Literature DB >> 10428492

Evidence for tissue-specific forms of glutaminyl cyclase.

P A Sykes1, S J Watson, J S Temple, R C Bateman.   

Abstract

Glutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides. An examination of the bovine tissue distribution of QC immunoreactivity, enzyme activity, and mRNA confirmed that QC was abundant in brain and pituitary by all three measures. However, enzymatic activity was considerably more widespread than either immunoreactivity or mRNA, suggesting multiple enzyme forms. Partially purified QC from bovine spleen differed significantly from the known bovine pituitary QC in physical and catalytic properties. We propose that this form of glutaminyl cyclase plays a role in the posttranslational processing of constitutively secreted pGlu-containing proteins.

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Year:  1999        PMID: 10428492     DOI: 10.1016/s0014-5793(99)00872-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  11 in total

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4.  Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.

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5.  Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex.

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8.  Abundant pyroglutamate-modified ABri and ADan peptides in extracellular and vascular amyloid deposits in familial British and Danish dementias.

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9.  Oxidative stress and mitochondria-mediated cell death mechanisms triggered by the familial Danish dementia ADan amyloid.

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Authors:  John Stuart Gillis
Journal:  J Transl Med       Date:  2006-07-04       Impact factor: 5.531

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