Home LiteratureArticle Details
PMID: 3013409 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Immunogold electron-microscopic localisation of calpain I in skeletal muscle of rats.

Cell and tissue research ·Vol. 244 ·No. 2 ·1986-00-00 ·Pages 265-70

Yoshimura N, Murachi T, Heath R, Kay J, Jasani B, Newman GR

Abstract

By using a double-affinity-purified first antibody and colloidal gold-conjugated second antibody, it is shown that calpain I (a cysteine proteinase activated by micromolar concentrations of Ca2+) has a predominant intracellular location in the I-band region of the extensor digitorum longus (EDL) muscle of the rat, but is not exclusively associated with the Z-line.

MeSH Terms
Animals Calpain/analysis,immunology Gold Male Muscles/enzymology,ultrastructure Rats Rats, Inbred Strains
Chemicals
Gold Calpain
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Yoshimura N
Murachi T
Heath R
Kay J
Jasani B
Newman G R
References (20)
20 references, click to expand
  1. Reconstitution of calpain I and calpain II from their subunits: interchangeability of the light subunits.
    Arch Biochem Biophys. 1984 Nov 1;234(2):639-45 PMID: 6093703
  2. Immunofluorescent localization of a Ca2+-dependent neutral protease in hamster muscle.
    Am J Physiol. 1981 May;240(5):E493-8 PMID: 6263102
  3. Immunocytochemical localization of a calcium-activated protease in skeletal muscle cells.
    Exp Cell Res. 1981 Dec;136(2):423-33 PMID: 6273198
  4. I-protein is localized at the junctional region of A-bands and I-bands of chicken fresh myofibrils.
    J Biochem. 1985 May;97(5):1323-8 PMID: 3897212
  5. A putative Ca2+-binding protein: structure of the light subunit of porcine calpain elucidated by molecular cloning and protein sequence analysis.
    Proc Natl Acad Sci U S A. 1985 Sep;82(18):6075-9 PMID: 2994060
  6. A NEUTRAL, CALCIUM-ACTIVATED PROTEINASE FROM THE SOLUBLE FRACTION OF RAT BRAIN.
    J Biol Chem. 1964 Jan;239:149-55 PMID: 14114836
  7. Non-deleterious dinitrophenyl (DNP) hapten labelling of antibody protein. Preparation and properties of some short-chain DNP imidoesters.
    J Immunol Methods. 1984 May 11;70(1):111-8 PMID: 6609207
  8. A simple post-embedding system for the rapid demonstration of tissue antigens under the electron microscope.
    Histochem J. 1983 Jun;15(6):543-55 PMID: 6409845
  9. Immunoelectronmicroscopy: immunogold and immunoperoxidase compared using a new post-embedding system.
    Med Lab Sci. 1984 Jul;41(3):238-45 PMID: 6384716
  10. Similarity and dissimilarity in subunit structures of calpains I and II from various sources as demonstrated by immunological cross-reactivity.
    J Biochem. 1983 Dec;94(6):2055-61 PMID: 6323387
  11. Comparison of tryptic peptides from the heavy and light subunits of calpain I and calpain II by high performance liquid chromatography.
    J Biochem. 1984 Nov;96(5):1531-7 PMID: 6098578
  12. Comparison of low and high calcium requiring forms of the calcium-activated neutral protease (CANP) from rabbit skeletal muscle.
    J Biochem. 1984 Jun;95(6):1661-70 PMID: 6088474
  13. Intracellular localization of two distinct Ca2+-proteases (calpain I and calpain II) as demonstrated by using discriminative antibodies.
    J Biol Chem. 1984 Aug 10;259(15):9847-52 PMID: 6086654
  14. Comparison of two calcium-dependent proteinases from bovine heart.
    Biochim Biophys Acta. 1984 Aug 14;788(3):348-55 PMID: 6087912
  15. A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium-requiring form of the protease.
    Biochim Biophys Acta. 1981 May 14;659(1):48-61 PMID: 6264963
  16. Two distinct Ca2+ proteases (calpain I and calpain II) purified concurrently by the same method from rat kidney.
    J Biol Chem. 1983 Jul 25;258(14):8883-9 PMID: 6306001
  17. Evidence for two structurally different forms of skeletal muscle Ca2+-activated protease.
    J Biol Chem. 1982 Nov 10;257(21):12471-4 PMID: 6290467
  18. Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?
    Nature. 1984 Dec 6-12;312(5994):566-70 PMID: 6095110
  19. Calcium-activated neutral protease. Its localization in the myofibril, especially at the Z-band.
    J Biochem. 1980 Jan;87(1):343-6 PMID: 6766927
  20. Large-scale purification of porcine calpain I and calpain II and comparison of proteolytic fragments of their subunits.
    J Biochem. 1984 Jun;95(6):1759-66 PMID: 6088477
Article Info
Journal
Cell and tissue research
Abbr.
Cell Tissue Res
ISSN
0302-766X
DOI
10.1007/BF00219201
Published
1986-00-00
Pages
265-70
Language
English
Region
Germany
NLM ID
0417625
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00219201 View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2