کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8633896 | 1569063 | 2016 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of Substance P processing in mouse spinal cord S9 fractions using high-resolution Quadrupole-Orbitrap mass spectrometry
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کلمات کلیدی
HRAMXICTAC1ESICPEPC1/3PC2PAMIDMSTachykininPrEPTFATICNK1FWHMMS/MS - MS / MSTrifluoroacetic acid - اسید TrifluoroaceticPain - دردCNS - دستگاه عصبی مرکزیcentral nervous system - سیستم عصبی مرکزیMass spectrometry - طیف سنجی جرمیIsotope dilution mass spectrometry - طیف سنجی جرمی رقیق ایزوتوپTandem mass spectrometry - طیف سنجی جرمی پشت سر هم یا متوالیfull width at half maximum - عرض کامل در نیمی از حداکثرSubstance P - ماده PProteolysis - پروتئولیزhigh performance liquid chromatography - کروماتوگرافی مایع با کارایی بالاHPLC - کروماتوگرافی مایعی کاراextracted ion chromatogram - کروماتوگرافی یون استخراج شدهtotal ion chromatogram - کروماتوگرافی یونی کلNeurokinin 1 receptor - گیرنده neurokinin 1
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
علوم غدد
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Characterization of Substance P processing in mouse spinal cord S9 fractions using high-resolution Quadrupole-Orbitrap mass spectrometry Characterization of Substance P processing in mouse spinal cord S9 fractions using high-resolution Quadrupole-Orbitrap mass spectrometry](/preview/png/8633896.png)
چکیده انگلیسی
Tachykinins are a family of pronociceptive neuropeptides with a specific role in pain and inflammation. Several mechanisms regulate endogenous tachykinins and Substance P (SP) levels, including the differential expression of protachykinin mRNA and the controlled secretion of tachykinins from neurons. Proteolysis is suspected to regulate extracellular SP concentrations but few studies were conducted on the metabolism of proneuropeptides and neuropeptides. Here, we provide evidence that proteolysis controls SP levels in the spinal cord leading to the formation of active C-terminal fragments. Using high-resolution mass spectrometry, specific tachykinins fragments were characterized and quantified. The metabolic stability of β-Tachykinin58-71 and SP were very short resulting in half-life of 5.7 and 3.5 min respectively. Several C-terminal fragments were identified, including SP3-11, SP5-11 and SP8-11, which conserve affinity for the Neurokinin 1 receptor. Interestingly, the metabolic stability of C-terminal fragments was significantly superior. Two specific Prolyl endopeptidase inhibitors were used and showed a significant reduction in the rate of formation of SP3-11 and SP5-11 providing strong evidence that Prolyl endopeptidase is involved into N-terminal processing of SP in the spinal cord.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuropeptides - Volume 59, October 2016, Pages 47-55
Journal: Neuropeptides - Volume 59, October 2016, Pages 47-55
نویسندگان
Mouna Saidi, Soufiane Kamali, Francis Beaudry,