Meat quality is a term used to describe a range of attributes of meat. Consumer research suggests that tenderness is a very important element of eating quality and that variations in tenderness affect the decision to repurchase. The present paper highlights recent information on the factors that affect tenderness. While the precise aetiology is not fully understood, a number of factors have been shown to affect tenderness. Of these factors, postmortem factors, particularly temperature, sarcomere length and proteolysis, which affect the conversion of muscle to meat, appear most important. However, it is now becoming clear that variation in other factors such as the muscle fibre type composition and the buffering capacity of the muscle together with the breed and nutritional status of the animals may also contribute to the observed variation in meat tenderness.

Tissue biomarker scoring by pathologists is central to defining the appropriate therapy for patients with cancer. Yet, inter-pathologist variability in the interpretation of ambiguous cases can affect diagnostic accuracy. Modern artificial intelligence methods such as deep learning have the potential to supplement pathologist expertise to ensure constant diagnostic accuracy. We developed a computational approach based on deep learning that automatically scores HER2, a biomarker that defines patient eligibility for anti-HER2 targeted therapies in breast cancer. In a cohort of 71 breast tumour resection samples, automated scoring showed a concordance of 83% with a pathologist. The twelve discordant cases were then independently reviewed, leading to a modification of diagnosis from initial pathologist assessment for eight cases. Diagnostic discordance was found to be largely caused by perceptual differences in assessing HER2 expression due to high HER2 staining heterogeneity. This study provides evidence that deep learning aided diagnosis can facilitate clinical decision making in breast cancer by identifying cases at high risk of misdiagnosis.

. Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. Am J Physiol Endocrinol Metab 282: E326-E335, 2002; 10.1152/ajpendo.00345.2001.-Rat gastrocnemius showed increased protein degradation (ϩ75-115%) at 48 h after traumatic injury. Injured muscle showed increased cathepsin B activity (ϩ327%) and mRNA encoding cathepsin B (ϩ670%), cathepsin L (ϩ298%), cathepsin H (ϩ159%), and cathepsin C (ϩ268%). 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-ubiquitinproteasome-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. injury; protein degradation IN A MODEL OF BLUNT TRAUMA TO MUSCLE, we demonstrated a period of degeneration lasting ϳ3 days, characterized by gross disruption of muscle cells, hemorrhage, inflammation, invasion of the injured site by mononuclear cells, and a 26% loss of previously existing muscle protein (12). A large increase in the process of protein catabolism occurs in injured muscle; however, it is not known which of the several distinct intracellular pro-

Matrix metalloproteinases (MMP) responsible for degradation of connective tissue are found in most tissues. The MMP are regulated at the levels of transcription, zymogen activation by plasmin or membrane-type- (MT) MMP, and control of enzyme activity by tissue inhibitors of metalloproteinases (TIMP). Whole bovine skeletal muscle showed multiple MMP activities on gelatin zymography and also expressed mRNA encoding MMP-1, -2, -9, -14, and -16, tissue inhibitors of metalloproteinase (TIMP)-1, -2, and -3 and plasminogen activator and its receptor. Purified intramuscular fibroblasts and myogenic cell culture derived from satellite cells expressed most or all of these elements. Statistical analysis (n = 35) revealed a strong positive correlation among the mRNA levels of several elements of the MMP system, including MMP-2, MMP-14, TIMP-1, -2, and -3 (r = 0.614 to 0.930, P < 0.0001). Our results provide an extensive profile of an extracellular proteolytic cascade involving MMP in skeletal muscle and suggest that 1) the activation cascades of muscle MMP may be initiated by both plasmin and membrane-type MMP; 2) a group of genes involved in the same "arm" of zymogen activation are coexpressed in this tissue; and 3) skeletal muscle cells, in addition to the intramuscular fibroblasts, express an extensive complement of MMP and related proteins.

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