α-Glucosidase Inhibitor Proteins from <i>Sesbania grandiflora</i> Flowers

Boonmee, Apaporn; Reynolds, C. D.; Sangvanich, Polkit

doi:10.1055/s-2007-981599

Cited by 17 publications

(14 citation statements)

References 7 publications

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“…(44) On the other hand, DING proteins are not restricted to terrestrial plants since one has been purified from Chlamydomonas. It is a protein phosphatase purified from thylakoids, (45) recalling the DING-related bacterial phosphatase.…”

Section: More Ding Proteinsmentioning

confidence: 99%

The DING family of proteins: ubiquitous in eukaryotes, but where are the genes?

et al. 2009

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PstS and DING proteins are members of a superfamily of secreted, high-affinity phosphate-binding proteins. Whereas microbial PstS have a well-defined role in phosphate ABC transporters, the physiological function of DING proteins, named after their DINGGG N termini, still needs to be determined. PstS and DING proteins co-exist in some Pseudomonas strains, to which they confer a highly adhesive and virulent phenotype. More than 30 DING proteins have now been purified, mostly from eukaryotes. They are often associated with infections or with dysregulation of cell proliferation. Consequently, eukaryotic DING proteins could also be involved in cell-cell communication or adherence. The ubiquitous presence in eukaryotes of proteins structurally and functionally related to bacterial virulence factors is intriguing, as is the absence of eukaryotic genes encoding DING proteins in databases. DING proteins in eukaryotes could originate from unidentified commensal or symbiotic bacteria and could contribute to essential functions. Alternatively, DING proteins could be encoded by eukaryotic genes sharing special features that prevent their cloning. Both hypotheses are discussed.

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Section: More Ding Proteinsmentioning

confidence: 99%

The DING family of proteins: ubiquitous in eukaryotes, but where are the genes?

et al. 2009

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“…Anyway, it could be approximately deduced that the fraction F50 had a 16.1-fold and 8.9-fold greater inhibitory activity than cuminaldehyde and acarbose, respectively. Furthermore, the crude protein preparation from Z. ottensii reported here revealed a 97.5% maximum inhibition activity compared with the 82.07% reported for the crude protein (after 90% saturated (NH 4 ) 2 SO 4 salting-out) from the flower extract of Sesbania grandiflora [30]. Moreover, after Superdex G200 and DEAE cellulose purification of the α-glucosidase inhibitory activity of reduced the maximal observed inhibition level to 74.0%, which concurs with our result here that after SP sepharose purification the F50 fraction revealed a 77.5% maximum α-glucosidase inhibitory activity compared with ∼97% in the crude Z. ottensii rhizome extract.…”

Section: Resultsmentioning

confidence: 43%

A Novel α-Glucosidase Inhibitor Protein from the Rhizomes of Zingiber ottensii Valeton

Tiengburanatam

Boonmee

Sangvanich

et al. 2010

Appl Biochem Biotechnol

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The objective of this study was to investigate a new protein with α-glucosidase inhibitory activity from the rhizomes of Zingiber ottensii. With a simple salting-out technique followed by single-step anion-exchange purification, the protein was successfully purified from the rhizomes. This protein was found to have three likely sub-unit types, 32.5, 15.2, and 13.8 kDa, as revealed by native and reducing SDS-PAGE analysis. Determination of the kinetics of the inhibition of α-glucosidase from Saccharomyces cerevisiae by standard enzymatic methods indicated the maximum percent inhibition; IC(50) and K ( i ) of this protein were 77.5%, 30.15 μg/ml, and 140 μmol, while the K ( m ) and V ( max ) were 2.35 μmol and 0.11 mM/min, respectively. The inhibitory action was pH-independent within the pH range 2-10, but was potentially affected by buffer salts, and was relatively temperature-stable between 4-35 °C, with a maximum activity at 65 °C. The amino acid sequence of an internal fragment of this purified Z. ottensii rhizomal protein had a similarity to the sequence from the plant cysteine proteinase family. Although this α-glucosidase inhibitory protein was purified from Z. ottensii rhizomes and preliminarily characterized, further studies are needed prior to firm applications being envisaged.

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“…Another possible mechanism of action may relate to the ability of DING proteins to act as a-glucosidase inhibitors [75], which can act as anti-HIV agents due to their ability to prevent viral fusion [81].…”

Section: Ding Protein From St John's Wort and Hiv Replicationmentioning

confidence: 99%

For whom the bell tolls? DING proteins in health and disease

Berna

Bernier

Chabrière

et al. 2009

Cell. Mol. Life Sci.

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DING proteins, identified mainly by their eponymous N-terminal sequences, are ubiquitous in living organisms. Amongst bacteria, they are common in pseudomonads, and have been characterised with respect to genetics and structure. They form part of a wider family of phosphate-binding proteins, with emerging roles in phosphate acquisition and pathogenicity. Many DING proteins have been isolated in eukaryotes, in which they have been associated with very diverse biological activities, often in the context of possible signalling roles. Disease states in which DING proteins have been implicated include rheumatoid arthritis, lithiasis, atherosclerosis, some tumours and tumour-associated cachexia, and bacterial and viral adherence. Complete genetic and structural characterisation of eukaryotic DING genes and proteins is still lacking, though the phosphate-binding site seems to be conserved. Whether as bacterial proteins related to bacterial pathogenicity, or as eukaryotic components of biochemical signalling systems, DING proteins require further study.

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α-Glucosidase Inhibitor Proteins from Sesbania grandiflora Flowers

Cited by 17 publications

References 7 publications

The DING family of proteins: ubiquitous in eukaryotes, but where are the genes?

The DING family of proteins: ubiquitous in eukaryotes, but where are the genes?

A Novel α-Glucosidase Inhibitor Protein from the Rhizomes of Zingiber ottensii Valeton

For whom the bell tolls? DING proteins in health and disease

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