Document Detail

A long-range ordered structure in mitochondrial cristae revealed by a pathological structural modification.
MedLine Citation:
PMID:  3404005     Owner:  NLM     Status:  MEDLINE    
An experimentally imposed 6-hr local ischemia in the anterior wall of the left ventricle in dog hearts leads to a structural modification of the mitochondria in the posterior wall with the cristae revealing a zig-zag pattern when viewed in cross sections. This pattern was found to reveal a change in the distribution of crista mass with an increase of mass at circumscribed regions in each crista membrane and a reduction of mass from the surrounding region in each crista membrane. The accumulation of mass contributed to the elevations that caused the zig-zag pattern. These elevations were distributed according to a tetragonal pattern with a periodicity of 850 A. The tetragonal pattern contributed by one crista membrane was translocated halfway along the diagonals of the tetrameric pattern of the other crista membrane within each crista. The change in mass distribution reveals differences in the strength of bonds that account for binding of the proteins to the cristae with strong bonds in the elevated regions, while enzymes less firmly bound are located in the surrounding region. The respiratory chain enzymes will then be located in the elevated regions and the soluble enzymes including the tricarboxylic acid cycle enzymes will be located in the surrounding region. The tissue in the posterior wall was functionally impaired and normal function was restored when substrate for oxidative phosphorylation was added to the blood perfusing the tissue. It is concluded that the functional impairment is a consequence of a partial breakdown of the structural organization of the tricarboxylic acid cycle enzymes. The discovery of a long-range structural order involving the entire cristae reveals that the enzymes of the multienzyme systems as well as those systems in the cristae are structurally highly organized and it excludes that the enzymes are randomly mixed and highly mobile.
F S Sjöstrand; B S Allen; F Beyersdorf; G Buckberg
Related Documents :
12077455 - Crystallization of the fad-independent acetolactate synthase of klebsiella pneumoniae.
21992235 - The thermal and enzymatic taxifolin-alphitonin rearrangement.
14687575 - Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel a...
10924115 - A closer look at the active site of gamma-class carbonic anhydrases: high-resolution cr...
22112955 - Direct and efficient ethanol production from high-yielding rice using a saccharomyces c...
19489025 - Metabolomics for biotransformations: intracellular redox cofactor analysis and enzyme k...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of ultrastructure and molecular structure research     Volume:  99     ISSN:  0889-1605     ISO Abbreviation:  J. Ultrastruct. Mol. Struct. Res.     Publication Date:  1988 Apr 
Date Detail:
Created Date:  1988-09-15     Completed Date:  1988-09-15     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  8612238     Medline TA:  J Ultrastruct Mol Struct Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1-17     Citation Subset:  IM    
Department of Biology, University of California, Los Angeles 90024-1606.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Coronary Disease / pathology*
Microscopy, Electron
Mitochondria, Heart / ultrastructure*

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Structure analysis of fibrinogen by electron microscopy and image processing.
Next Document:  Phosphorus imaging of the 7-S ribonucleoprotein particle.