RGD Reference Report - Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. - Rat Genome Database

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Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis.

Authors: Farges, MC  Balcerzak, D  Fisher, BD  Attaix, D  Bechet, D  Ferrara, M  Baracos, VE 
Citation: Farges MC, etal., Am J Physiol Endocrinol Metab 2002 Feb;282(2):E326-35.
RGD ID: 631244
Pubmed: PMID:11788364   (View Abstract at PubMed)
DOI: DOI:10.1152/ajpendo.00345.2001   (Journal Full-text)

Rat gastrocnemius showed increased protein degradation (+75-115%) at 48 h after traumatic injury. Injured muscle showed increased cathepsin B activity (+327%) and mRNA encoding cathepsin B (+670%), cathepsin L (+298%), cathepsin H (+159%), and cathepsin C (+268%). In in situ hybridization, cathepsin B mRNA localized to the mononuclear cell infiltrate in injured muscle, and only background levels of hybridization were observed either over muscle cells in injured tissue or in uninjured muscle. Immunogold/electron microscopy showed specific staining for cathepsin B only in lysosome-like structures in cells of the mononuclear cell infiltrate in injured muscle. Muscle cells were uniformly negative in the immunocytochemistry. Matrix metalloproteinase-9 (granulocyte-macrophage gelatinase) mRNA and activity were not present in uninjured muscle but were expressed after trauma. There was no activation of the ATP-ubiquitin-proteasome-dependent proteolytic pathway in injured muscle, by contrast to diverse forms of muscle wasting where the activity of this system and the expression of genes encoding ubiquitin and proteasome elements rise. These results suggest that proteolytic systems of the muscle cells remain unstimulated after local injury and that lysosomal enzymes of the inflammatory infiltrated cells are likely to be the major participant in protein catabolism associated with local trauma.

RGD Manual Disease Annotations    Click to see Annotation Detail View
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
Contusions  ISOCtsb (Rattus norvegicus)631244; 631244mRNA more ...RGD 
Contusions  ISOCtsh (Rattus norvegicus)631244; 631244mRNA:increased expression:gastrocnemius (rat)RGD 
Contusions  ISOCtsl (Rattus norvegicus)631244; 631244mRNA more ...RGD 
Contusions  IEP 631244; 631244mRNA more ...RGD 
Contusions  IEP 631244mRNA:increased expression:gastrocnemius (rat)RGD 
Skeletal Muscle Injuries  ISOCtsb (Rattus norvegicus)631244; 631244protein:increased activity:gastrocnemius (rat)RGD 
Skeletal Muscle Injuries  IEP 631244protein:increased activity:gastrocnemius (rat)RGD 

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein catabolic process  IDA 631244; 631244; 631244 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
aminopeptidase activity  IDA 631244 RGD 
cysteine-type endopeptidase activity  NAS 631244 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Ctsb  (cathepsin B)
Ctsc  (cathepsin C)
Ctsh  (cathepsin H)
Ctsl  (cathepsin L)
Mmp9  (matrix metallopeptidase 9)

Genes (Mus musculus)
Ctsb  (cathepsin B)
Ctsh  (cathepsin H)
Ctsl  (cathepsin L)

Genes (Homo sapiens)
CTSB  (cathepsin B)
CTSH  (cathepsin H)
CTSL  (cathepsin L)


Additional Information