as control mice, while FMOD was increased on day 3 after injury. These results indicate that DCN, in addition to its effects on fibrillogenesis, plays a regulatory role in angiogenesis and that FMOD in endothelial cells may be able to partially substitute for DCN.

show abstract

Leucine-rich repeat glycoproteins of the extracellular matrix

Cited by 414 publications

References 114 publications

Molecular aspects of pathogenesis in osteoarthritis: the role of inflammation

Molecular aspects of pathogenesis in osteoarthritis: the role of inflammation

The leucine-rich repeat structure

Decorin Deficiency Leads to Impaired Angiogenesis in Injured Mouse Cornea

Contact Info

Product

Resources

About