The isolation and partial characterization of a sulphated glycoprotein from human whole saliva which aggregates strains of Streptococcus sanguis but not Streptococcus mutans

Hogg, S. D.; Embery, G.

doi:10.1016/0003-9969(79)90040-2

Cited by 57 publications

(34 citation statements)

References 17 publications

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“…HA beads appeared much more selective than S beads for the glycoproteins adsorbed. It has been reported that the high molecular weight salivary glycoproteins that are believed to be a major component of salivary pellicle have a hexose/protein ratio of 2 : 1 (Hogg & Embery, 1979) which is much closer to that found associated with S (Table 1).…”

Section: Discussionsupporting

confidence: 57%

Kinetics of Adherence of Actinomyces viscosus to Saliva-coated Silica and Hydroxyapatite Beads

Myerthall¹,

Thomas²

1983

Microbiology

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Adherence of 4C-labelled strains of Actinomyces viscosus to uncoated and saliva-coated silica and hydroxyapatite beads had both loose and firm components, probably reflecting different subpopulations of bacteria within a single culture. Adherence was characterized by the proportion of bacteria available for each type of adherence and a constant ( K b ) for each combination of bacterial strain and bead surface. Loose adherence, which was greater with silica than with hydroxyapatite beads, always involved many more bacteria than firm adherence. Firm adherence was greater with A . viscosus WVU627 than A . viscosus TF11. The association rate constants (K,) for loose and firm adherence were similar, indicating simultaneous processes, but the dissociation rate constant ( K d ) was lower for loose adherence than for firm adherence. Removal of loosely adhering bacteria by washing may only reflect their distance from the bead surface. Silica beads were convenient for studying bacterial adherence and formed an acceptable coating of salivary glycoprotein.

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Section: Discussionsupporting

confidence: 57%

Kinetics of Adherence of Actinomyces viscosus to Saliva-coated Silica and Hydroxyapatite Beads

Myerthall¹,

Thomas²

1983

Microbiology

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“…Although MG2 seems to bind to a wide variety of bacteria suspended in saliva (Biesbrock et al, 1991;Brack et al, 1987;Gibbons et al, 1978;Hogg et al, 1979;Levine et al, 1978;Scannapieco et al, 1987;Schenkels et al, 1993), highly purified MG2 does not bind directly to these same bacteria (Biesbrock et al, 1991). Mucins appear to lose the ability to interact with bacteria as a result of the purification process.…”

Section: Mucinsmentioning

confidence: 99%

Saliva-Bacterium Interactions in Oral Microbial Ecology

Scannapieco

1994

Critical Reviews in Oral Biology & Medicine

282

250

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Saliva is thought to have a significant impact on the colonization of microorganisms in the oral cavity. Salivary components may participate in this process by one of four general mechanisms: binding to microorganisms to facilitate their clearance from the oral cavity, serving as receptors in oral pellicles for microbial adhesion to host surfaces, inhibiting microbial growth or mediating microbial killing, and serving as microbial nutritional substrates. This article reviews information pertinent to the molecular interaction of salivary components with bacteria (primarily the oral streptococci and Actinomyces) and explores the implications of these interactions for oral bacterial colonization and dental plaque formation. Knowledge of the molecular mechanisms controlling bacterial colonization of the oral cavity may suggest methods to prevent not only dental plaque formation but also serious medical infections that may follow microbial colonization of the oral cavity.

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“…Clusterin (CLU) protein was first discovered more than thirty years ago [1], and a large volume of research has been dedicated to it since -there are more than two thousand publications in Pubmed/NCBI databases when using 'clusterin' as a keyword search criteria today. Human CLU gene (NCBI Gene ID: 1191) is located at chromosome 8p21-p12, and consists of 10 exons, in which the first two exons are alternative (designated 1 and 1') [2].…”

Section: Clu Gene Isoforms and Cellular Localizationmentioning

confidence: 99%

From Humans to Experimental Models: The Cytoprotective Role of Clusterin in the Kidney

Guan¹,

Alnasser²,

Nguan

et al. 2014

Med Surg Urol

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Clusterin (CLU) is a chaperone-like protein and has been discovered more than thirty years ago; however, its biological significance is still not fully understood. This review aims to summarize the principal observations of CLU roles related to the kidney. In humans, three or more mRNA isoforms of CLU could be expressed due to different translation start sites, but only two forms of CLU protein, secreted (sCLU, isoform 2) and nuclear (nCLU, isoform 1), have been well characterized, whereas there is only sCLU form in mice. In the biopsies of renal tissue from patients, up regulated CLU expression has been found in rejecting kidney transplants or diseased kidneys, and a lower level of serum CLU is correlated with many types of kidney disease in patients. In mice, a deficiency in CLU expression specifically leads to the phenotype of age-dependent chronic glomerular injury -moderate to severe accumulation of the mesangial matrix, becomes more susceptible to ischemia-reperfusion injury (IRI), negatively impacts renal repair after IRI and worsens renal fibrosis after ureteral obstruction. All these observations may imply the biological significance of CLU for the maintenance of the tissue homeostasis in adult kidneys. However, how CLU protects the kidney from injury or by which extracellular and intracellular pathways mediate the cyto-protection of CLU in the kidney has not been well investigated. Understanding of the cyto-protective activities of CLU in the kidney could lead to the development of novel therapeutic strategies for the prevention and/or treatment of kidney injury or diseases. CLU Gene, Isoforms and Cellular LocalizationClusterin (CLU) protein was first discovered more than thirty years ago [1], and a large volume of research has been dedicated to it since -there are more than two thousand publications in Pubmed/NCBI databases when using 'clusterin' as a keyword search criteria today. Human CLU gene (NCBI Gene ID: 1191) is located at chromosome 8p21-p12, and consists of 10 exons, in which the first two exons are alternative (designated 1 and 1') [2]. Thus, CLU gene can be transcribed into at least three mRNA variants (NCBI Reference No.: NM_001831.3; NR_038335.1; NR_045494.1) or perhaps even more [3]. The mRNA isoform 1 is a major form of CLU mRNA, whereas other forms including mRNA isoform 2 collectively count for less than 1% of total CLU mRNA [3]. Two isoforms of CLU proteins have been well characterized; nuclear isoform of CLU (nCLU, isoform 1) containing the nuclear localization signal that is translated due to the splicing at exon 1 and 3 together placing a downstream AUG at exon 3 as the first available translation and lacking of exon 2 [3,4], while pre-secreted isoform of CLU (sCLU) containing the endoplasmic reticulum (ER)-targeting signalencoding in exon 2 [3]. The nCLU is translocated into the nucleus after translation andprobably without glycosylation [3], whereas the pre-secreted sCLU is targeted to ER and Golgi bodies glycosylation and cleavage between Arg-205 and Ser-206 to produc...

show abstract

The isolation and partial characterization of a sulphated glycoprotein from human whole saliva which aggregates strains of Streptococcus sanguis but not Streptococcus mutans

Cited by 57 publications

References 17 publications

Kinetics of Adherence of Actinomyces viscosus to Saliva-coated Silica and Hydroxyapatite Beads

Kinetics of Adherence of Actinomyces viscosus to Saliva-coated Silica and Hydroxyapatite Beads

Saliva-Bacterium Interactions in Oral Microbial Ecology

From Humans to Experimental Models: The Cytoprotective Role of Clusterin in the Kidney

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