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Šedo, Aleksi; Duke‐Cohan, Jonathan S.; Balážiová, Eva; Šedová, Liliana

doi:10.1186/ar1852

Cited by 62 publications

(23 citation statements)

References 106 publications

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“…31 However, some of these inhibitors showed anti-arthritic effects in DPP IV deficient animals, suggesting the potential importance of DPP IVlike enzymes in the pathogenesis. 32 Our results confirm the previously proposed theory that other proteins which posses DPP IV-like activity are active in serum and could be involved in the development of rheumatoid diseases.…”

Section: Discussionsupporting

confidence: 81%

Is Dipeptidyl Peptidase IV (DPP IV) Associated with Inflammation Present in Human Spondyloarthritides and Rheumatoid Arthritis?

Detel¹,

Kehler²,

Buljević³

et al. 2012

Croat. Chem. Acta

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Abstract. Dipeptidyl peptidase IV (DPP IV) is a serine peptidase which has been suggested to play a role in the pathogenesis of rheumatoid arthritis, but its mediator actions have not been well investigated in patients with spondyloarthritides. The purpose of this study was to investigate clinical relevance of changes in serum DPP IV activity and concentration in these diseases. Serum DPP IV activity was significantly decreased in patients with spondyloarthritides and rheumatoid arthritis compared to the control group, while DPP IV concentration was increased. Among spondyloarthritides patients, DPP IV concentration was decreased in patients with reactive arthritis. No difference was observed in DPP IV activity or concentration between spondyloarthritides and rheumatoid arthritis, as well as between patients with clinically active disease and those in remission. Our results suggest that DPP IV could not be used as a specific serum marker, but could be potentially used as a non-specific inflammatory marker. (doi: 10.5562/cca1863)

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Section: Discussionsupporting

confidence: 81%

Is Dipeptidyl Peptidase IV (DPP IV) Associated with Inflammation Present in Human Spondyloarthritides and Rheumatoid Arthritis?

Detel¹,

Kehler²,

Buljević³

et al. 2012

Croat. Chem. Acta

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“…Of these, we particularly focused on the serine exopeptidases dipeptidyl-peptidase V (DPPIV, also called CD26)222324 and transmembrane protease, serine 2 (TMPRSS2)25, which are apical membrane-bound serine proteases, highly expressing at the brush border of proximal tubular epithelial cells. We first tested whether DPPIV and/or TMPRSS2 cleave AIM.…”

Section: Resultsmentioning

confidence: 99%

A proteolytic modification of AIM promotes its renal excretion

Yamazaki

Sugisawa

Hiramoto

et al. 2016

Sci Rep

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Apoptosis inhibitor of macrophage (AIM, encoded by cd5l) is a multi-functional circulating protein that has a beneficial role in the regulation of a broad range of diseases, some of which are ameliorated by AIM administration in mice. In blood, AIM is stabilized by association with IgM pentamers and maintains its high circulating levels. The mechanism regulating the excessive accumulation of blood AIM remains unknown, although it is important, since a constitutive increase in AIM levels promotes chronic inflammation. Here we found a physiological AIM-cleavage process that induces destabilization of AIM and its excretion in urine. In blood, IgM-free AIM appeared to be cleaved and reduced in size approximately 10 kDa. Cleaved AIM was unable to bind to IgM and was selectively filtered by the glomerulus, thereby excreted in urine. Amino acid substitution at the cleavage site resulted in no renal excretion of AIM. Interestingly, cleaved AIM retained a comparable potency with full-length AIM in facilitating the clearance of dead cell debris in injured kidney, which is a key response in the recovery of acute kidney injury. Identification of AIM-cleavage and resulting functional modification could be the basis for designing safe and efficient AIM therapy for various diseases.

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“…DPPIV is a plasma membrane anchored ecto-protease also known as the leukocyte antigen CD26; it is expressed in a variety of epithelial and non-epithelial cells [16]. The kidney is a main site of expression of DPPIV, where it constitutes up to 14% of total membrane protein [17]. It is a highly specific serine protease with catalytic activity, but it can also function as a binding protein [18,19].…”

Section: Effect Of Serine Proteases On Na+ Transporting Proteins Of Tmentioning

confidence: 99%

Potential Role of Serine Proteases in Modulating Renal Sodium Transport in vivo

Jacquillet

Rubera²,

Unwin³

2011

Nephron Physiol

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The maintenance of sodium (Na⁺) homeostasis is an essential function of the kidney. It is achieved by a variety of transport processes localized all along the highly specialised segments of the nephron. Impairment of these transport mechanisms, and thereby Na⁺ handling, is associated with disturbed Na⁺ and water balance, leading to hypertension and oedema. This review focuses on the novel regulation of sodium reabsorption by serine proteases acting along the entire nephron.

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Untitled

Cited by 62 publications

References 106 publications

Is Dipeptidyl Peptidase IV (DPP IV) Associated with Inflammation Present in Human Spondyloarthritides and Rheumatoid Arthritis?

Is Dipeptidyl Peptidase IV (DPP IV) Associated with Inflammation Present in Human Spondyloarthritides and Rheumatoid Arthritis?

A proteolytic modification of AIM promotes its renal excretion

Potential Role of Serine Proteases in Modulating Renal Sodium Transport in vivo

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