دورية أكاديمية
أعرض في EDS

Fast and slow skeletal myosin binding protein-C and aging.

التفاصيل البيبلوغرافية
العنوان: Fast and slow skeletal myosin binding protein-C and aging.
المؤلفون: Perazza LR; Department of Physical Therapy, College of Health & Rehabilitation Sciences: Sargent College, Boston University, 635 Commonwealth Ave, Boston, MA, 02215, USA., Wei G; Department of Physical Therapy, College of Health & Rehabilitation Sciences: Sargent College, Boston University, 635 Commonwealth Ave, Boston, MA, 02215, USA., Thompson LV; Department of Physical Therapy, College of Health & Rehabilitation Sciences: Sargent College, Boston University, 635 Commonwealth Ave, Boston, MA, 02215, USA. lvthomp@bu.edu.
المصدر: GeroScience [Geroscience] 2023 Apr; Vol. 45 (2), pp. 915-929. Date of Electronic Publication: 2022 Nov 21.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Springer International Publishing Country of Publication: Switzerland NLM ID: 101686284 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2509-2723 (Electronic) Linking ISSN: 25092723 NLM ISO Abbreviation: Geroscience Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cham : Springer International Publishing, [2017]-
مواضيع طبية MeSH: Myocardium*/pathology , Muscle, Skeletal*/metabolism, Mice ; Animals ; Myosins/metabolism ; Aging
مستخلص: Aging is associated with skeletal muscle strength decline and cardiac diastolic dysfunction. The structural arrangements of the sarcomeric proteins, such as myosin binding protein-C (MyBP-C) are shown to be pivotal in the pathogenesis of diastolic dysfunction. Yet, the role of fast (fMyBP-C) and slow (sMyBP-C) skeletal muscle MyBP-C remains to be elucidated. Herein, we aimed to characterize MyBP-C and its paralogs in the fast tibialis anterior (TA) muscle from adult and old mice. Immunoreactivity preparations showed that the relative abundance of the fMyBP-C paralog was greater in the TA of both adult and old, but no differences were noted between groups. We further found that the expression level of cardiac myosin binding protein-C (cMyBP-C), an important modulator of cardiac output, was lowered by age. Standard SDS-PAGE along with Pro-Q Diamond phosphoprotein staining did not identify age-related changes in phosphorylated MyBP-C proteins from TA and cardiac muscles; however, it revealed that MyBP-C paralogs in fast skeletal and cardiac muscle were highly phosphorylated. Mass spectrometry further identified glycogen phosphorylase, desmin, actin, troponin T, and myosin regulatory light chain 2 as phosphorylated myofilament proteins in both ages. MyBP-C protein-bound carbonyls were determined using anti-DNP immunostaining and found the carbonyl level of fMyBP-C, sMyBP-C, and cMyBP-C to be similar between old and adult animals. In summary, our data showed some differences regarding the MyBP-C paralog expression and identified an age-related reduction of cMyBP-C expression. Future studies are needed to elucidate which are the age-driven post-translational modifications in the MyBP-C paralogs.
(© 2022. The Author(s).)
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معلومات مُعتمدة: K07 AG072124 United States AG NIA NIH HHS; R56 AG067724 United States AG NIA NIH HHS
فهرسة مساهمة: Keywords: Aging; Muscle contractility; Phosphorylation
المشرفين على المادة: 0 (myosin-binding protein C)
EC 3.6.4.1 (Myosins)
تواريخ الأحداث: Date Created: 20221121 Date Completed: 20230201 Latest Revision: 20240407
رمز التحديث: 20240407
مُعرف محوري في PubMed: PMC9886727
DOI: 10.1007/s11357-022-00689-y
PMID: 36409445
قاعدة البيانات: MEDLINE
الوصف
تدمد:2509-2723
DOI:10.1007/s11357-022-00689-y