Dipeptidyl Peptidase IV – Activity and Subcellular Localisation in Lymphocytes from Control Subjects, Immunodeficient Patients and Cord Blood

Harland, C.C.; Shah, T.; Webster, A. D.

doi:10.1042/cs073029p

Cited by 2 publications

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“…However, we have found that OX-61 binds to 95% to 98% of resting rat thymocytes (McCaughan GW, Unpublished observations). There is evidence that the blockage of DPP-IV activity, either by natural inhibitors or antibodies, leads to an inhibition of lymphocyte proliferation (51).…”

Section: As Seen Inmentioning

confidence: 99%

Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: An analysis by tissue distribution, purification andN-terminal amino acid sequence

et al. 1990

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This paper describes the tissue distribution, purification and N-terminal amino acid sequence of the bile canalicular cell surface molecule dipeptidyl peptidase IV. Immunoperoxidase staining of cryostat sections of rat liver with a monoclonal antibody, Medical Research Council OX-61, indicated specific binding to hepatocyte bile canalicular domains and brush borders of bile ducts. Additional staining was seen in other epithelial brush borders (small intestine, kidney, colon, pancreatic duct); acinar structures in salivary glands; endothelial structures and T cell areas in thymus, spleen and lymph node. The tissue distribution suggested that monoclonal antibody OX-61 binds to the ectoenzyme dipeptidyl peptidase IV. This was confirmed by depletion of dipeptidyl peptidase IV activity from tissue homogenates by monoclonal antibody OX-61 coupled to Sepharose. The molecule recognized by OX-61 was then purified from liver and kidney by monoclonal antibody affinity chromatography. The molecule had a molecular weight of 110 kD under reducing conditions. The purified molecule was subsequently analyzed for amino acid composition and N-terminal amino acid sequence. Thirty-one N-terminal amino acids were sequenced and indicated identity with part of the predicted N-terminus of the previously cloned bile canalicular molecule GP110. On review, other similarities between dipeptidyl peptidase IV and GP110 were detected: molecular weight, deglycosylated form and metabolic half-life. Finally, the recent cloning of dipeptidyl peptidase IV permitted a comparison between the molecule recognized by monoclonal antibody OX-61, GP110 and dipeptidyl peptidase IV. It is concluded that these three molecules are almost certainly identical.

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Section: As Seen Inmentioning

confidence: 99%

Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: An analysis by tissue distribution, purification andN-terminal amino acid sequence

et al. 1990

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“…While specific proteolytic processing of DP proteins has not been reported, non-specific DP8/9 degradation in mammalian cell extracts demonstrate protease affinity for DP8 and DP9 (M.R. Pitman, unpublished results) DPIV is highly glycosylated (79) and traffics to the extracellular plasma membrane (80). Although no splice variants have been reported for the DPIV gene, a soluble DPIV form exists; thought to occur through proteolytic cleavage of the membrane-bound form into the circulation (81).…”

Section: Post-translational Modifications Of Dp Proteinsmentioning

confidence: 99%

Dipeptidyl peptidase 8 and 9 - guilty by association?

Pitman

Sulda²,

Kuss³

et al. 2009

Front Biosci

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Dipeptidyl peptidases (DP) 8 and 9 are members of the DPIV enzyme family. Other members include DPIV, fibroblast activation protein (FAP) and the non-enzymes DP6 and DP10. DPIV family members have diverse biological roles, and have been implicated in a range of diseases including diabetes, cancer, inflammatory bowel disease, multiple sclerosis (MS), arthritis and asthma. While DP8/9 biological functions are yet to be established, they have been predicted to have similar roles to the other DPs due to high sequence similarities within the active site of the enzymes. While there is mounting evidence towards the involvement of DP8 and/or DP9 in innate and acquired immunity, direct proof for the link between DP8 and DP9 and human disease is yet to be definitively shown, thus DP8 and 9 proteins remain guilty by association.

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Dipeptidyl Peptidase IV – Activity and Subcellular Localisation in Lymphocytes from Control Subjects, Immunodeficient Patients and Cord Blood

Cited by 2 publications

References 0 publications

Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: An analysis by tissue distribution, purification andN-terminal amino acid sequence

Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: An analysis by tissue distribution, purification andN-terminal amino acid sequence

Dipeptidyl peptidase 8 and 9 - guilty by association?

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