The family of bacterial ADP-ribosylating exotoxins

Krueger, Kathleen M.; Barbieri, Joseph T.

doi:10.1128/cmr.8.1.34

Cited by 150 publications

(106 citation statements)

References 151 publications

Supporting

Mentioning

103

Contrasting

Order By: Relevance

“…PTX can exert its effect on G proteins on membrane receptors or can be transported into intracellular sites (50,51). Inhibitory G proteins have been localized in the trans-Golgi network (52)(53)(54) and in secretory granules (11,43,44,46,55,56).…”

Section: Discussionmentioning

confidence: 99%

Participation of G Proteins in Natriuretic Peptide Hormone Secretion from Heart Atria

Bensimon¹,

Chang²,

Bold³

et al. 2004

Endocrinology

View full text Add to dashboard Cite

The involvement of G proteins in the mechanism underlying the increased atrial natriuretic factor (ANF) secretion observed after atrial muscle stretch (stretch-secretion coupling) was assessed using a combined pharmacological, immunocytochemical, and tissue fractionation approach. It was found that G(i/o) inhibition by pertussis toxin (PTX) abolished stretch-secretion coupling without affecting baseline secretion through a mechanism that is independent of G(q) signaling agonists. Mastoparan-7, a G(i/o) agonist, significantly increased ANF secretion even in the absence of muscle stretch through a PTX-sensitive mechanism. By confocal and electron immunocytochemistry, ANF and G(o) partially colocalized, whereas ultracentrifugation analysis suggested the presence of two populations of granules, one of which was partially associated with G(o), as demonstrated by Western blotting. PTX did not affect basal or endothelin-1-stimulated ANF secretion, in line with the view that endothelin-1 signals mainly through G(q). It is concluded there are at least two types of regulated secretory processes in atrial cardiocytes: one is acutely responsive to muscle stretch and is PTX sensitive, and the other is G(q)mediated and PTX insensitive and may be responsible for changes in secretion after chronic changes in the neuroendocrine environment.

show abstract

Section: Discussionmentioning

confidence: 99%

Participation of G Proteins in Natriuretic Peptide Hormone Secretion from Heart Atria

Bensimon¹,

Chang²,

Bold³

et al. 2004

Endocrinology

View full text Add to dashboard Cite

show abstract

“…Various pathogenic bacteria secrete toxins that ADP-rybosylate human proteins, thus causing severe diseases, such as cholera, diphtheria, pertussis, and botulism [108-111]. …”

Section: Mono- and Poly(adp-ribosyl)ationmentioning

confidence: 99%

Chemical and Functional Aspects of Posttranslational Modification of Proteins

2009

View full text Add to dashboard Cite

This paper reviews the chemical and functional aspects of the posttranslational modifications of proteins, which are achieved by the addition of various groups to the side chain of the amino acid residue backbone of proteins. It describes the main prosthetic groups and the interaction of these groups and the apoenzyme in the process of catalysis, using pyridoxal catalysis as an example. Much attention is paid to the role of posttranslational modification of proteins in the regulation of biochemical processes in live organisms, and especially to the role of protein kinases and their respective phosphotases. Methylation and acetylation reactions and their role in the "histone code", which regulates genome expression on the transcription level, are also reviewed. This paper also describes the modification of proteins by large hydrophobic residues and their role in the function of membrane-associated proteins. Much attention is paid to the glycosylation of proteins, which leads to the formation of glycoproteins. We also describe the main non-enzymatic protein modifications such as glycation, homocysteination, and desamida-tion of amide residues in dibasic acids.

show abstract

“…This mechanism is used by several bacterial toxins, such as diphtheria and cholera, to alter the metabolism of their hosts. 5 However, one of the best characterized systems of ADP-ribosylation is the regulation of the NifH component of nitrogenase, which occurs in Proteobacteria such as Rhodospirillum rubrum and Azospirillum brasilense. 6 Nitrogenase activity in these bacteria is reversibly down-regulated in the presence of ammonium or upon energy depletion.…”

Section: Introductionmentioning

confidence: 99%