Hyaluronan-binding Proteins: Tying Up the Giant

Day, Anthony J.; Prestwich, Glenn D.

doi:10.1074/jbc.r100036200

Cited by 520 publications

(449 citation statements)

References 62 publications

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“…Most of the proteins that bind to HA at the cell surface or within the ECM, do so through a common domain, the so-called link domain or link module (33). This module is defined by two disulfide bonds and is composed of two ␣-helices and two antiparallel ␤-sheets arranged around a large hydrophobic core, similar in structure to the C-type lectin domain, a Ca 2ϩ -dependent carbohydrate-binding domain (33,34).…”

Section: Discussionmentioning

confidence: 99%

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A Hyaluronan Binding Link Protein Gene Family Whose Members Are Physically Linked Adjacent to Chrondroitin Sulfate Proteoglycan Core Protein Genes

Spicer

Joo

Bowling

2003

Journal of Biological Chemistry

182

154

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We describe a vertebrate hyaluronan and proteoglycan binding link protein gene family (HAPLN), consisting of four members including cartilage link protein. The encoded proteins share 45-52% overall amino acid identity. In contrast to the average sequence identity between family members, the sequence conservation between vertebrate species was very high. Human and mouse link proteins share 81-96% amino acid sequence identity. Two of the four link protein genes (HAPLN2 and HAPLN4) were restricted in expression to the brain/central nervous system, while one of the four genes (HAPLN3) was widely expressed. Genomic structures revealed that all four HAPLN genes were similar in exon-intron organization and were also similar in genomic organization to the 5 exons for the CSPG core protein genes. Strikingly, all four HAPLN genes were located immediately adjacent to the four CSPG core protein genes creating four pairs of CSPG-HAPLN genes within the mammalian genome. Furthermore, the two brain-specific HAPLN genes (HAPLN2 and HAPLN4) were physically linked to the brain-specific CSPG genes encoding brevican and neurocan, respectively. The tight physical association of the HAPLN and CSPG genes supports a hypothesis that the first HAPLN gene arose as a partial gene duplication event from an ancestral CSPG gene. There is some degree of coordinated expression of each gene pair. Collectively, the four HAPLN genes are expressed by most tissue types, reflecting the fundamental importance of the hyaluronan-dependent extracellular matrix to tissue architecture and function in vertebrate species. Comparison of the genomic structures for the HAPLN, CSPG genes and other members of the link module superfamily provide strong support for a common evolutionary origin from an ancestral gene containing one link module encoding exon.

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Section: Discussionmentioning

confidence: 99%

“…This module is defined by two disulfide bonds and is composed of two ␣-helices and two antiparallel ␤-sheets arranged around a large hydrophobic core, similar in structure to the C-type lectin domain, a Ca 2ϩ -dependent carbohydrate-binding domain (33,34). The link module containing proteins constitute the link module superfamily (33).…”

Section: Discussionmentioning

confidence: 99%

A Hyaluronan Binding Link Protein Gene Family Whose Members Are Physically Linked Adjacent to Chrondroitin Sulfate Proteoglycan Core Protein Genes

Spicer

Joo

Bowling

2003

Journal of Biological Chemistry

182

154

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“…CD 44 can exist in numerous isoforms. HA binding properties of CD44 are determined by the isoform and the cell type on which it is expressed [16]. HA participates in tissue repair and wound healing and is used topically as anti inflammatory and anti-oedematous agent [17].…”

Section: Inrtoductionmentioning

confidence: 99%

Hyaluronic Acid as an Adjunct to Scaling and Root Planing in Chronic Periodontitis. A Randomized Clinical Trail

Padma

Baramappa

Rao

et al. 2014

JCDR

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Aim: Aim of the present study was to evaluate the adjunctive effect of local application of hyaluronon gel following scaling and root planing (SRP) in chronic periodontitis patients. Materials and Methods:In this randomized split mouth study 33 subjects with chronic periodontitis were evaluated after full mouth SRP. In the test sites hyaluronon gel was applied immediately after SRP and one week post therapy, the control sites were treated with SRP alone. Bleeding on probing (BOP), probing pocket depth (PPD), and clinical attachment level (CAL) were recorded at baseline, 4 wk and 12 wk.Results: Significant reduction in BOP scores was observed in both the groups at 12weeks (p<0.001). The hyaluronon group

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“…Chondroitin, and later HA, arose to extend the repertoire of the extracellular matrix of higher animals. GAG polymers interact in a selective fashion with a wide variety of proteins and factors (reviewed in Day and Prestwich, 2002;Capila and Linhardt, 2002). These binding events yield intracellular adhesion and/or communication systems during development, growth, and adult life.…”

Section: Discussionmentioning

confidence: 99%

Evolution of glycosaminoglycans and their glycosyltransferases: Implications for the extracellular matrices of animals and the capsules of pathogenic bacteria

DeAngelis

2002

Anat. Rec.

101

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Glycosaminoglycans (linear polysaccharides with a repeating disaccharide backbone containing an amino sugar) are essential components of extracellular matrices of animals. These complex molecules play important structural, adhesion, and signaling roles in mammals. Direct detection of glycosaminoglycans has been reported in a variety of organisms, but perhaps more definitive tests for the glycosyltransferase genes should be utilized to clarify the distribution of glycosaminoglycans in metazoans. Recently, glycosyltransferases that form the hyaluronan, heparin/heparan, or chondroitin backbone were identified at the molecular level. The three types of glycosyltransferases appear to have evolved independently based on sequence comparisons and other characteristics. All metazoans appear to possess heparin/heparan. Chondroitin is found in some worms, arthropods, and higher animals. Hyaluronan is found only in two of the three main branches of chordates. The presence of several types of glycosaminoglycans in the body allows multiple communication channels and adhesion systems to operate simultaneously. Certain pathogenic bacteria produce extracellular coatings, called capsules, which are composed of glycosaminoglycans that increase their virulence during infection. The capsule helps shield the microbe from the host defenses and/or modulates host physiology. The bacterial and animal polysaccharides are chemically identical or at least very similar. Therefore, no immune response is generated, in contrast to the vast majority of capsular polymers from other bacteria. In microbial systems, it appears that in most cases functional convergent evolution of glycosaminoglycan glycosyltransferases occurred, rather than direct horizontal gene transfer from their vertebrate hosts. Anat Rec 268: 317-326, 2002.

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Hyaluronan-binding Proteins: Tying Up the Giant

Cited by 520 publications

References 62 publications

A Hyaluronan Binding Link Protein Gene Family Whose Members Are Physically Linked Adjacent to Chrondroitin Sulfate Proteoglycan Core Protein Genes

A Hyaluronan Binding Link Protein Gene Family Whose Members Are Physically Linked Adjacent to Chrondroitin Sulfate Proteoglycan Core Protein Genes

Hyaluronic Acid as an Adjunct to Scaling and Root Planing in Chronic Periodontitis. A Randomized Clinical Trail

Evolution of glycosaminoglycans and their glycosyltransferases: Implications for the extracellular matrices of animals and the capsules of pathogenic bacteria

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